Structured Review

Santa Cruz Biotechnology anti vegf
Effect of cyclin A1 expression on tumor invasion is associated with its effect on <t>VEGF</t> expression in MCF-7 cells. (A) Evaluation of cyclin A1 and VEGF expression in metastatic lesions from lymph nodes from patients with breast cancer metastasis using immunohistochemical analysis. Representative pictures show the cancer cells are strongly positive to cyclin A1 and VEGF expression. Upper panels represent cores at 20x magnificantion and lower panels represent the higher magnification (40x) of the selected areas. (B) MCF-7 cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP vectors were applied on the Matrigel-coated invasion chamber and were assessed after 48 or 72 hours. Data in graphs are the mean ± SD represents two independent experiments, each performed in duplicates. P value is indicated. (C) MDA-MB-231 cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP were applied on the Matrigel-coated invasion chamber and were analyzed after 48 or 72 hours. Data in graphs are the mean of two independent experiments, each performed in duplicate, p=0.002 for 48 h and p=0.02 for 72 h. (D) Cell cycle distribution of the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Data in graphs are the mean ± SD represents three independent experiments from flow cytometry analysis. The percentage of cells at onset of each cell cycle phase is indicated. (E) Western blot analysis shows the levels of cyclin D1 and <t>CDK1</t> protein expression in the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. (F) Representative picture shows the VEGF mRNA expression in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP (upper panel). Quantification of VEGF mRNA level in the samples is indicated. P value is shown (lower panel). (G) ELISA assay of VEGF secretion in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Mean ± SD represents three independent experiments (lower panel). Breast cancer cell lines used for these studies are T47D, MCF-7 and MDA-MB231 as indicated.
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1) Product Images from "Cyclin A1 Modulates the Expression of Vascular Endothelial Growth Factor and Promotes Hormone-Dependent Growth and Angiogenesis of Breast Cancer"

Article Title: Cyclin A1 Modulates the Expression of Vascular Endothelial Growth Factor and Promotes Hormone-Dependent Growth and Angiogenesis of Breast Cancer

Journal: PLoS ONE

doi: 10.1371/journal.pone.0072210

Effect of cyclin A1 expression on tumor invasion is associated with its effect on VEGF expression in MCF-7 cells. (A) Evaluation of cyclin A1 and VEGF expression in metastatic lesions from lymph nodes from patients with breast cancer metastasis using immunohistochemical analysis. Representative pictures show the cancer cells are strongly positive to cyclin A1 and VEGF expression. Upper panels represent cores at 20x magnificantion and lower panels represent the higher magnification (40x) of the selected areas. (B) MCF-7 cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP vectors were applied on the Matrigel-coated invasion chamber and were assessed after 48 or 72 hours. Data in graphs are the mean ± SD represents two independent experiments, each performed in duplicates. P value is indicated. (C) MDA-MB-231 cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP were applied on the Matrigel-coated invasion chamber and were analyzed after 48 or 72 hours. Data in graphs are the mean of two independent experiments, each performed in duplicate, p=0.002 for 48 h and p=0.02 for 72 h. (D) Cell cycle distribution of the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Data in graphs are the mean ± SD represents three independent experiments from flow cytometry analysis. The percentage of cells at onset of each cell cycle phase is indicated. (E) Western blot analysis shows the levels of cyclin D1 and CDK1 protein expression in the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. (F) Representative picture shows the VEGF mRNA expression in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP (upper panel). Quantification of VEGF mRNA level in the samples is indicated. P value is shown (lower panel). (G) ELISA assay of VEGF secretion in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Mean ± SD represents three independent experiments (lower panel). Breast cancer cell lines used for these studies are T47D, MCF-7 and MDA-MB231 as indicated.
Figure Legend Snippet: Effect of cyclin A1 expression on tumor invasion is associated with its effect on VEGF expression in MCF-7 cells. (A) Evaluation of cyclin A1 and VEGF expression in metastatic lesions from lymph nodes from patients with breast cancer metastasis using immunohistochemical analysis. Representative pictures show the cancer cells are strongly positive to cyclin A1 and VEGF expression. Upper panels represent cores at 20x magnificantion and lower panels represent the higher magnification (40x) of the selected areas. (B) MCF-7 cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP vectors were applied on the Matrigel-coated invasion chamber and were assessed after 48 or 72 hours. Data in graphs are the mean ± SD represents two independent experiments, each performed in duplicates. P value is indicated. (C) MDA-MB-231 cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP were applied on the Matrigel-coated invasion chamber and were analyzed after 48 or 72 hours. Data in graphs are the mean of two independent experiments, each performed in duplicate, p=0.002 for 48 h and p=0.02 for 72 h. (D) Cell cycle distribution of the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Data in graphs are the mean ± SD represents three independent experiments from flow cytometry analysis. The percentage of cells at onset of each cell cycle phase is indicated. (E) Western blot analysis shows the levels of cyclin D1 and CDK1 protein expression in the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. (F) Representative picture shows the VEGF mRNA expression in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP (upper panel). Quantification of VEGF mRNA level in the samples is indicated. P value is shown (lower panel). (G) ELISA assay of VEGF secretion in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Mean ± SD represents three independent experiments (lower panel). Breast cancer cell lines used for these studies are T47D, MCF-7 and MDA-MB231 as indicated.

Techniques Used: Expressing, Immunohistochemistry, Transfection, Multiple Displacement Amplification, Flow Cytometry, Cytometry, Western Blot, Enzyme-linked Immunosorbent Assay

Long-term effect of elevated level of cyclin A1 on growth and angiogenesis phenotype of xenograft tumors in mice. MCF-7 cells stable expressing pcDNA–cyclin A1 or pcDNA vectors were subcutaneous implanted into female nude mice with E2 supplementation. (A, B) Representative microphotographs of xenograft tumor sections stained with Haematoxylin and Eosin are shown. (C, D) Representative pictures show the xenograft tumors stained with antibody against human CD31, the CD31 positive vessels are indicated. The control tumor “control-pcDNA” and cyclin A1 expressing tumors “cyclin A1-pcDNA” are indicated. (E) Growth curves of the two groups of xenograft tumors are indicated. The time is indicated in x-axis and tumor volume in mm 3 is indicated in y-axis. (F) Quantification of the tumor vascularizations in cyclin A1 expressing xenograft tumors “cyclin A1-pcDNA” and in control xenograft tumors “control-pcDNA”. The numbers of CD31-positive blood vessels in the central vs. edge regions of the tumor areas are shown. P values are indicated. Mean ± SD represents three independent experiments. (G–N) Xenograft tumors from “cyclin A1-pcDNA” and “control-pcDNA” groups were immunostained with antibodies against VEGF, VEGFR1, ER-α and Ki67. The representative microphotographs are shown.
Figure Legend Snippet: Long-term effect of elevated level of cyclin A1 on growth and angiogenesis phenotype of xenograft tumors in mice. MCF-7 cells stable expressing pcDNA–cyclin A1 or pcDNA vectors were subcutaneous implanted into female nude mice with E2 supplementation. (A, B) Representative microphotographs of xenograft tumor sections stained with Haematoxylin and Eosin are shown. (C, D) Representative pictures show the xenograft tumors stained with antibody against human CD31, the CD31 positive vessels are indicated. The control tumor “control-pcDNA” and cyclin A1 expressing tumors “cyclin A1-pcDNA” are indicated. (E) Growth curves of the two groups of xenograft tumors are indicated. The time is indicated in x-axis and tumor volume in mm 3 is indicated in y-axis. (F) Quantification of the tumor vascularizations in cyclin A1 expressing xenograft tumors “cyclin A1-pcDNA” and in control xenograft tumors “control-pcDNA”. The numbers of CD31-positive blood vessels in the central vs. edge regions of the tumor areas are shown. P values are indicated. Mean ± SD represents three independent experiments. (G–N) Xenograft tumors from “cyclin A1-pcDNA” and “control-pcDNA” groups were immunostained with antibodies against VEGF, VEGFR1, ER-α and Ki67. The representative microphotographs are shown.

Techniques Used: Mouse Assay, Expressing, Staining

2) Product Images from "MicroRNA-15a-5p induces pulmonary artery smooth muscle cell apoptosis in a pulmonary arterial hypertension model via the VEGF/p38/MMP-2 signaling pathway"

Article Title: MicroRNA-15a-5p induces pulmonary artery smooth muscle cell apoptosis in a pulmonary arterial hypertension model via the VEGF/p38/MMP-2 signaling pathway

Journal: International Journal of Molecular Medicine

doi: 10.3892/ijmm.2019.4434

Inhibition of VEGF affected the VEGF/p38/MMP-2 signaling pathway in PASMCs from rats with monocrotaline-induced pulmonary arterial hypertension by attenuating the effects of miR-15a-5p inhibition. (A) Expression of VEGF, p-p38, MMP-2, Bax and Bcl-2 proteins detected using western blot analysis. Quantification of (B) VEGF, (C) p-p38, (D) MMP-2, (E) Bax and (F) Bcl-2 protein expression. ## P
Figure Legend Snippet: Inhibition of VEGF affected the VEGF/p38/MMP-2 signaling pathway in PASMCs from rats with monocrotaline-induced pulmonary arterial hypertension by attenuating the effects of miR-15a-5p inhibition. (A) Expression of VEGF, p-p38, MMP-2, Bax and Bcl-2 proteins detected using western blot analysis. Quantification of (B) VEGF, (C) p-p38, (D) MMP-2, (E) Bax and (F) Bcl-2 protein expression. ## P

Techniques Used: Inhibition, Expressing, Western Blot

Upregulation of VEGF affected the VEGF/p38/MMP-2 signaling pathway in PASMCs from rats with monocrotaline-induced pulmonary arterial hypertension by the effects of miR-15a-5p. (A) Results of the protein expression of VEGF, p38, MMP-2, Bax and Bcl-2 measured using western blot analysis. Protein expression of (B) VEGF, (C) p-p38, (D) MMP-2, (E) Bax and (F) Bcl-2. ## P
Figure Legend Snippet: Upregulation of VEGF affected the VEGF/p38/MMP-2 signaling pathway in PASMCs from rats with monocrotaline-induced pulmonary arterial hypertension by the effects of miR-15a-5p. (A) Results of the protein expression of VEGF, p38, MMP-2, Bax and Bcl-2 measured using western blot analysis. Protein expression of (B) VEGF, (C) p-p38, (D) MMP-2, (E) Bax and (F) Bcl-2. ## P

Techniques Used: Expressing, Western Blot

3) Product Images from "β-arrestin1 over-expression is associated with an unfavorable prognosis in lung adenocarcinomas and correlated with vascular endothelial growth factor"

Article Title: β-arrestin1 over-expression is associated with an unfavorable prognosis in lung adenocarcinomas and correlated with vascular endothelial growth factor

Journal: International Journal of Clinical and Experimental Pathology

doi:

Intratumoral vascular endothelial growth factor (VEGF) in relation to β-arrestin1 protein immunoreactivity. Mann-Whitney U test demonstrated that tumors with β-arrestin1 nuclear positive expression showed significantly higher intratumoral
Figure Legend Snippet: Intratumoral vascular endothelial growth factor (VEGF) in relation to β-arrestin1 protein immunoreactivity. Mann-Whitney U test demonstrated that tumors with β-arrestin1 nuclear positive expression showed significantly higher intratumoral

Techniques Used: MANN-WHITNEY, Expressing

Kaplan-Meier curves of overall survival and progression-free survival stratified according to the β-arrestin1 (A, B) and VEGF expression (C, D).
Figure Legend Snippet: Kaplan-Meier curves of overall survival and progression-free survival stratified according to the β-arrestin1 (A, B) and VEGF expression (C, D).

Techniques Used: Expressing

4) Product Images from "Sarpogrelate hydrochloride ameliorates diabetic nephropathy associated with inhibition of macrophage activity and inflammatory reaction in db/db mice"

Article Title: Sarpogrelate hydrochloride ameliorates diabetic nephropathy associated with inhibition of macrophage activity and inflammatory reaction in db/db mice

Journal: PLoS ONE

doi: 10.1371/journal.pone.0179221

Western blot analysis of the renal cortex after treatment with sarpogrelate hydrochloride. The renal expression of nephrin and VEGF was analyzed by Western blotting (A). The relative expression of nephrin (B) and VEGF (C) were analyzed by ImageJ software. The expression of renal Cldn1 and Sirt1 was analyzed by IHC (D) and western blotting (E).The difference renal nephrin and VEGF levels among four groups. NC, normal mice group; NC+SH, normal mice with sarpogrelate hydrochloride treatment group; DB, diabetic mice group; DB+SH, diabetic mice with sarpogrelate hydrochloride treatment group. Values shown are mean ± SEM. * p
Figure Legend Snippet: Western blot analysis of the renal cortex after treatment with sarpogrelate hydrochloride. The renal expression of nephrin and VEGF was analyzed by Western blotting (A). The relative expression of nephrin (B) and VEGF (C) were analyzed by ImageJ software. The expression of renal Cldn1 and Sirt1 was analyzed by IHC (D) and western blotting (E).The difference renal nephrin and VEGF levels among four groups. NC, normal mice group; NC+SH, normal mice with sarpogrelate hydrochloride treatment group; DB, diabetic mice group; DB+SH, diabetic mice with sarpogrelate hydrochloride treatment group. Values shown are mean ± SEM. * p

Techniques Used: Western Blot, Expressing, Software, Immunohistochemistry, Mouse Assay

5) Product Images from "Up-Regulation of pVHL along with Down-Regulation of HIF-1? by NDRG2 Expression Attenuates Proliferation and Invasion in Renal Cancer Cells"

Article Title: Up-Regulation of pVHL along with Down-Regulation of HIF-1? by NDRG2 Expression Attenuates Proliferation and Invasion in Renal Cancer Cells

Journal: PLoS ONE

doi: 10.1371/journal.pone.0084127

Proposed model that NDRG2 exerts its anti-tumor effect. The NDRG2 caused down-regulation of HIF-1α and VEGF was partly due to up-regulation of the tumor suppressor pVHL. It could not be excluded that NDRG2 may also regulate HIF-1α expression and consequent VEGF changes independent of pVHL.
Figure Legend Snippet: Proposed model that NDRG2 exerts its anti-tumor effect. The NDRG2 caused down-regulation of HIF-1α and VEGF was partly due to up-regulation of the tumor suppressor pVHL. It could not be excluded that NDRG2 may also regulate HIF-1α expression and consequent VEGF changes independent of pVHL.

Techniques Used: Expressing

Effect of NDRG2 on the expression of pVHL, HIF-1α and VEGF under normoxia or hypoxia. (A) 786-O, Ad-LacZ-786-O and Ad-NDRG2-786-O cells were incubated under normoxia and hypoxia for 24 h. After incubation, the cells were analyzed by western blot assay. β-actin protein levels were used as a loading control. (B) After infection of 786-O cells with 40 MOI Ad-NDRG2 under normoxia for 24 h, protein levels of NDRG2, pVHL, HIF-1α and VEGF in the cells were measured using immunofluorescence assay (400× magnification).
Figure Legend Snippet: Effect of NDRG2 on the expression of pVHL, HIF-1α and VEGF under normoxia or hypoxia. (A) 786-O, Ad-LacZ-786-O and Ad-NDRG2-786-O cells were incubated under normoxia and hypoxia for 24 h. After incubation, the cells were analyzed by western blot assay. β-actin protein levels were used as a loading control. (B) After infection of 786-O cells with 40 MOI Ad-NDRG2 under normoxia for 24 h, protein levels of NDRG2, pVHL, HIF-1α and VEGF in the cells were measured using immunofluorescence assay (400× magnification).

Techniques Used: Expressing, Incubation, Western Blot, Infection, Immunofluorescence

Effects of Ad-NDRG2 intratumoral injections on NDRG2, pVHL, HIF-1α and VEGF expression of 786-O cell xenografts in mice. (A) Intratumoral expressions of NDRG2, pVHL, HIF-1a and VEGF were assessed by Immunohistochemistry (200× magnification) on paraffin-embedded 786-O cell tumor sections. Representative images are shown. (B) Integrated optical density (IOD) values of NDRG2, pVHL, HIF-1α and VEGF protein expression of the tumors were evaluated. ImagePro Plus software was utilized to analyze the IOD values of the positive areas of immunohistochemical staining, and the resulting histograms are shown. Statistical analysis was carried out using one-way ANOVA. The results were shown as the mean ± SD. ***P
Figure Legend Snippet: Effects of Ad-NDRG2 intratumoral injections on NDRG2, pVHL, HIF-1α and VEGF expression of 786-O cell xenografts in mice. (A) Intratumoral expressions of NDRG2, pVHL, HIF-1a and VEGF were assessed by Immunohistochemistry (200× magnification) on paraffin-embedded 786-O cell tumor sections. Representative images are shown. (B) Integrated optical density (IOD) values of NDRG2, pVHL, HIF-1α and VEGF protein expression of the tumors were evaluated. ImagePro Plus software was utilized to analyze the IOD values of the positive areas of immunohistochemical staining, and the resulting histograms are shown. Statistical analysis was carried out using one-way ANOVA. The results were shown as the mean ± SD. ***P

Techniques Used: Expressing, Mouse Assay, Immunohistochemistry, Software, Staining

6) Product Images from "Anti-myeloma Effects of Icariin Are Mediated Through the Attenuation of JAK/STAT3-Dependent Signaling Cascade"

Article Title: Anti-myeloma Effects of Icariin Are Mediated Through the Attenuation of JAK/STAT3-Dependent Signaling Cascade

Journal: Frontiers in Pharmacology

doi: 10.3389/fphar.2018.00531

Icariin induces apoptosis in U266 cells. (A) U266 cells (1 × 10 6 cells/well) were treated with various indicated concentrations for 24 h. Then 10 μg proteins of those whole cell extracts was loaded on 15% SDS–PAGE gel followed by western blot analysis against Bcl-2, Bcl-xl, Survivin, IAP-1, IAP-2, COX-2, VEGF, and MMP-9. (B) U266 cells (1 × 10 6 cells/well) were treated with various indicated concentrations for 8 h. Total RNA was extracted and equal amounts were prepared to probe for Bcl-2, Bcl-xl, and Survivin by RT-PCR. (C) U266 cells (1 × 10 6 cells/well) were treated with various indicated concentrations for 24 h. Equal amounts of whole cell lysates were prepared and performed to detect caspase-3 and PARP by western blotting. (D) After Icariin treatment (0, 50, 100 μM for 24 h), cells were washed with PBS and digested with RNase A for 1 h, then stained with propidium iodide and analyzed cell for cycle division using flow cytometry. (E) After U266 cells (1 × 10 6 cells/well) were incubated with 100 μM icariin for 24 h, stained with Annexin V-FITC for 15 min and add PI then were analyzed by flow cytometry. (F) U266 cells (1 × 10 4 cells/well) were incubated with icariin (0, 50, 100 μM) for different indicated time periods. After incubation, difference in degree of cell proliferation was analyzed by MTT assay. (G) U266 cells (1 × 10 4 cells/well) and PBMC cells (1 × 10 4 cells/well) were incubated with 100 μM icariin for 24 h. The results shown are representative of three independent experiments.
Figure Legend Snippet: Icariin induces apoptosis in U266 cells. (A) U266 cells (1 × 10 6 cells/well) were treated with various indicated concentrations for 24 h. Then 10 μg proteins of those whole cell extracts was loaded on 15% SDS–PAGE gel followed by western blot analysis against Bcl-2, Bcl-xl, Survivin, IAP-1, IAP-2, COX-2, VEGF, and MMP-9. (B) U266 cells (1 × 10 6 cells/well) were treated with various indicated concentrations for 8 h. Total RNA was extracted and equal amounts were prepared to probe for Bcl-2, Bcl-xl, and Survivin by RT-PCR. (C) U266 cells (1 × 10 6 cells/well) were treated with various indicated concentrations for 24 h. Equal amounts of whole cell lysates were prepared and performed to detect caspase-3 and PARP by western blotting. (D) After Icariin treatment (0, 50, 100 μM for 24 h), cells were washed with PBS and digested with RNase A for 1 h, then stained with propidium iodide and analyzed cell for cycle division using flow cytometry. (E) After U266 cells (1 × 10 6 cells/well) were incubated with 100 μM icariin for 24 h, stained with Annexin V-FITC for 15 min and add PI then were analyzed by flow cytometry. (F) U266 cells (1 × 10 4 cells/well) were incubated with icariin (0, 50, 100 μM) for different indicated time periods. After incubation, difference in degree of cell proliferation was analyzed by MTT assay. (G) U266 cells (1 × 10 4 cells/well) and PBMC cells (1 × 10 4 cells/well) were incubated with 100 μM icariin for 24 h. The results shown are representative of three independent experiments.

Techniques Used: SDS Page, Western Blot, Reverse Transcription Polymerase Chain Reaction, Staining, Flow Cytometry, Cytometry, Incubation, MTT Assay

Icariin and Bortezomib induce apoptosis by caspase-3 and PARP in U266 cells. (A) To confirm the synergistic effect between icariin and bortezomib on cell cycle, U266 cells (1 × 10 6 cells/well) were incubated with icariin (10 μM) and bortezomib (1 nM) for 24h then treated with RNase A for 1h. After staining with propidium iodide, cells were analyzed by flow cytometry. (B) U266 cells were treated with icariin and bortezomib for 24 h. Cells were fixed and stained with TUNEL assay reagent, then analyzed with a flow cytometer. (C,D) We confirm the synergistic effect for induced apoptosis by western blot analysis. U266 cells (1 × 10 6 cells/well) were treated with 10 μM icariin and 1 nM bortezomib for 24 h. Same amounts of whole cell lysates were prepared and probed using Bcl-2, Bcl-xl, Survivin, IAP-1, IAP-2, COX-2, VEGF, MMP-9, caspase-3, and PARP antibodies then analyzed by Western blotting. (E) To confirm the anti-cancer effect of icariin and bortezomib, U266 cells (1 × 10 6 cells/well) were incubated with icariin (10 μM) and bortezomib (1 nM) for 24h then proteins were resolved on SDS–PAGE and probed against p21 antibody. (F) U266 cells were transfected with STAT3 siRNA or scramble siRNA for 48 h, then 100 μM of icariin were treated for 24 h. The Whole cell lysates were prepared and 15 μg proteins were resolved on SDS–PAGE and probed against PARP antibody. b-actin was used as internal controls. (G) U266 cells were transfected with STAT3 siRNA or scramble siRNA for 48 h, then 100 μM of icariin were treated for 24 h. Then cell viability was analyzed by MTT assay. The results shown are representative of three independent experiments.
Figure Legend Snippet: Icariin and Bortezomib induce apoptosis by caspase-3 and PARP in U266 cells. (A) To confirm the synergistic effect between icariin and bortezomib on cell cycle, U266 cells (1 × 10 6 cells/well) were incubated with icariin (10 μM) and bortezomib (1 nM) for 24h then treated with RNase A for 1h. After staining with propidium iodide, cells were analyzed by flow cytometry. (B) U266 cells were treated with icariin and bortezomib for 24 h. Cells were fixed and stained with TUNEL assay reagent, then analyzed with a flow cytometer. (C,D) We confirm the synergistic effect for induced apoptosis by western blot analysis. U266 cells (1 × 10 6 cells/well) were treated with 10 μM icariin and 1 nM bortezomib for 24 h. Same amounts of whole cell lysates were prepared and probed using Bcl-2, Bcl-xl, Survivin, IAP-1, IAP-2, COX-2, VEGF, MMP-9, caspase-3, and PARP antibodies then analyzed by Western blotting. (E) To confirm the anti-cancer effect of icariin and bortezomib, U266 cells (1 × 10 6 cells/well) were incubated with icariin (10 μM) and bortezomib (1 nM) for 24h then proteins were resolved on SDS–PAGE and probed against p21 antibody. (F) U266 cells were transfected with STAT3 siRNA or scramble siRNA for 48 h, then 100 μM of icariin were treated for 24 h. The Whole cell lysates were prepared and 15 μg proteins were resolved on SDS–PAGE and probed against PARP antibody. b-actin was used as internal controls. (G) U266 cells were transfected with STAT3 siRNA or scramble siRNA for 48 h, then 100 μM of icariin were treated for 24 h. Then cell viability was analyzed by MTT assay. The results shown are representative of three independent experiments.

Techniques Used: Incubation, Staining, Flow Cytometry, Cytometry, TUNEL Assay, Western Blot, SDS Page, Transfection, MTT Assay

7) Product Images from "Activation of STAT3 in Human Gastric Cancer Cells via Interleukin (IL)-6-Type Cytokine Signaling Correlates with Clinical Implications"

Article Title: Activation of STAT3 in Human Gastric Cancer Cells via Interleukin (IL)-6-Type Cytokine Signaling Correlates with Clinical Implications

Journal: PLoS ONE

doi: 10.1371/journal.pone.0075788

Western blot analysis of protein expression of IL-6, p-STAT3, survivin, STAT3, and VEGF. Protein levels of IL-6, Survivin, p-STAT3, STAT3, and VEGF in normal gastric and tumor tissue were determined using western blotting. Beta-actin was a loading control. Relative protein expression of IL-6 (A), VEGF (B), surviving (C), p-STAT3 (D) was normalized to of the corresponding beta-actin level. Positive immunoreactive bands were quantified densitometrically and expressed as IL-6, Survivin, p-STAT3, STAT3, and VEGF in optical density units, respectively. * P
Figure Legend Snippet: Western blot analysis of protein expression of IL-6, p-STAT3, survivin, STAT3, and VEGF. Protein levels of IL-6, Survivin, p-STAT3, STAT3, and VEGF in normal gastric and tumor tissue were determined using western blotting. Beta-actin was a loading control. Relative protein expression of IL-6 (A), VEGF (B), surviving (C), p-STAT3 (D) was normalized to of the corresponding beta-actin level. Positive immunoreactive bands were quantified densitometrically and expressed as IL-6, Survivin, p-STAT3, STAT3, and VEGF in optical density units, respectively. * P

Techniques Used: Western Blot, Expressing

Expression of STAT3 in human gastric cancer tissues. The expression and localization of STAT3, IL-6, VEGF, and survivin in gastric cancer cells were determined using immunohistochemical staining. There was weak or negative expression of STAT3 in adjacent normal mucosa. However, there was strong expression of phosphorylated STAT3 in gastric cancer tissues. The STAT3 staining was mainly localized in the nuclei of tumor epithelial cells, which was indicated by numerous yellowish granules. STAT3 overexpression was associated with with increased expression of IL-6, surviving, and VEGF as well as with increased vessel density (Original magnification of A1-A3 and B1-B3, ×400; A4 and B4, ×200)..
Figure Legend Snippet: Expression of STAT3 in human gastric cancer tissues. The expression and localization of STAT3, IL-6, VEGF, and survivin in gastric cancer cells were determined using immunohistochemical staining. There was weak or negative expression of STAT3 in adjacent normal mucosa. However, there was strong expression of phosphorylated STAT3 in gastric cancer tissues. The STAT3 staining was mainly localized in the nuclei of tumor epithelial cells, which was indicated by numerous yellowish granules. STAT3 overexpression was associated with with increased expression of IL-6, surviving, and VEGF as well as with increased vessel density (Original magnification of A1-A3 and B1-B3, ×400; A4 and B4, ×200)..

Techniques Used: Expressing, Immunohistochemistry, Staining, Over Expression

8) Product Images from "Activity of Porophyllum ruderale leaf extract and 670-nm InGaP laser during burns repair in rats"

Article Title: Activity of Porophyllum ruderale leaf extract and 670-nm InGaP laser during burns repair in rats

Journal: BMC Complementary and Alternative Medicine

doi: 10.1186/s12906-015-0805-2

Immunoblot analysis of the expression of TGF-β1 and VEGF after 7, 14 and 21 days of the experiment in second-degree burns in rats in different treatment groups. C: untreated control; L: treated with 670-nm InGaP laser; P: treated with the Porophyllum ruderale extract PL: treated with the P. ruderale extract and 670-nm InGaP laser. Typical blots are shown above average densitometry results. Values are the mean and standard deviation of each group and were compared by ANOVA with Tukey’s post-test (* p
Figure Legend Snippet: Immunoblot analysis of the expression of TGF-β1 and VEGF after 7, 14 and 21 days of the experiment in second-degree burns in rats in different treatment groups. C: untreated control; L: treated with 670-nm InGaP laser; P: treated with the Porophyllum ruderale extract PL: treated with the P. ruderale extract and 670-nm InGaP laser. Typical blots are shown above average densitometry results. Values are the mean and standard deviation of each group and were compared by ANOVA with Tukey’s post-test (* p

Techniques Used: Expressing, Standard Deviation

9) Product Images from "Identification of telocytes in skeletal muscle interstitium: implication for muscle regeneration"

Article Title: Identification of telocytes in skeletal muscle interstitium: implication for muscle regeneration

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/j.1582-4934.2011.01330.x

Human skeletal muscle, immunohistochemistry with HRP conjugated antibodies on cryosections (A, B, E, H) and immunofluorescence-confocal microscopy (C, D). TCs are located within interstitium, and express c-kit (A–D), caveolin-1 (E), vimentin (F) and VEGF (G). TCs were also revealed by methylene blue vital staining (H). In C and D, TCs are identified by c-kit expression (green), the basal lamina by laminin expression (red) and nuclei are stained with DAPI (blue). Original magnification 1000×.
Figure Legend Snippet: Human skeletal muscle, immunohistochemistry with HRP conjugated antibodies on cryosections (A, B, E, H) and immunofluorescence-confocal microscopy (C, D). TCs are located within interstitium, and express c-kit (A–D), caveolin-1 (E), vimentin (F) and VEGF (G). TCs were also revealed by methylene blue vital staining (H). In C and D, TCs are identified by c-kit expression (green), the basal lamina by laminin expression (red) and nuclei are stained with DAPI (blue). Original magnification 1000×.

Techniques Used: Immunohistochemistry, Immunofluorescence, Confocal Microscopy, Staining, Expressing

10) Product Images from "Indomethacin suppresses growth of colon cancer via inhibition of angiogenesis in vivo"

Article Title: Indomethacin suppresses growth of colon cancer via inhibition of angiogenesis in vivo

Journal: World Journal of Gastroenterology : WJG

doi: 10.3748/wjg.v11.i3.340

Sections of immunohistochemical staining for MVD (stained for CD34) and VEGF expression in both groups. A: MVD of control group; B: MVD of treated group; C: VEGF expression of control group; D: VEGF expression of treated group (S-P method ×400).
Figure Legend Snippet: Sections of immunohistochemical staining for MVD (stained for CD34) and VEGF expression in both groups. A: MVD of control group; B: MVD of treated group; C: VEGF expression of control group; D: VEGF expression of treated group (S-P method ×400).

Techniques Used: Immunohistochemistry, Staining, Expressing

11) Product Images from "Loss of p53 and Acquisition of Angiogenic MicroRNA Profile Are Insufficient to Facilitate Progression of Bladder Urothelial Carcinoma in Situ to Invasive Carcinoma *"

Article Title: Loss of p53 and Acquisition of Angiogenic MicroRNA Profile Are Insufficient to Facilitate Progression of Bladder Urothelial Carcinoma in Situ to Invasive Carcinoma *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M110.198069

VEGF in UPK II-SV40 bladder carcinoma. A , total protein lysates from whole bladder were analyzed by Western blot for VEGF showing an increased expression of the main pro-angiogenic factor in UPK II-SV40 carcinoma in situ ; expression of SV40 was used as
Figure Legend Snippet: VEGF in UPK II-SV40 bladder carcinoma. A , total protein lysates from whole bladder were analyzed by Western blot for VEGF showing an increased expression of the main pro-angiogenic factor in UPK II-SV40 carcinoma in situ ; expression of SV40 was used as

Techniques Used: Western Blot, Expressing, In Situ

12) Product Images from "Knockdown of dickkopf2 inhibits vascular endothelia growth factor expression through the Wnt/β-catenin signaling pathway in human retinal pigment epithelial cells under hypoxic conditions"

Article Title: Knockdown of dickkopf2 inhibits vascular endothelia growth factor expression through the Wnt/β-catenin signaling pathway in human retinal pigment epithelial cells under hypoxic conditions

Journal: Experimental and Therapeutic Medicine

doi: 10.3892/etm.2018.5915

Knockdown of DKK2 inhibits hypoxia-induced HIF-1α and VEGF expression in RPE cells. RPE cells transfected with siRNA-DKK2 or siRNA-mock were exposed to hypoxia for 24 h. The mRNA expression levels of (A) HIF-1α and (B) VEGF mRNA. mRNA levels were normalized to those of β-actin. (C) The protein expression levels of HIF-1α and VEGF. HIF-1α and VEGF protein expression levels were normalized to GAPDH. (D) Quantification of HIF-1α and VEGF protein expression levels. Data are presented at the mean ± standard deviation from three independent experiments performed in duplicate. *P
Figure Legend Snippet: Knockdown of DKK2 inhibits hypoxia-induced HIF-1α and VEGF expression in RPE cells. RPE cells transfected with siRNA-DKK2 or siRNA-mock were exposed to hypoxia for 24 h. The mRNA expression levels of (A) HIF-1α and (B) VEGF mRNA. mRNA levels were normalized to those of β-actin. (C) The protein expression levels of HIF-1α and VEGF. HIF-1α and VEGF protein expression levels were normalized to GAPDH. (D) Quantification of HIF-1α and VEGF protein expression levels. Data are presented at the mean ± standard deviation from three independent experiments performed in duplicate. *P

Techniques Used: Expressing, Transfection, Standard Deviation

13) Product Images from "Kidney-derived c-kit+ progenitor/stem cells contribute to podocyte recovery in a model of acute proteinuria"

Article Title: Kidney-derived c-kit+ progenitor/stem cells contribute to podocyte recovery in a model of acute proteinuria

Journal: Scientific Reports

doi: 10.1038/s41598-018-33082-x

Kidney-derived c-kit + progenitor/stem cells present multi-compartment engraftment and differentiate into podocyte-like cells after PAN injection. ( A – C ) GFP-labelled c-kit + cells were observed in the interstitial compartment of cortex, including the peri-glomerular region (*), and in tubular compartment of cortex and corticomedullar regions. ( D ) GFP-labelled c-kit + cells stained for aquaporin-1 (AQP-1) in the Bowman’s capsule. Inset shows region at higher magnification ( D’ ). GFP-labelled c-kit + cells also stained for AQP-1 in proximal tubules ( D” ). Orthogonal slides of three-dimensional reconstructed images at all three different planes allows visualization of coexpression of fluorescence signals AQP-1 (red), GFP (green), ensuring that the yellow signal is not due to cell stacking ( D”’ ). ( E ) GFP-labelled c-kit + cells stained for smooth muscle actin (SMA) in a vessel, as demonstrated by 2-D confocal image ( E’ ) (arrows). ( F ) GFP-labeled c-kit + cells stained for α-Actinin-4 in glomeruli. Inset shows region at higher magnification ( F’ ) (arrow). ( G ) GFP-labeled c-kit + cells stained for synaptopodin in glomeruli. Inset shows higher magnification ( G” ) (arrows). ( H ) GFP-labeled c-kit + cells stained for WT-1 in a few podocytes. 3-D confocal image shows the co-localization ( H’ ) (arrows). ( I , J ) Clusters of GFP-labeled c-kit + cells were also found in glomeruli and did not stain for VEGF and desmin. ( K ) GFP-MSCs did not engraft at day 21 after PAN injection. ( L ) GFP-antibody in saline group. ( M ) On day 21, the number of GFP-labeled c-kit + cells was 4.6 ± 0.91 and 3.4 ± 1.15% in the glomerular and T-I compartments, respectively. No engraftment was observed in the MSC treated group. Scale bars represent 20 μm for confocal images. At day 10, n = 5 and n = 8 for saline and c-kit-treated group, respectively, and n = 12, n = 10, and n = 6 for saline, c-kit, and MSC-treated groups at day 21, respectively.
Figure Legend Snippet: Kidney-derived c-kit + progenitor/stem cells present multi-compartment engraftment and differentiate into podocyte-like cells after PAN injection. ( A – C ) GFP-labelled c-kit + cells were observed in the interstitial compartment of cortex, including the peri-glomerular region (*), and in tubular compartment of cortex and corticomedullar regions. ( D ) GFP-labelled c-kit + cells stained for aquaporin-1 (AQP-1) in the Bowman’s capsule. Inset shows region at higher magnification ( D’ ). GFP-labelled c-kit + cells also stained for AQP-1 in proximal tubules ( D” ). Orthogonal slides of three-dimensional reconstructed images at all three different planes allows visualization of coexpression of fluorescence signals AQP-1 (red), GFP (green), ensuring that the yellow signal is not due to cell stacking ( D”’ ). ( E ) GFP-labelled c-kit + cells stained for smooth muscle actin (SMA) in a vessel, as demonstrated by 2-D confocal image ( E’ ) (arrows). ( F ) GFP-labeled c-kit + cells stained for α-Actinin-4 in glomeruli. Inset shows region at higher magnification ( F’ ) (arrow). ( G ) GFP-labeled c-kit + cells stained for synaptopodin in glomeruli. Inset shows higher magnification ( G” ) (arrows). ( H ) GFP-labeled c-kit + cells stained for WT-1 in a few podocytes. 3-D confocal image shows the co-localization ( H’ ) (arrows). ( I , J ) Clusters of GFP-labeled c-kit + cells were also found in glomeruli and did not stain for VEGF and desmin. ( K ) GFP-MSCs did not engraft at day 21 after PAN injection. ( L ) GFP-antibody in saline group. ( M ) On day 21, the number of GFP-labeled c-kit + cells was 4.6 ± 0.91 and 3.4 ± 1.15% in the glomerular and T-I compartments, respectively. No engraftment was observed in the MSC treated group. Scale bars represent 20 μm for confocal images. At day 10, n = 5 and n = 8 for saline and c-kit-treated group, respectively, and n = 12, n = 10, and n = 6 for saline, c-kit, and MSC-treated groups at day 21, respectively.

Techniques Used: Derivative Assay, Injection, Staining, Fluorescence, Labeling

14) Product Images from "VEGF is essential for the growth and migration of human hepatocellular carcinoma cells"

Article Title: VEGF is essential for the growth and migration of human hepatocellular carcinoma cells

Journal: Molecular biology reports

doi: 10.1007/s11033-011-1304-2

Effects of VEGF on PKCα and p53 expression in BEL7402 cells A, PKCα and p53 protein levels in BEL7402 cells were detected by western blot analysis. Cells were treated with Ad-GFP or Ad-shVEGF165 for 1 or 3 days as indicated before the blotting analysis. α-tubulin served as an internal control. B–C, Quantitative analysis of PKCα (B) and p53(C) protein expression in BEL7402 cells by optical density value. * P
Figure Legend Snippet: Effects of VEGF on PKCα and p53 expression in BEL7402 cells A, PKCα and p53 protein levels in BEL7402 cells were detected by western blot analysis. Cells were treated with Ad-GFP or Ad-shVEGF165 for 1 or 3 days as indicated before the blotting analysis. α-tubulin served as an internal control. B–C, Quantitative analysis of PKCα (B) and p53(C) protein expression in BEL7402 cells by optical density value. * P

Techniques Used: Expressing, Western Blot

15) Product Images from "CPA4 is a Novel Diagnostic and Prognostic Marker for Human Non-Small-Cell Lung Cancer"

Article Title: CPA4 is a Novel Diagnostic and Prognostic Marker for Human Non-Small-Cell Lung Cancer

Journal: Journal of Cancer

doi: 10.7150/jca.15209

CPA4, Survivin and VEGF expression in lung cancer tissues were determined by immunochemistry. A. Positive expression of CPA4, B. Positive expression of VEGF, and C. Positive expression of Survivin.
Figure Legend Snippet: CPA4, Survivin and VEGF expression in lung cancer tissues were determined by immunochemistry. A. Positive expression of CPA4, B. Positive expression of VEGF, and C. Positive expression of Survivin.

Techniques Used: Expressing

Survival curves for NSCLC cancer using the Kaplan-Meier method and the log-rank test. A. O verall survival curves for patients with negative CPA4 expression (blue line) and patients with positive CPA4 (green line); B. Overall survival curves for patients with negative Survivin expression (blue line) and patients with positive Survivin (green line); C. Overall survival curves for patients with negative VEGF expression (green line) and patients with positive VEGF (blue line).
Figure Legend Snippet: Survival curves for NSCLC cancer using the Kaplan-Meier method and the log-rank test. A. O verall survival curves for patients with negative CPA4 expression (blue line) and patients with positive CPA4 (green line); B. Overall survival curves for patients with negative Survivin expression (blue line) and patients with positive Survivin (green line); C. Overall survival curves for patients with negative VEGF expression (green line) and patients with positive VEGF (blue line).

Techniques Used: Expressing

Elevated Serum CPA4 levels in lung cancer serum samples. A. Serum levels of CPA4 in healthy controls (n=80) and lung cancer patients(n=100). B. Serum levels of CPA4 in healthy controls (n=80), lung squamous cell carcinomas (LSCC, n=52) and Adenocarcinoma(AD, n=48). C. Receiver operator curves demonstrating the ability of CPA4. D. Receiver operator curves demonstrating the ability of serum CPA4, CYFRA21-1, NSE, SCCA, VEGF and Survivin alone to predict lung cancer. E. Receiver operator curves demonstrating the ability of the combination between CPA4 and CYFRA21-1.
Figure Legend Snippet: Elevated Serum CPA4 levels in lung cancer serum samples. A. Serum levels of CPA4 in healthy controls (n=80) and lung cancer patients(n=100). B. Serum levels of CPA4 in healthy controls (n=80), lung squamous cell carcinomas (LSCC, n=52) and Adenocarcinoma(AD, n=48). C. Receiver operator curves demonstrating the ability of CPA4. D. Receiver operator curves demonstrating the ability of serum CPA4, CYFRA21-1, NSE, SCCA, VEGF and Survivin alone to predict lung cancer. E. Receiver operator curves demonstrating the ability of the combination between CPA4 and CYFRA21-1.

Techniques Used:

16) Product Images from "Microglial VEGF Receptor Response Is an Integral Chemotactic Component in Alzheimer's Disease Pathology"

Article Title: Microglial VEGF Receptor Response Is an Integral Chemotactic Component in Alzheimer's Disease Pathology

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.2888-08.2009

Staining of Flt-1, VEGF, and Aβ in wild-type (WT) and transgenic mice. A , The upper panels show typical Flt-1 and Aβ ir and merged staining in WT mice. The lower panels present representative staining for the markers in transgenic APP23 animals. Scale bar is for 50 μm. B , Upper panels show representative patterns of staining for VEGF, Aβ, and merging of the two factors in WT mice. The lower panels present staining for the same markers in APP23 mice. Scale bar represents 50 μm.
Figure Legend Snippet: Staining of Flt-1, VEGF, and Aβ in wild-type (WT) and transgenic mice. A , The upper panels show typical Flt-1 and Aβ ir and merged staining in WT mice. The lower panels present representative staining for the markers in transgenic APP23 animals. Scale bar is for 50 μm. B , Upper panels show representative patterns of staining for VEGF, Aβ, and merging of the two factors in WT mice. The lower panels present staining for the same markers in APP23 mice. Scale bar represents 50 μm.

Techniques Used: Staining, Transgenic Assay, Mouse Assay

Association of Flt-1 and VEGF with β-amyloid peptide in AD tissue. The upper panels show representative images of Flt-1 and Aβ ir (left and middle panels) and merged staining of Flt-1/Aβ (right panel) in AD brain tissue. The lower panels show representative results for staining of VEGF with Aβ. Scale bar: 50 μm.
Figure Legend Snippet: Association of Flt-1 and VEGF with β-amyloid peptide in AD tissue. The upper panels show representative images of Flt-1 and Aβ ir (left and middle panels) and merged staining of Flt-1/Aβ (right panel) in AD brain tissue. The lower panels show representative results for staining of VEGF with Aβ. Scale bar: 50 μm.

Techniques Used: Staining

17) Product Images from "IKK? Knockout Prevents High Fat Diet Induced Arterial Atherosclerosis and NF-?B Signaling in Mice"

Article Title: IKK? Knockout Prevents High Fat Diet Induced Arterial Atherosclerosis and NF-?B Signaling in Mice

Journal: PLoS ONE

doi: 10.1371/journal.pone.0064930

Protein expression of NF-κB cascade components determined by Western blotting. ( A ) Protein levels of IKB-α, P50, P65, phosphorylated p50 (Pi-P50), phosphorylated p65 (Pi-P65), IL-18 and VEGF were measured by Western blotting. ( B ) Expression levels of P50, P65, Pi-P50 and Pi-P65 in the aortic vessel wall, after normalization to GAPDH were all significantly decreased in the DK group compared to the AK group of mice. ( C ) Expression of IKB-α normalized to GAPDH in the aortic vessel wall was greatly increased in the DK group compared with the AK group. ( D ) Expression of both NF-κB downstream factors, IL-18 and VEGF were downregulated in the DK group compared with the AK group. Values are means ± SD; n = 9 per group. Densitometric data are from one representative experiment of three separate experiments. * P
Figure Legend Snippet: Protein expression of NF-κB cascade components determined by Western blotting. ( A ) Protein levels of IKB-α, P50, P65, phosphorylated p50 (Pi-P50), phosphorylated p65 (Pi-P65), IL-18 and VEGF were measured by Western blotting. ( B ) Expression levels of P50, P65, Pi-P50 and Pi-P65 in the aortic vessel wall, after normalization to GAPDH were all significantly decreased in the DK group compared to the AK group of mice. ( C ) Expression of IKB-α normalized to GAPDH in the aortic vessel wall was greatly increased in the DK group compared with the AK group. ( D ) Expression of both NF-κB downstream factors, IL-18 and VEGF were downregulated in the DK group compared with the AK group. Values are means ± SD; n = 9 per group. Densitometric data are from one representative experiment of three separate experiments. * P

Techniques Used: Expressing, Western Blot, Mouse Assay

Protein expression of NF-κB cascade components determined by immunofluorescence. Representative images show merged nuclei (Hoechst, blue)+P50-positive staining (A, red), nuclei (Hoechst, blue)+P65-positive staining (B, red) and nuclei (Hoechst, blue) +VEGF-positive staining (C, red). The positively stained areas are marked with arrows (400×); n = 8 per group.
Figure Legend Snippet: Protein expression of NF-κB cascade components determined by immunofluorescence. Representative images show merged nuclei (Hoechst, blue)+P50-positive staining (A, red), nuclei (Hoechst, blue)+P65-positive staining (B, red) and nuclei (Hoechst, blue) +VEGF-positive staining (C, red). The positively stained areas are marked with arrows (400×); n = 8 per group.

Techniques Used: Expressing, Immunofluorescence, Staining

18) Product Images from "SPARC-induced increase in glioma matrix and decrease in vascularity are associated with reduced VEGF expression and secretion"

Article Title: SPARC-induced increase in glioma matrix and decrease in vascularity are associated with reduced VEGF expression and secretion

Journal: International Journal of Cancer. Journal International du Cancer

doi: 10.1002/ijc.23450

Assessment of SPARC, VEGF and VEGFR expression. ( a and b ) Conditioned media (CM) from control (VC2) and SPARC-transfected (S2) spheroids were subjected to immunoprecipitation (IP) with antibody to (Ab) to either VEGF or SPARC, followed by Western immunoblotting (IB) with anti-VEGF antibody ( a ) or anti-SPARC antibody ( b ). (Panel a ) Lane 1: VEGF antibody alone (control), Lane 2: anti-VEGF IP of VEGF protein (control), Lane 3: IP of VC2-CM minus primary Ab (control), Lane 4: anti-SPARC IP of VC2-CM, Lane 5: anti-VEGF IP of VC2-CM, Lane 6: anti-SPARC IP of S2-CM, Lane 7: anti-VEGF IP of S2-CM, Lane 8: empty lane, Lane 9: VEGF protein (for size standard) and Lane 10: molecular weight standard. Arrow: VEGF antibody immunoprecipitated VEGF only from control VC2-CM. (Panel b ) Lane 11: SPARC antibody alone (control), Lane 12: empty lane, Lane 13: IP of VC2-CM minus primary Ab (control), Lane 14: Anti-SPARC IP of VC2-CM, Lane 15: Anti-VEGF IP of VC2-CM, Lane 16: Anti-SPARC IP of S2-CM, Lane 17: anti-VEGF IP of S2-CM, Lane 18: empty lane, Lane 19: SPARC protein (for size standard) and Lane 20: molecular weight standard. Arrow: SPARC antibody immunoprecipitated SPARC only from control VC2- and S2-CM. Bands at 55 and 23 KDa are IgG heavy and light chains. Note that no coimmunoprecipitation was observed using either antibody, even when blots were overexposed as illustrated. ( c ) RT-PCR analysis of VEGFR1 (Flt-1) and VEGFR2 (Flk-1). (Top gel) Lane 1: molecular weight standard, Lane 2: control parental U87 cells, Lane 3: vector control VC1, Lane 4: vector control VC2, Lane 5: SPARC-transfected clone S1, Lane 6: SPARC-transfected clone S2, Lane 7: normal brain N141, Lane 8: astrocytoma A203, Lane 9: anaplastic astrocytoma AA152, Lane 10: GBM373, Lane 11: −RT-control, Lane 12: H 2 O Control reaction without cDNA. (Middle gel) GAPDH control coamplification of GAPDH in the same samples used with VEGFR1 primers to confirm integrity of cDNA. Note the lack of VEGFR1 in U87-transfected cells. (Bottom gel) VEGFR2 RT-PCR analysis of the same samples as the top gel. ( d ) Western blot analysis of VEGFR2. Lane 1: SPARC-transfected clone S2, Lane 2: vector-transfected control VC2, Lane 3: parental U87, Lane 4: THP-1-positive VEGFR2 control and Lane 5: molecular weight standard. The VEGFR2 blot was stripped and reprobed for actin as control for loading. ( e ) Immunoprecipitation (IP) of VEGFR2 for the same samples in panel b , followed by Western blotting (IB) for VEGFR2. VEGFR2 is present in U87 parental and transfected cells. ( c – e ) (∧) Indicates that the signal is on the same gel but moved closer. ( f ) VEGFR2 immunohistochemistry in normal rat brain, 41 controls (P, VC2) and SPARC-transfected S2 tumor. Magnifications as indicated. VEGFR2 transcript and protein are present in the U87 control and SPARC-transfectants.
Figure Legend Snippet: Assessment of SPARC, VEGF and VEGFR expression. ( a and b ) Conditioned media (CM) from control (VC2) and SPARC-transfected (S2) spheroids were subjected to immunoprecipitation (IP) with antibody to (Ab) to either VEGF or SPARC, followed by Western immunoblotting (IB) with anti-VEGF antibody ( a ) or anti-SPARC antibody ( b ). (Panel a ) Lane 1: VEGF antibody alone (control), Lane 2: anti-VEGF IP of VEGF protein (control), Lane 3: IP of VC2-CM minus primary Ab (control), Lane 4: anti-SPARC IP of VC2-CM, Lane 5: anti-VEGF IP of VC2-CM, Lane 6: anti-SPARC IP of S2-CM, Lane 7: anti-VEGF IP of S2-CM, Lane 8: empty lane, Lane 9: VEGF protein (for size standard) and Lane 10: molecular weight standard. Arrow: VEGF antibody immunoprecipitated VEGF only from control VC2-CM. (Panel b ) Lane 11: SPARC antibody alone (control), Lane 12: empty lane, Lane 13: IP of VC2-CM minus primary Ab (control), Lane 14: Anti-SPARC IP of VC2-CM, Lane 15: Anti-VEGF IP of VC2-CM, Lane 16: Anti-SPARC IP of S2-CM, Lane 17: anti-VEGF IP of S2-CM, Lane 18: empty lane, Lane 19: SPARC protein (for size standard) and Lane 20: molecular weight standard. Arrow: SPARC antibody immunoprecipitated SPARC only from control VC2- and S2-CM. Bands at 55 and 23 KDa are IgG heavy and light chains. Note that no coimmunoprecipitation was observed using either antibody, even when blots were overexposed as illustrated. ( c ) RT-PCR analysis of VEGFR1 (Flt-1) and VEGFR2 (Flk-1). (Top gel) Lane 1: molecular weight standard, Lane 2: control parental U87 cells, Lane 3: vector control VC1, Lane 4: vector control VC2, Lane 5: SPARC-transfected clone S1, Lane 6: SPARC-transfected clone S2, Lane 7: normal brain N141, Lane 8: astrocytoma A203, Lane 9: anaplastic astrocytoma AA152, Lane 10: GBM373, Lane 11: −RT-control, Lane 12: H 2 O Control reaction without cDNA. (Middle gel) GAPDH control coamplification of GAPDH in the same samples used with VEGFR1 primers to confirm integrity of cDNA. Note the lack of VEGFR1 in U87-transfected cells. (Bottom gel) VEGFR2 RT-PCR analysis of the same samples as the top gel. ( d ) Western blot analysis of VEGFR2. Lane 1: SPARC-transfected clone S2, Lane 2: vector-transfected control VC2, Lane 3: parental U87, Lane 4: THP-1-positive VEGFR2 control and Lane 5: molecular weight standard. The VEGFR2 blot was stripped and reprobed for actin as control for loading. ( e ) Immunoprecipitation (IP) of VEGFR2 for the same samples in panel b , followed by Western blotting (IB) for VEGFR2. VEGFR2 is present in U87 parental and transfected cells. ( c – e ) (∧) Indicates that the signal is on the same gel but moved closer. ( f ) VEGFR2 immunohistochemistry in normal rat brain, 41 controls (P, VC2) and SPARC-transfected S2 tumor. Magnifications as indicated. VEGFR2 transcript and protein are present in the U87 control and SPARC-transfectants.

Techniques Used: Expressing, Transfection, Immunoprecipitation, Western Blot, Molecular Weight, Reverse Transcription Polymerase Chain Reaction, Plasmid Preparation, Immunohistochemistry

Immunohistochemical, Western blot and RT-PCR analysis of VEGF protein and transcripts in control- (−SPARC) and SPARC- (+SPARC) transfected clones. ( a ) Representative tumor sections immunohistochemically stained for VEGF expression (×40). Note the decreased VEGF expression in the SPARC-expressing tumors. ( b ) Control and SPARC-expressing spheroids were assessed for VEGF and SPARC expression and secretion by Western blot analysis. L: lysate, M: medium. The same blot was used for all lysate analyses. Actin detection was used as a loading control. Note that increased SPARC expression correlated with decreased VEGF expression and secretion. ( c ) RT-PCR was performed to detect all 4 major VEGF isoforms as indicated. ( b and c ) (∧) Indicates that the signal is on the same gel but moved closer. ( d ) Real-time RT-PCR analysis of the VEGF165 isoform. Note that enhanced SPARC expression is associated with decreased VEGF165 transcript abundance. P-parental clonal U87MG-derived cell line, VC1- and VC1-vector control cell lines, S1- and S2- SPARC-transfected cell lines.
Figure Legend Snippet: Immunohistochemical, Western blot and RT-PCR analysis of VEGF protein and transcripts in control- (−SPARC) and SPARC- (+SPARC) transfected clones. ( a ) Representative tumor sections immunohistochemically stained for VEGF expression (×40). Note the decreased VEGF expression in the SPARC-expressing tumors. ( b ) Control and SPARC-expressing spheroids were assessed for VEGF and SPARC expression and secretion by Western blot analysis. L: lysate, M: medium. The same blot was used for all lysate analyses. Actin detection was used as a loading control. Note that increased SPARC expression correlated with decreased VEGF expression and secretion. ( c ) RT-PCR was performed to detect all 4 major VEGF isoforms as indicated. ( b and c ) (∧) Indicates that the signal is on the same gel but moved closer. ( d ) Real-time RT-PCR analysis of the VEGF165 isoform. Note that enhanced SPARC expression is associated with decreased VEGF165 transcript abundance. P-parental clonal U87MG-derived cell line, VC1- and VC1-vector control cell lines, S1- and S2- SPARC-transfected cell lines.

Techniques Used: Immunohistochemistry, Western Blot, Reverse Transcription Polymerase Chain Reaction, Transfection, Clone Assay, Staining, Expressing, Quantitative RT-PCR, Derivative Assay, Plasmid Preparation

19) Product Images from "Supercritical Fluid Extraction of Citrus iyo Hort. ex Tanaka Pericarp Inhibits Growth and Induces Apoptosis Through Abrogation of STAT3 Regulated Gene Products in Human Prostate Cancer Xenograft Mouse Model"

Article Title: Supercritical Fluid Extraction of Citrus iyo Hort. ex Tanaka Pericarp Inhibits Growth and Induces Apoptosis Through Abrogation of STAT3 Regulated Gene Products in Human Prostate Cancer Xenograft Mouse Model

Journal: Integrative Cancer Therapies

doi: 10.1177/1534735416649659

SEYG exerts the effect against tumor cell proliferation and angiogenesis in prostate cancer. (A) Immunohistochemical analysis of proliferation marker Ki-67+ cell indicates the inhibition of human prostate cancer cells proliferation by SEYG dose-dependent treated groups of animals. Samples from 3 animals in each treatment group were analyzed, and representative data are shown (A, left panel ). Quantification of Ki-67 proliferation index as described in “Materials and Methods.” Values are represented as mean ± SD of triplicate (A, right panel ). Columns, mean of triplicate; bars, SD. (B) Immunohistochemical analysis of CD31 for microvessel density in prostate tumors indicates the inhibition of angiogenesis by SEYG dose-dependent treated groups of animals. Samples from 3 animals in each treatment group were analyzed, and representative data are shown (B, left panel ). Quantification of CD31 angiogenesis index as described in “Materials and Methods.” Values are represented as mean ± SD of triplicate (B, right panel ). Columns, mean of triplicate; bars, SD. (C) Immunohistochemical analysis of cleaved caspase-3 in prostate tumors. Samples from 3 animals in each treatment group were analyzed, and representative data are shown (C, left panel ). Quantification of cleaved caspase-3 as described in “Materials and Methods.” Values are represented as mean ± SD of triplicate (C, right panel ). Columns, mean of triplicate; bars, SD. (D) Western blot analysis showed the inhibition of p-STAT3, p-JAK1, p-JAK2, and p-Src by SEYG in whole cell extracts from animal tissue. The same blots were stripped and reprobed with STAT3, JAK1, JAK2, and Src antibody to verify equal protein loading. (E-G) Equal amounts of lysates were analyzed by Western blot analysis using antibodies against bcl-2, bcl-xL, survivin, IAP-1, IAP-2, COX-2, cyclin D1, cyclin E, VEGF, MMP-9, p53, and p21. β-Actin was used as a loading control. Western blotting samples from 3 mice in each group were analyzed and representative data are shown.
Figure Legend Snippet: SEYG exerts the effect against tumor cell proliferation and angiogenesis in prostate cancer. (A) Immunohistochemical analysis of proliferation marker Ki-67+ cell indicates the inhibition of human prostate cancer cells proliferation by SEYG dose-dependent treated groups of animals. Samples from 3 animals in each treatment group were analyzed, and representative data are shown (A, left panel ). Quantification of Ki-67 proliferation index as described in “Materials and Methods.” Values are represented as mean ± SD of triplicate (A, right panel ). Columns, mean of triplicate; bars, SD. (B) Immunohistochemical analysis of CD31 for microvessel density in prostate tumors indicates the inhibition of angiogenesis by SEYG dose-dependent treated groups of animals. Samples from 3 animals in each treatment group were analyzed, and representative data are shown (B, left panel ). Quantification of CD31 angiogenesis index as described in “Materials and Methods.” Values are represented as mean ± SD of triplicate (B, right panel ). Columns, mean of triplicate; bars, SD. (C) Immunohistochemical analysis of cleaved caspase-3 in prostate tumors. Samples from 3 animals in each treatment group were analyzed, and representative data are shown (C, left panel ). Quantification of cleaved caspase-3 as described in “Materials and Methods.” Values are represented as mean ± SD of triplicate (C, right panel ). Columns, mean of triplicate; bars, SD. (D) Western blot analysis showed the inhibition of p-STAT3, p-JAK1, p-JAK2, and p-Src by SEYG in whole cell extracts from animal tissue. The same blots were stripped and reprobed with STAT3, JAK1, JAK2, and Src antibody to verify equal protein loading. (E-G) Equal amounts of lysates were analyzed by Western blot analysis using antibodies against bcl-2, bcl-xL, survivin, IAP-1, IAP-2, COX-2, cyclin D1, cyclin E, VEGF, MMP-9, p53, and p21. β-Actin was used as a loading control. Western blotting samples from 3 mice in each group were analyzed and representative data are shown.

Techniques Used: Immunohistochemistry, Marker, Inhibition, Western Blot, Mouse Assay

SEYG inhibits binding of STAT3 to the DNA and expression of various gene products in human prostate cancer cells. (A) SEYG suppresses STAT3 binding activity. DU145 cells (1 × 10 6 cells/well) were treated with various indicated concentrations of SEYG for 6 hours, analyzed for nuclear STAT3 levels by EMSA. Oct-1 EMSA is shown as a loading control. (B) SEYG causes the inhibition of translocation of STAT3 to the nucleus. After 6 hours of SEYG treatment, the cells were fixed and permeabilized. STAT3 (green) was immunostained with rabbit anti-STAT3 followed by FITC-conjugated secondary antibodies and the nuclei (blue) were stained with DAPI. The third panels show the merged images of the first and second panels. The results shown are representative of 2 independent experiments. (C) Cell proliferation assay was performed using the Roche xCELLigence Real-Time Cell Analyzer (RTCA) DP instrument (Roche Diagnostics GmbH) as described in “Material and Methods.” After DU145 cells (5 × 10 3 cells/well) were seeded onto 96-well E-plates and continuously monitored using impedance technology. (D-F) DU145 cells (1 × 10 6 cells/well) were incubated with the indicated concentrations of SEYG for 24 hours. Whole-cell extracts were prepared, and 20 µg of the whole-cell lysate was resolved by SDS-PAGE, electrotransferred to nitrocellulose membrane, sliced from the membrane based on the molecular weight, and then probed with antibodies against bcl-2, bcl-xL, survivin, IAP1/2, cyclin D1, cyclin E, COX-2, VEGF, and MMP-9 as described in “Materials and Methods.” The same blots were stripped and reprobed with β-actin antibody to verify equal protein loading. The results shown here are representative of 3 independent experiments.
Figure Legend Snippet: SEYG inhibits binding of STAT3 to the DNA and expression of various gene products in human prostate cancer cells. (A) SEYG suppresses STAT3 binding activity. DU145 cells (1 × 10 6 cells/well) were treated with various indicated concentrations of SEYG for 6 hours, analyzed for nuclear STAT3 levels by EMSA. Oct-1 EMSA is shown as a loading control. (B) SEYG causes the inhibition of translocation of STAT3 to the nucleus. After 6 hours of SEYG treatment, the cells were fixed and permeabilized. STAT3 (green) was immunostained with rabbit anti-STAT3 followed by FITC-conjugated secondary antibodies and the nuclei (blue) were stained with DAPI. The third panels show the merged images of the first and second panels. The results shown are representative of 2 independent experiments. (C) Cell proliferation assay was performed using the Roche xCELLigence Real-Time Cell Analyzer (RTCA) DP instrument (Roche Diagnostics GmbH) as described in “Material and Methods.” After DU145 cells (5 × 10 3 cells/well) were seeded onto 96-well E-plates and continuously monitored using impedance technology. (D-F) DU145 cells (1 × 10 6 cells/well) were incubated with the indicated concentrations of SEYG for 24 hours. Whole-cell extracts were prepared, and 20 µg of the whole-cell lysate was resolved by SDS-PAGE, electrotransferred to nitrocellulose membrane, sliced from the membrane based on the molecular weight, and then probed with antibodies against bcl-2, bcl-xL, survivin, IAP1/2, cyclin D1, cyclin E, COX-2, VEGF, and MMP-9 as described in “Materials and Methods.” The same blots were stripped and reprobed with β-actin antibody to verify equal protein loading. The results shown here are representative of 3 independent experiments.

Techniques Used: Binding Assay, Expressing, Activity Assay, Inhibition, Translocation Assay, Staining, Proliferation Assay, Incubation, SDS Page, Molecular Weight

20) Product Images from "Pegylated siRNA-loaded calcium phosphate nanoparticle-driven amplification of cancer cell internalization in vivo"

Article Title: Pegylated siRNA-loaded calcium phosphate nanoparticle-driven amplification of cancer cell internalization in vivo

Journal: Biomaterials

doi: 10.1016/j.biomaterials.2013.01.046

Doxorubicin-incorporated nanoparticles enhance siRNA delivery and target-specific knock-down in cancer cells. (a) A decrease in relative mRNA expression of XIAP, PARP, VEGF, and EGFR in H292 cells following a 24 h treatment with corresponding nanoparticles.
Figure Legend Snippet: Doxorubicin-incorporated nanoparticles enhance siRNA delivery and target-specific knock-down in cancer cells. (a) A decrease in relative mRNA expression of XIAP, PARP, VEGF, and EGFR in H292 cells following a 24 h treatment with corresponding nanoparticles.

Techniques Used: Expressing

21) Product Images from "Novel mechanism for obesity-induced colon cancer progression"

Article Title: Novel mechanism for obesity-induced colon cancer progression

Journal: Carcinogenesis

doi: 10.1093/carcin/bgp041

Inhibition of conditioned media driven HUVEC cell proliferation. ( A ) The effect of conditioned media from leptin (50 ng/ml)-treated IMCE ( Apc Min/+ ) cells and coincubation with anti-VEGF or anti-VEGFR-2 antibody (1 μg/ml) on HUVEC cell proliferation
Figure Legend Snippet: Inhibition of conditioned media driven HUVEC cell proliferation. ( A ) The effect of conditioned media from leptin (50 ng/ml)-treated IMCE ( Apc Min/+ ) cells and coincubation with anti-VEGF or anti-VEGFR-2 antibody (1 μg/ml) on HUVEC cell proliferation

Techniques Used: Inhibition

22) Product Images from "MiR-492 impairs the angiogenic potential of endothelial cells"

Article Title: MiR-492 impairs the angiogenic potential of endothelial cells

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.12085

The luciferase assay showed that miR-492 was unable to bind eNOS 3′UTR, whereas the selected miR-492 pull-out targets, except for BRAF, were able to interact with reporters containing putative binding sites in the mRNA target sequence ( A ). HUVEC transfected with miR-492 in comparison to those transfected with ds-nc showed the down-regulation of VEGF ( B ). The expression of miR-492 in VEGF-HUVEC ( C ). VEGF-HUVEC transfected with miR-492 in comparison to those transfected with ds-nc showed the reduction of cell proliferation ( D ), eNOS expression ( E ) and wound-healing activity ( F ). Data are reported as mean of at least three independent experiments (* P
Figure Legend Snippet: The luciferase assay showed that miR-492 was unable to bind eNOS 3′UTR, whereas the selected miR-492 pull-out targets, except for BRAF, were able to interact with reporters containing putative binding sites in the mRNA target sequence ( A ). HUVEC transfected with miR-492 in comparison to those transfected with ds-nc showed the down-regulation of VEGF ( B ). The expression of miR-492 in VEGF-HUVEC ( C ). VEGF-HUVEC transfected with miR-492 in comparison to those transfected with ds-nc showed the reduction of cell proliferation ( D ), eNOS expression ( E ) and wound-healing activity ( F ). Data are reported as mean of at least three independent experiments (* P

Techniques Used: Luciferase, Binding Assay, Sequencing, Transfection, Expressing, Activity Assay

23) Product Images from "EGCG Attenuates Autoimmune Arthritis by Inhibition of STAT3 and HIF-1? with Th17/Treg Control"

Article Title: EGCG Attenuates Autoimmune Arthritis by Inhibition of STAT3 and HIF-1? with Th17/Treg Control

Journal: PLoS ONE

doi: 10.1371/journal.pone.0086062

Expression of inflammatory cytokines and molecules associated with mTOR signaling. (A–B) The joint tissues were obtained from CIA and EGCG injected mice and were stained with the anti-IL-1β, anti–IL-6, anti-TNF-α, anti-IL-17, anti-RANK, anti-VEGF (A), anti-mTOR, anti-HIF-1α, anti-STAT3 or isotype control Abs (B). Data are representative of three independent experiments.
Figure Legend Snippet: Expression of inflammatory cytokines and molecules associated with mTOR signaling. (A–B) The joint tissues were obtained from CIA and EGCG injected mice and were stained with the anti-IL-1β, anti–IL-6, anti-TNF-α, anti-IL-17, anti-RANK, anti-VEGF (A), anti-mTOR, anti-HIF-1α, anti-STAT3 or isotype control Abs (B). Data are representative of three independent experiments.

Techniques Used: Expressing, Injection, Mouse Assay, Staining

24) Product Images from "The hypoxia-inducible factor-responsive proteins semaphorin 4D and vascular endothelial growth factor promote tumor growth and angiogenesis in oral squamous cell carcinoma"

Article Title: The hypoxia-inducible factor-responsive proteins semaphorin 4D and vascular endothelial growth factor promote tumor growth and angiogenesis in oral squamous cell carcinoma

Journal: Experimental Cell Research

doi: 10.1016/j.yexcr.2012.04.019

SEMA4D and VEGF production by HN12 cells cooperates to promote tumor growth, neoplastic cell proliferation and vascularity
Figure Legend Snippet: SEMA4D and VEGF production by HN12 cells cooperates to promote tumor growth, neoplastic cell proliferation and vascularity

Techniques Used:

HIF-mediated expression of SEMA4D and VEGF by OSCC cooperate to promote a pro-angiogenic response in vivo
Figure Legend Snippet: HIF-mediated expression of SEMA4D and VEGF by OSCC cooperate to promote a pro-angiogenic response in vivo

Techniques Used: Expressing, In Vivo

HIF-mediated expression of SEMA4D and VEGF by OSCC cooperate to promote a pro-angiogenic response in vitro
Figure Legend Snippet: HIF-mediated expression of SEMA4D and VEGF by OSCC cooperate to promote a pro-angiogenic response in vitro

Techniques Used: Expressing, In Vitro

25) Product Images from "Calvarial Defect Healing Induced by Small Molecule Smoothened Agonist"

Article Title: Calvarial Defect Healing Induced by Small Molecule Smoothened Agonist

Journal: Tissue Engineering. Part A

doi: 10.1089/ten.tea.2016.0167

Immunohistochemical analysis of calvarial defect healing. (A, B) OCN, (C, D) BSP, and (E, F) VEGF expression were interrogated by immunohistochemistry among control- and SAG-treated conditions (1 mM). Black arrowheads indicate immunostaining within osteocytes. Black dashed lines
Figure Legend Snippet: Immunohistochemical analysis of calvarial defect healing. (A, B) OCN, (C, D) BSP, and (E, F) VEGF expression were interrogated by immunohistochemistry among control- and SAG-treated conditions (1 mM). Black arrowheads indicate immunostaining within osteocytes. Black dashed lines

Techniques Used: Immunohistochemistry, Expressing, Immunostaining

26) Product Images from "Brain protection against ischemic stroke using choline as a new molecular bypass treatment"

Article Title: Brain protection against ischemic stroke using choline as a new molecular bypass treatment

Journal: Acta Pharmacologica Sinica

doi: 10.1038/aps.2015.104

Effects of oral choline treatment on the gene and protein expression levels, respectively, of α7 nAChR (A and B), HIF-1α (C and D), and VEGF (E and F) in the ischemic cerebral cortex. Mean±SEM. n =3. b P
Figure Legend Snippet: Effects of oral choline treatment on the gene and protein expression levels, respectively, of α7 nAChR (A and B), HIF-1α (C and D), and VEGF (E and F) in the ischemic cerebral cortex. Mean±SEM. n =3. b P

Techniques Used: Expressing

Schematic illustration of a new molecular bypass therapy against ischemic stroke using choline. Choline confers brain protection against ischemic stroke in the pMCAO-operated rats possibly via a pathway that facilitates angiogenesis through mechanisms that include activating the α7 receptor, up-regulating HIF-1α expression, and increasing VEGF release, resulting in endothelial cell proliferation, migration, and tube formation.
Figure Legend Snippet: Schematic illustration of a new molecular bypass therapy against ischemic stroke using choline. Choline confers brain protection against ischemic stroke in the pMCAO-operated rats possibly via a pathway that facilitates angiogenesis through mechanisms that include activating the α7 receptor, up-regulating HIF-1α expression, and increasing VEGF release, resulting in endothelial cell proliferation, migration, and tube formation.

Techniques Used: Expressing, Migration

27) Product Images from "The Wilms' Tumor Gene WT1 − 17AA/− KTS Splice Variant Increases Tumorigenic Activity Through Up-Regulation of Vascular Endothelial Growth Factor in an In Vivo Ovarian Cancer Model"

Article Title: The Wilms' Tumor Gene WT1 − 17AA/− KTS Splice Variant Increases Tumorigenic Activity Through Up-Regulation of Vascular Endothelial Growth Factor in an In Vivo Ovarian Cancer Model

Journal: Translational Oncology

doi: 10.1016/j.tranon.2014.07.008

The effects of the WT1 − 17AA/− KTS splice variant on the expression of VEGF protein and angiogenesis. (A) Intra-abdominally disseminated tumors were harvested from mice injected with cells expressing control vector or
Figure Legend Snippet: The effects of the WT1 − 17AA/− KTS splice variant on the expression of VEGF protein and angiogenesis. (A) Intra-abdominally disseminated tumors were harvested from mice injected with cells expressing control vector or

Techniques Used: Variant Assay, Expressing, Mouse Assay, Injection, Plasmid Preparation

28) Product Images from "Effects of hypoxia-inducible factor-1? silencing on the proliferation of CBRH-7919 hepatoma cells"

Article Title: Effects of hypoxia-inducible factor-1? silencing on the proliferation of CBRH-7919 hepatoma cells

Journal: World Journal of Gastroenterology : WJG

doi: 10.3748/wjg.v19.i11.1749

Protein expression levels of hypoxia-inducible factor-1α and vascular endothelial growth factor after small interfering RNAs transfection (24 h processing time). A: The Western blotting analysis of protein expression levels of hypoxia-inducible
Figure Legend Snippet: Protein expression levels of hypoxia-inducible factor-1α and vascular endothelial growth factor after small interfering RNAs transfection (24 h processing time). A: The Western blotting analysis of protein expression levels of hypoxia-inducible

Techniques Used: Expressing, Transfection, Western Blot

mRNA expression levels of hypoxia-inducible factor-1α and vascular endothelial growth factor. A, B: Histograms illustrating hypoxia-inducible factor-1α (HIF-1α) mRNA expression after exposure to various concentrations of CoCl 2
Figure Legend Snippet: mRNA expression levels of hypoxia-inducible factor-1α and vascular endothelial growth factor. A, B: Histograms illustrating hypoxia-inducible factor-1α (HIF-1α) mRNA expression after exposure to various concentrations of CoCl 2

Techniques Used: Expressing

Protein expression levels of hypoxia-inducible factor-1α and vascular endothelial growth factor after exposure to 0-300 μmol/L CoCl 2 for 12 and 24 h. A, B: The Western blotting analysis of protein expression levels of hypoxia-inducible
Figure Legend Snippet: Protein expression levels of hypoxia-inducible factor-1α and vascular endothelial growth factor after exposure to 0-300 μmol/L CoCl 2 for 12 and 24 h. A, B: The Western blotting analysis of protein expression levels of hypoxia-inducible

Techniques Used: Expressing, Western Blot

Protein expression levels of p-AKT, AKT, p21, cyclinD1, vascular endothelial growth factor and hypoxia-inducible factor-1α after the transfection with specific small interfering RNAs (processing time of 24 h). A: The Western blotting analysis
Figure Legend Snippet: Protein expression levels of p-AKT, AKT, p21, cyclinD1, vascular endothelial growth factor and hypoxia-inducible factor-1α after the transfection with specific small interfering RNAs (processing time of 24 h). A: The Western blotting analysis

Techniques Used: Expressing, Transfection, Western Blot

29) Product Images from "New 3-Cyano-2-Substituted Pyridines Induce Apoptosis in MCF 7 Breast Cancer Cells"

Article Title: New 3-Cyano-2-Substituted Pyridines Induce Apoptosis in MCF 7 Breast Cancer Cells

Journal: Molecules

doi: 10.3390/molecules21020230

Compound 9a downregulated metastatic-related genes. ( A ) Compound 9a down-regulated phosphoAkt and β catenin. Cells were treated with 0.5, 1 and 2 μM of 9a for 24 h. The cell lysates were collected and the expression of phospho Akt and β catenin was studied by western blot analysis using specific antibodies in treated and non-treated control cells. β-actin was used as a loading control; ( B ) Compound 9a down-regulated MMP 9 and VEGF. Cells were treated with 2 μM of 9a for 24 h. The cell lysates were collected and the expression of MMP 9 and VEGF was studied by western blot analysis using specific antibodies in treated and non-treated control cells. β-actin was used as a loading control. C: control (untreated cells).
Figure Legend Snippet: Compound 9a downregulated metastatic-related genes. ( A ) Compound 9a down-regulated phosphoAkt and β catenin. Cells were treated with 0.5, 1 and 2 μM of 9a for 24 h. The cell lysates were collected and the expression of phospho Akt and β catenin was studied by western blot analysis using specific antibodies in treated and non-treated control cells. β-actin was used as a loading control; ( B ) Compound 9a down-regulated MMP 9 and VEGF. Cells were treated with 2 μM of 9a for 24 h. The cell lysates were collected and the expression of MMP 9 and VEGF was studied by western blot analysis using specific antibodies in treated and non-treated control cells. β-actin was used as a loading control. C: control (untreated cells).

Techniques Used: Expressing, Western Blot

30) Product Images from "Endoplasmic Reticulum Stress is implicated in Retinal Inflammation and Diabetic Retinopathy"

Article Title: Endoplasmic Reticulum Stress is implicated in Retinal Inflammation and Diabetic Retinopathy

Journal: FEBS letters

doi: 10.1016/j.febslet.2009.04.007

Inhibition of ER stress by PBA ameliorated hypoxia-induced VEGF and TNF-α expression in HREC
Figure Legend Snippet: Inhibition of ER stress by PBA ameliorated hypoxia-induced VEGF and TNF-α expression in HREC

Techniques Used: Inhibition, Expressing

31) Product Images from "Fibroblast-Derived Extracellular Matrix Induces Chondrogenic Differentiation in Human Adipose-Derived Mesenchymal Stromal/Stem Cells in Vitro"

Article Title: Fibroblast-Derived Extracellular Matrix Induces Chondrogenic Differentiation in Human Adipose-Derived Mesenchymal Stromal/Stem Cells in Vitro

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms17081259

Anti-senescence effect of fd-ECM on ad-MSCs. ( A ) Ad-MSCs were cultured on plastic dishes (−) and on fd-ECM (+) for 48 h, harvested, and total RNA extracted. RT-qPCR was performed to evaluate human Telomerase Reverse Transcriptase ( hTERT ), VEGF , and bFGF mRNA levels; ( B ) Ad-MSCs were cultured on plastic and on an fd-ECM for 48 h, harvested, and total RNA extracted. RT-qPCR was performed to evaluate P16 , P21 , and P53 mRNA levels; ( C ) Ad-MSCs were cultured on plastic (−) and on fd-ECM (+), harvested, and immunoblot analysis was performed to evaluate VEGF, bFGF, p21, and p53 protein levels; and ( D ) ad-MSCs were cultured on plastic (−) and on an fd-ECM (+) and immunoblot analysis was performed to evaluate cleaved caspases 3 and 9 protein levels. * p
Figure Legend Snippet: Anti-senescence effect of fd-ECM on ad-MSCs. ( A ) Ad-MSCs were cultured on plastic dishes (−) and on fd-ECM (+) for 48 h, harvested, and total RNA extracted. RT-qPCR was performed to evaluate human Telomerase Reverse Transcriptase ( hTERT ), VEGF , and bFGF mRNA levels; ( B ) Ad-MSCs were cultured on plastic and on an fd-ECM for 48 h, harvested, and total RNA extracted. RT-qPCR was performed to evaluate P16 , P21 , and P53 mRNA levels; ( C ) Ad-MSCs were cultured on plastic (−) and on fd-ECM (+), harvested, and immunoblot analysis was performed to evaluate VEGF, bFGF, p21, and p53 protein levels; and ( D ) ad-MSCs were cultured on plastic (−) and on an fd-ECM (+) and immunoblot analysis was performed to evaluate cleaved caspases 3 and 9 protein levels. * p

Techniques Used: Cell Culture, Quantitative RT-PCR

32) Product Images from "Nitrosative Stress Plays an Important Role in Wnt Pathway Activation in Diabetic Retinopathy"

Article Title: Nitrosative Stress Plays an Important Role in Wnt Pathway Activation in Diabetic Retinopathy

Journal: Antioxidants & Redox Signaling

doi: 10.1089/ars.2012.4583

UA downregulated the expression of ICAM-1 and VEGF, and reduced inflammation and vascular leakage in the retina of diabetic rats. STZ-induced diabetic rats were fed with UA in drinking water for 6 weeks. The retinas were dissected after thorough perfusion.
Figure Legend Snippet: UA downregulated the expression of ICAM-1 and VEGF, and reduced inflammation and vascular leakage in the retina of diabetic rats. STZ-induced diabetic rats were fed with UA in drinking water for 6 weeks. The retinas were dissected after thorough perfusion.

Techniques Used: Expressing

UA decreased high-glucose (HG)-induced tyrosine nitration and suppressed VEGF and ICAM-1 expression. ARPE19 cells were treated with 30 m M glucose for 48 h and then treated with different concentrations of UA for another 16 h, with
Figure Legend Snippet: UA decreased high-glucose (HG)-induced tyrosine nitration and suppressed VEGF and ICAM-1 expression. ARPE19 cells were treated with 30 m M glucose for 48 h and then treated with different concentrations of UA for another 16 h, with

Techniques Used: Nitration, Expressing

33) Product Images from "Loss of X-box binding protein 1 in Müller cells augments retinal inflammation in a mouse model of diabetes"

Article Title: Loss of X-box binding protein 1 in Müller cells augments retinal inflammation in a mouse model of diabetes

Journal: Diabetologia

doi: 10.1007/s00125-018-4776-y

Loss of XBP1 enhances expression of inflammatory factors and ER stress in Müller cells. ( a ) Primary retinal Müller cells (P1) isolated from Xbp1 Müller+/+ (WT) and Xbp1 Müller−/− (KO) mice were stained for the Müller-cell marker glutamine synthetase (GS) (red), and nuclei were stained with DAPI (blue). ( b ) Knockout efficiency was evaluated by measuring expression of Xbp1 mRNA by real-time RT-PCR ( n =3). ( c , d ) Vegf and Tnf-α mRNA levels were examined by real-time RT-PCR ( n =3). ( e ) Protein levels of VEGF, TNF-α and p-JNK were determined by western blot analysis and quantified by densitometry, with β-actin as the loading control ( n =3). ( f ) Levels of ER-stress-related proteins GRP78, p-eIF2α, ATF4 and ATF6 were determined by western blot analysis ( n =3). ( g ) Primary Müller cells were treated with HG (25 mmol/l) for up to 72 h. Expression levels of GRP78 and p-eIF2α were examined after 24 h of HG treatment, and levels of ATF6, VEGF, TNF-α and p-JNK were determined after 72 h of HG treatment, by western blot analysis ( n =3). All results are shown as mean ± SD. * p
Figure Legend Snippet: Loss of XBP1 enhances expression of inflammatory factors and ER stress in Müller cells. ( a ) Primary retinal Müller cells (P1) isolated from Xbp1 Müller+/+ (WT) and Xbp1 Müller−/− (KO) mice were stained for the Müller-cell marker glutamine synthetase (GS) (red), and nuclei were stained with DAPI (blue). ( b ) Knockout efficiency was evaluated by measuring expression of Xbp1 mRNA by real-time RT-PCR ( n =3). ( c , d ) Vegf and Tnf-α mRNA levels were examined by real-time RT-PCR ( n =3). ( e ) Protein levels of VEGF, TNF-α and p-JNK were determined by western blot analysis and quantified by densitometry, with β-actin as the loading control ( n =3). ( f ) Levels of ER-stress-related proteins GRP78, p-eIF2α, ATF4 and ATF6 were determined by western blot analysis ( n =3). ( g ) Primary Müller cells were treated with HG (25 mmol/l) for up to 72 h. Expression levels of GRP78 and p-eIF2α were examined after 24 h of HG treatment, and levels of ATF6, VEGF, TNF-α and p-JNK were determined after 72 h of HG treatment, by western blot analysis ( n =3). All results are shown as mean ± SD. * p

Techniques Used: Expressing, Isolation, Mouse Assay, Staining, Marker, Knock-Out, Quantitative RT-PCR, Western Blot

XBP1 deficiency exacerbates hypoxia-induced ER stress and inflammation in Müller cells. Primary mouse Müller cells were exposed to hypoxia for up to 4 h. ( a ) Protein levels of p-eIF2α were determined by western blot analysis and semi-quantified by densitometry ( n =3). ( b–d ) mRNA levels of spliced Xbp1 , Chop and Vegf were examined by real-time RT-PCR after 4 h of hypoxia (Hypo) or normoxia (Ctrl) treatment ( n =3). ( e ) Müller cells from Xbp1 Müller +/+ (WT) and Xbp1 Müller −/− (KO) mice were treated with hypoxia for 4 h. Protein levels of ER-stress markers, TNF-α and VEGF were determined by western blot analysis and quantified by densitometry, with β-actin as the loading control ( n =3). All results are shown as mean ± SD. * p
Figure Legend Snippet: XBP1 deficiency exacerbates hypoxia-induced ER stress and inflammation in Müller cells. Primary mouse Müller cells were exposed to hypoxia for up to 4 h. ( a ) Protein levels of p-eIF2α were determined by western blot analysis and semi-quantified by densitometry ( n =3). ( b–d ) mRNA levels of spliced Xbp1 , Chop and Vegf were examined by real-time RT-PCR after 4 h of hypoxia (Hypo) or normoxia (Ctrl) treatment ( n =3). ( e ) Müller cells from Xbp1 Müller +/+ (WT) and Xbp1 Müller −/− (KO) mice were treated with hypoxia for 4 h. Protein levels of ER-stress markers, TNF-α and VEGF were determined by western blot analysis and quantified by densitometry, with β-actin as the loading control ( n =3). All results are shown as mean ± SD. * p

Techniques Used: Western Blot, Quantitative RT-PCR, Mouse Assay

Inhibition of ER stress by chemical chaperones reduces hypoxia-induced TNF-α and VEGF production in Müller cells. Müller cells from Xbp1 Müller+/+ (WT) and Xbp1 Müller−/− (KO) mice were pre-treated with DMSO vehicle only, 5 mmol/l TMAO (TMAO 5) or 10 mmol/l TMAO (TMAO 10) ( a ) or with 0.5 mmol/l PBA (PBA 0.5) or 1.0 mmol/l PBA (PBA 1.0) ( b ) for 1 h and then exposed to hypoxia for an additional 4 h. Levels of ER-stress markers, TNF-α and VEGF were determined with western blot analysis and quantified by densitometry, with β-actin as the loading control ( n =3). All results are shown as mean ± SD. **p
Figure Legend Snippet: Inhibition of ER stress by chemical chaperones reduces hypoxia-induced TNF-α and VEGF production in Müller cells. Müller cells from Xbp1 Müller+/+ (WT) and Xbp1 Müller−/− (KO) mice were pre-treated with DMSO vehicle only, 5 mmol/l TMAO (TMAO 5) or 10 mmol/l TMAO (TMAO 10) ( a ) or with 0.5 mmol/l PBA (PBA 0.5) or 1.0 mmol/l PBA (PBA 1.0) ( b ) for 1 h and then exposed to hypoxia for an additional 4 h. Levels of ER-stress markers, TNF-α and VEGF were determined with western blot analysis and quantified by densitometry, with β-actin as the loading control ( n =3). All results are shown as mean ± SD. **p

Techniques Used: Inhibition, Mouse Assay, Western Blot

34) Product Images from "Wnt5a attenuates the pathogenic effects of the Wnt/β-catenin pathway in human retinal pigment epithelial cells via down-regulating β-catenin and Snail"

Article Title: Wnt5a attenuates the pathogenic effects of the Wnt/β-catenin pathway in human retinal pigment epithelial cells via down-regulating β-catenin and Snail

Journal: BMB Reports

doi: 10.5483/BMBRep.2015.48.9.140

Wnt5a downregulates the levels of angiogenic/inflammatory factors in human RPE cells. Total proteins were prepared from ARPE-19 (A) and hTERT-PRE-1 (B) cells treated with Wnt3a-CM and/or Wnt5a-CM and subjected to western blot analysis with antibody against NF-κB, TNF-α, or VEGF. The blots were re-probed with anti-actin antibody as loading control. The histogram shows the average volume density corrected for the loading control (n = 3) and bars indicate standard deviations group. *P
Figure Legend Snippet: Wnt5a downregulates the levels of angiogenic/inflammatory factors in human RPE cells. Total proteins were prepared from ARPE-19 (A) and hTERT-PRE-1 (B) cells treated with Wnt3a-CM and/or Wnt5a-CM and subjected to western blot analysis with antibody against NF-κB, TNF-α, or VEGF. The blots were re-probed with anti-actin antibody as loading control. The histogram shows the average volume density corrected for the loading control (n = 3) and bars indicate standard deviations group. *P

Techniques Used: Western Blot

35) Product Images from "Liver X receptor and STAT1 cooperate downstream of Gas6/Mer to induce anti-inflammatory arginase 2 expression in macrophages"

Article Title: Liver X receptor and STAT1 cooperate downstream of Gas6/Mer to induce anti-inflammatory arginase 2 expression in macrophages

Journal: Scientific Reports

doi: 10.1038/srep29673

STAT1 activation mediates Gas6-induced increases in LXRα and LXRβ as well as ABCA1, ABCG1, ApoE, AIM, Arg2 , and VEGF expression. BMDM from C57BL/6 mice ( a ) or from Mer −/− and WT mice ( b ) were stimulated with 400 ng/ml Gas6 for the indicated times. BMDM from WT or STAT1 −/− mice were stimulated with 400 ng/ml Gas6 for the indicated times ( c – g ). ( h ) RAW 264.7 cells were co-transfected with an LXRE-driven luciferase reporter vector and a Renilla control plasmid. After 24 h, cells were treated with 400 ng/ml Gas6 in the absence or presence of fludarabine at the indicated concentrations. LXR activity was then measured by the dual luciferase assay. ( i,j ) BMDM from C57BL/6 mice were pretreated with vehicle or the indicated concentrations of the JAK2 inhibitor tyrphostin AG490 (Tyr) for 1 h before being treated with 400 ng/ml Gas6. ( a,b,e,f ) The relative abundances of total STAT1, phosphorylated STAT1 (Y701), LXRα, and LXRβ proteins were determined by Western blotting analysis. The relative densitometric intensity was determined for each band and normalized to the indicated proteins. ( c,d,g,i,j ) The amounts of the LXRα, LXRβ, ABCA1, ABCG1, ApoE, AIM, Arg2 , and VEGF mRNAs were analyzed by real-time PCR and normalized to that of Hprt mRNA. Data in all bar graphs are means ± SEM of three independent experiments. * P
Figure Legend Snippet: STAT1 activation mediates Gas6-induced increases in LXRα and LXRβ as well as ABCA1, ABCG1, ApoE, AIM, Arg2 , and VEGF expression. BMDM from C57BL/6 mice ( a ) or from Mer −/− and WT mice ( b ) were stimulated with 400 ng/ml Gas6 for the indicated times. BMDM from WT or STAT1 −/− mice were stimulated with 400 ng/ml Gas6 for the indicated times ( c – g ). ( h ) RAW 264.7 cells were co-transfected with an LXRE-driven luciferase reporter vector and a Renilla control plasmid. After 24 h, cells were treated with 400 ng/ml Gas6 in the absence or presence of fludarabine at the indicated concentrations. LXR activity was then measured by the dual luciferase assay. ( i,j ) BMDM from C57BL/6 mice were pretreated with vehicle or the indicated concentrations of the JAK2 inhibitor tyrphostin AG490 (Tyr) for 1 h before being treated with 400 ng/ml Gas6. ( a,b,e,f ) The relative abundances of total STAT1, phosphorylated STAT1 (Y701), LXRα, and LXRβ proteins were determined by Western blotting analysis. The relative densitometric intensity was determined for each band and normalized to the indicated proteins. ( c,d,g,i,j ) The amounts of the LXRα, LXRβ, ABCA1, ABCG1, ApoE, AIM, Arg2 , and VEGF mRNAs were analyzed by real-time PCR and normalized to that of Hprt mRNA. Data in all bar graphs are means ± SEM of three independent experiments. * P

Techniques Used: Activation Assay, Expressing, Mouse Assay, Transfection, Luciferase, Plasmid Preparation, Activity Assay, Western Blot, Real-time Polymerase Chain Reaction

Gas6-induced LXRα and LXRβ transcriptional response is decreased in Mer - deficient BMDM. Mouse BMDM from wild-type or Mer −/− mice were stimulated with 400 ng/ml Gas6 for the indicated times ( a – d ). ( a,b,d ) The amounts of the LXRα, LXRβ, ABCA1, ABCG1, ApoE, AIM, Arg2 , and VEGF mRNAs were analyzed by real-time PCR and normalized to that of Hprt mRNA. ( c ) The relative abundances of LXRα and LXRβ proteins were determined by Western blotting analysis. The relative densitometric intensity was determined for each band and normalized to β-actin. Data in all bar graphs are means ± SEM of three independent experiments. * P
Figure Legend Snippet: Gas6-induced LXRα and LXRβ transcriptional response is decreased in Mer - deficient BMDM. Mouse BMDM from wild-type or Mer −/− mice were stimulated with 400 ng/ml Gas6 for the indicated times ( a – d ). ( a,b,d ) The amounts of the LXRα, LXRβ, ABCA1, ABCG1, ApoE, AIM, Arg2 , and VEGF mRNAs were analyzed by real-time PCR and normalized to that of Hprt mRNA. ( c ) The relative abundances of LXRα and LXRβ proteins were determined by Western blotting analysis. The relative densitometric intensity was determined for each band and normalized to β-actin. Data in all bar graphs are means ± SEM of three independent experiments. * P

Techniques Used: Mouse Assay, Real-time Polymerase Chain Reaction, Western Blot

Gas6 treatment enhances expression of LXRα and LXRβ and their target genes in BMDM. Mouse BMDM were stimulated with 400 ng/ml Gas6, 1 μM T0901317, 10 ng/ml interferon (IFN)-γ, 10 ng/ml IL-4, or 100 ng/ml LPS for 4 h ( a,b ) or 400 ng/ml Gas6 for the indicated times ( c – g ). ( a,b,e ) The amounts of the LXRα, LXRβ, ABCA1, ABCG1, ApoE, AIM, Arg2, VEGF, YM1 , and Arg1 mRNAs were analyzed by real-time PCR and normalized to that of Hprt mRNA. ( c,d,f,g ) The relative abundances of LXRα, LXRβ, ABCA1, ABCG1, ApoE, Aim, Arg2, and VEGF proteins were determined by Western blotting analysis. The relative densitometric intensity was determined for each band and normalized to β-actin. Data in all bar graphs are means ± SEM of three independent experiments. * P
Figure Legend Snippet: Gas6 treatment enhances expression of LXRα and LXRβ and their target genes in BMDM. Mouse BMDM were stimulated with 400 ng/ml Gas6, 1 μM T0901317, 10 ng/ml interferon (IFN)-γ, 10 ng/ml IL-4, or 100 ng/ml LPS for 4 h ( a,b ) or 400 ng/ml Gas6 for the indicated times ( c – g ). ( a,b,e ) The amounts of the LXRα, LXRβ, ABCA1, ABCG1, ApoE, AIM, Arg2, VEGF, YM1 , and Arg1 mRNAs were analyzed by real-time PCR and normalized to that of Hprt mRNA. ( c,d,f,g ) The relative abundances of LXRα, LXRβ, ABCA1, ABCG1, ApoE, Aim, Arg2, and VEGF proteins were determined by Western blotting analysis. The relative densitometric intensity was determined for each band and normalized to β-actin. Data in all bar graphs are means ± SEM of three independent experiments. * P

Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Western Blot

36) Product Images from "Brain protection against ischemic stroke using choline as a new molecular bypass treatment"

Article Title: Brain protection against ischemic stroke using choline as a new molecular bypass treatment

Journal: Acta Pharmacologica Sinica

doi: 10.1038/aps.2015.104

Effects of oral choline treatment on the gene and protein expression levels, respectively, of α7 nAChR (A and B), HIF-1α (C and D), and VEGF (E and F) in the ischemic cerebral cortex. Mean±SEM. n =3. b P
Figure Legend Snippet: Effects of oral choline treatment on the gene and protein expression levels, respectively, of α7 nAChR (A and B), HIF-1α (C and D), and VEGF (E and F) in the ischemic cerebral cortex. Mean±SEM. n =3. b P

Techniques Used: Expressing

Schematic illustration of a new molecular bypass therapy against ischemic stroke using choline. Choline confers brain protection against ischemic stroke in the pMCAO-operated rats possibly via a pathway that facilitates angiogenesis through mechanisms that include activating the α7 receptor, up-regulating HIF-1α expression, and increasing VEGF release, resulting in endothelial cell proliferation, migration, and tube formation.
Figure Legend Snippet: Schematic illustration of a new molecular bypass therapy against ischemic stroke using choline. Choline confers brain protection against ischemic stroke in the pMCAO-operated rats possibly via a pathway that facilitates angiogenesis through mechanisms that include activating the α7 receptor, up-regulating HIF-1α expression, and increasing VEGF release, resulting in endothelial cell proliferation, migration, and tube formation.

Techniques Used: Expressing, Migration

37) Product Images from "Effects of ultrasound and ultrasound contrast agent on vascular tissue"

Article Title: Effects of ultrasound and ultrasound contrast agent on vascular tissue

Journal: Cardiovascular Ultrasound

doi: 10.1186/1476-7120-10-29

Assessment of endothelial integrity by immunohistochemistry. Aortic sections were stained with three endothelial markers, anti-VEGF, anti- FLT-1 and anti-FLK-1 and the epitopes were revealed by DAB staining I ) Negative control, no primary antibodies, II ) Treated sections: A ) control, B ) US, C ) OPT and D ) US + OPT; The short arrows mark the endothelium. Magnification is 40x and representative sections from two experiments are shown.
Figure Legend Snippet: Assessment of endothelial integrity by immunohistochemistry. Aortic sections were stained with three endothelial markers, anti-VEGF, anti- FLT-1 and anti-FLK-1 and the epitopes were revealed by DAB staining I ) Negative control, no primary antibodies, II ) Treated sections: A ) control, B ) US, C ) OPT and D ) US + OPT; The short arrows mark the endothelium. Magnification is 40x and representative sections from two experiments are shown.

Techniques Used: Immunohistochemistry, Staining, Negative Control

38) Product Images from "Effect of Silibinin in Human Colorectal Cancer Cells: Targeting the Activation of NF-?B Signaling"

Article Title: Effect of Silibinin in Human Colorectal Cancer Cells: Targeting the Activation of NF-?B Signaling

Journal: Molecular carcinogenesis

doi: 10.1002/mc.21843

Effect of oral silibinin feeding on protein expression levels of various NF-κB-regulated molecules viz., cyclin D1, Bcl-2, COX2, iNOS, VEGF and MMPs in CRC xenograft tissues. Xenograft tissues of LoVo and SW480 cells, detailed in , were
Figure Legend Snippet: Effect of oral silibinin feeding on protein expression levels of various NF-κB-regulated molecules viz., cyclin D1, Bcl-2, COX2, iNOS, VEGF and MMPs in CRC xenograft tissues. Xenograft tissues of LoVo and SW480 cells, detailed in , were

Techniques Used: Expressing

39) Product Images from "Snail promotes the generation of vascular endothelium by breast cancer cells"

Article Title: Snail promotes the generation of vascular endothelium by breast cancer cells

Journal: Cell Death & Disease

doi: 10.1038/s41419-020-2651-5

Snail and p300 co-activate Sox2 and VEGF transcription. a MCF-7 cells were immunoprecipitated with Snail antibodies or pre-immune control serum (IgG) followed by western blotting with antibodies against p300 or Snail. b Luciferase reporter assay of MCF-7 cells cotransfected with Sox2 promotor-Luc or VEGF promotor-Luc with control siRNA or p300 siRNA. c qRT-PCR analysis of Sox2 or VEGF 165 mRNA expression in MCF-7 and ZR75-1 cells transfected with the indicated plasmids. d Western blotting and ELISA of MCF-7 cells transfected with the indicated plasmids using the indicated antibodies. e Relative luciferase activity of wild-type and mutated Sox2 promotor reporter constructs in MCF-7 cells transfected with empty vector or Snail. A and B indicate putative binding sites of Snail. The ‘X’ symbol denotes a mutated Snail-binding site. f ChIP analysis with the indicated antibodies in MCF-7 cells showed the occupancy of Snail, p300, and H3K27AC protein on putative Snail-binding sites in the Sox2 promoter. All values shown are means ± SD of three independent experiments performed in triplicate. g Relative luciferase activity of wild-type and mutated VEGF promotor reporter constructs in MCF-7 cells transfected with empty vector or Snail. A and B indicate putative binding sites of Snail. The ‘X’ symbol denotes a mutated Snail-binding site. h ChIP analysis with the indicated antibodies in MCF-7 cells showed the occupancy of Snail, p300, and H3K27AC protein on putative Snail-binding sites in the VEGF promoter. All values shown are means ± SD of three independent experiments performed in triplicate. * P
Figure Legend Snippet: Snail and p300 co-activate Sox2 and VEGF transcription. a MCF-7 cells were immunoprecipitated with Snail antibodies or pre-immune control serum (IgG) followed by western blotting with antibodies against p300 or Snail. b Luciferase reporter assay of MCF-7 cells cotransfected with Sox2 promotor-Luc or VEGF promotor-Luc with control siRNA or p300 siRNA. c qRT-PCR analysis of Sox2 or VEGF 165 mRNA expression in MCF-7 and ZR75-1 cells transfected with the indicated plasmids. d Western blotting and ELISA of MCF-7 cells transfected with the indicated plasmids using the indicated antibodies. e Relative luciferase activity of wild-type and mutated Sox2 promotor reporter constructs in MCF-7 cells transfected with empty vector or Snail. A and B indicate putative binding sites of Snail. The ‘X’ symbol denotes a mutated Snail-binding site. f ChIP analysis with the indicated antibodies in MCF-7 cells showed the occupancy of Snail, p300, and H3K27AC protein on putative Snail-binding sites in the Sox2 promoter. All values shown are means ± SD of three independent experiments performed in triplicate. g Relative luciferase activity of wild-type and mutated VEGF promotor reporter constructs in MCF-7 cells transfected with empty vector or Snail. A and B indicate putative binding sites of Snail. The ‘X’ symbol denotes a mutated Snail-binding site. h ChIP analysis with the indicated antibodies in MCF-7 cells showed the occupancy of Snail, p300, and H3K27AC protein on putative Snail-binding sites in the VEGF promoter. All values shown are means ± SD of three independent experiments performed in triplicate. * P

Techniques Used: Immunoprecipitation, Western Blot, Luciferase, Reporter Assay, Quantitative RT-PCR, Expressing, Transfection, Enzyme-linked Immunosorbent Assay, Activity Assay, Construct, Plasmid Preparation, Binding Assay, Chromatin Immunoprecipitation

Snail promotes tumor growth and endothelium generation in breast cancer cells in vivo. a Volume of xenograft tumors of ZR75-1 cells infected with lentivirus carrying Snail-copGFP or copGFP and Sox2 shRNA or VEGF shRNA. The tumors were measured by vernier caliper and tumor growth curves were plotted. Tumor volumes are presented as means ± SD ( n = 6). b Representative IF staining of endothelium marker endomucin and copGFP in xenograft tumors of the indicated groups. Scale bar: 50 μm. c Graphs show relative MVD of the indicated groups. Data are shown as means ± SD. d Graphic summary of Snail promoting tumor initiation and endothelium cell differentiation of breast cancer cells. Snail recruits p300 activation complex to the Sox2 promoter and enhances the cancer stem cell properties. Meanwhile, Snail/p300 complex binds to the VEGF promoter and activates the expression of VEGF. Elevated VEGF expression enhances the generation of breast CSCs to endothelial cells. * P
Figure Legend Snippet: Snail promotes tumor growth and endothelium generation in breast cancer cells in vivo. a Volume of xenograft tumors of ZR75-1 cells infected with lentivirus carrying Snail-copGFP or copGFP and Sox2 shRNA or VEGF shRNA. The tumors were measured by vernier caliper and tumor growth curves were plotted. Tumor volumes are presented as means ± SD ( n = 6). b Representative IF staining of endothelium marker endomucin and copGFP in xenograft tumors of the indicated groups. Scale bar: 50 μm. c Graphs show relative MVD of the indicated groups. Data are shown as means ± SD. d Graphic summary of Snail promoting tumor initiation and endothelium cell differentiation of breast cancer cells. Snail recruits p300 activation complex to the Sox2 promoter and enhances the cancer stem cell properties. Meanwhile, Snail/p300 complex binds to the VEGF promoter and activates the expression of VEGF. Elevated VEGF expression enhances the generation of breast CSCs to endothelial cells. * P

Techniques Used: In Vivo, Infection, shRNA, Staining, Marker, Cell Differentiation, Activation Assay, Expressing

40) Product Images from "Circ-ADAM9 targeting PTEN and ATG7 promotes autophagy and apoptosis of diabetic endothelial progenitor cells by sponging mir-20a-5p"

Article Title: Circ-ADAM9 targeting PTEN and ATG7 promotes autophagy and apoptosis of diabetic endothelial progenitor cells by sponging mir-20a-5p

Journal: Cell Death & Disease

doi: 10.1038/s41419-020-02745-x

Mir-20a-5p regulates apoptosis, autophagy, and angiogenic function of EPCs induced by high glucose in vitro. EPC dysfunction was induced by high glucose (30 mM) treatment for 24 h. Mannitol was used as an osmolar control treatment. EPCs were transfected with mir-20a-5p or negative control (NC) inhibitor, or mir-20a-5p or NC mimic. a RT-qPCR analysis of mir-20a-5p expression. b Flow-cytometric analysis of apoptosis using annexin V/propidium iodide (PI). Annexin V + /PI + or Annexin V + /PI − (quadrants 2 and 3) cells were defined as apoptotic cells. c Protein levels of BCL-2, BAX, and cleaved-CASP3 as detected by western blotting. d Representative images showing LC3 staining in different groups of EPCs infected with GFP-RFP-LC3 adenovirus for 24 h. Scale bar: 20 μm. e Western blot analysis of LC3B-II/LC3B-I and SQSTM1/p62 levels. f The angiogenic capability of EPCs was determined by a tube formation assay. Tube length was normalized to that in the control group. Scale: 200 μm. g Protein levels of VEGF as detected by western blotting. Inh inhibito, Mic mimic, * P
Figure Legend Snippet: Mir-20a-5p regulates apoptosis, autophagy, and angiogenic function of EPCs induced by high glucose in vitro. EPC dysfunction was induced by high glucose (30 mM) treatment for 24 h. Mannitol was used as an osmolar control treatment. EPCs were transfected with mir-20a-5p or negative control (NC) inhibitor, or mir-20a-5p or NC mimic. a RT-qPCR analysis of mir-20a-5p expression. b Flow-cytometric analysis of apoptosis using annexin V/propidium iodide (PI). Annexin V + /PI + or Annexin V + /PI − (quadrants 2 and 3) cells were defined as apoptotic cells. c Protein levels of BCL-2, BAX, and cleaved-CASP3 as detected by western blotting. d Representative images showing LC3 staining in different groups of EPCs infected with GFP-RFP-LC3 adenovirus for 24 h. Scale bar: 20 μm. e Western blot analysis of LC3B-II/LC3B-I and SQSTM1/p62 levels. f The angiogenic capability of EPCs was determined by a tube formation assay. Tube length was normalized to that in the control group. Scale: 200 μm. g Protein levels of VEGF as detected by western blotting. Inh inhibito, Mic mimic, * P

Techniques Used: In Vitro, Transfection, Negative Control, Quantitative RT-PCR, Expressing, Western Blot, Staining, Infection, Tube Formation Assay

Circ-ADAM9 regulates apoptosis, autophagy, and angiogenic function of EPCs induced by high glucose. EPC dysfunction was induced by high glucose (30 mM) treatment for 24 h. Mannitol was used as an osmolar control treatment. Cells were transfected with circ-ADAM9 knockout (sh-circ-ADAM9) or overexpression (LV-circ-ADAM9) lentiviral construct or negative control lentivirus (sh-NC or EV-circ-ADAM9). a Flow-cytometric analysis of apoptosis using annexin V/PI. Annexin V + /PI + or Annexin V + /PI – (quadrants 2 and 3) cells were defined as apoptotic cells. b Protein levels of cleaved-CASP3, BAX, and BCL-2 as detected by western blotting. c Representative images showing LC3 staining in different groups of EPCs infected with GFP-RFP-LC3 adenovirus for 24 h. Scale bar: 20 μm. d Western blot analysis of LC3B-II/LC3B-I and SQSTM1/p62 levels. e The angiogenic capability of EPCs was determined by a tube formation assay. Tube length was normalized to that in the control group. Scale: 200 μm. f Protein levels of VEGF as detected by western blotting. * P
Figure Legend Snippet: Circ-ADAM9 regulates apoptosis, autophagy, and angiogenic function of EPCs induced by high glucose. EPC dysfunction was induced by high glucose (30 mM) treatment for 24 h. Mannitol was used as an osmolar control treatment. Cells were transfected with circ-ADAM9 knockout (sh-circ-ADAM9) or overexpression (LV-circ-ADAM9) lentiviral construct or negative control lentivirus (sh-NC or EV-circ-ADAM9). a Flow-cytometric analysis of apoptosis using annexin V/PI. Annexin V + /PI + or Annexin V + /PI – (quadrants 2 and 3) cells were defined as apoptotic cells. b Protein levels of cleaved-CASP3, BAX, and BCL-2 as detected by western blotting. c Representative images showing LC3 staining in different groups of EPCs infected with GFP-RFP-LC3 adenovirus for 24 h. Scale bar: 20 μm. d Western blot analysis of LC3B-II/LC3B-I and SQSTM1/p62 levels. e The angiogenic capability of EPCs was determined by a tube formation assay. Tube length was normalized to that in the control group. Scale: 200 μm. f Protein levels of VEGF as detected by western blotting. * P

Techniques Used: Transfection, Knock-Out, Over Expression, Construct, Negative Control, Western Blot, Staining, Infection, Tube Formation Assay

Related Articles

Immunohistochemistry:

Article Title: β-arrestin1 over-expression is associated with an unfavorable prognosis in lung adenocarcinomas and correlated with vascular endothelial growth factor
Article Snippet: .. Immunohistochemical staining was performed on formalin-fixed paraffin-embedded tissue sections with anti-beta-arrestin1 (E274, rabbit monoclonal; Ab-32099, Abcam), anti-VEGF (A-20, rabbit polyclonal, Santa Cruz) diluted at 1:100, 1:100 respectively. .. The immunohistochemical procedures were performed using serial sections from the same paraffin-embedded blocks by previously described methods [ , ].

Formalin-fixed Paraffin-Embedded:

Article Title: β-arrestin1 over-expression is associated with an unfavorable prognosis in lung adenocarcinomas and correlated with vascular endothelial growth factor
Article Snippet: .. Immunohistochemical staining was performed on formalin-fixed paraffin-embedded tissue sections with anti-beta-arrestin1 (E274, rabbit monoclonal; Ab-32099, Abcam), anti-VEGF (A-20, rabbit polyclonal, Santa Cruz) diluted at 1:100, 1:100 respectively. .. The immunohistochemical procedures were performed using serial sections from the same paraffin-embedded blocks by previously described methods [ , ].

Immunostaining:

Article Title: Pancreatic duct cells as a source of VEGF in mice
Article Snippet: .. Primary antibodies for immunostaining were: guinea pig polyclonal anti-insulin and anti-pancreatic polypeptide (Dako), goat polyclonal anti-VEGF-A (R & D systems, Minneapolis, MN, USA) and anti-insulin (Santa Cruz, CA, USA); rabbit polyclonal anti-somatostatin (Dako) and anti-VEGF-A (Santa Cruz); rat polyclonal anti-CD31 (BD, San Jose, CA, USA) and mouse monoclonal anti-glucagon (Sigma, St Louis, MO, USA). .. Nuclear staining was performed with Hoechst (BD).

Incubation:

Article Title: MicroRNA-15a-5p induces pulmonary artery smooth muscle cell apoptosis in a pulmonary arterial hypertension model via the VEGF/p38/MMP-2 signaling pathway
Article Snippet: .. The membranes were blocked with 5% skimmed milk in 1X Tris-buffered saline with 0.1% Tween-20 (TBST) followed by incubation overnight at 4°C with the following primary antibodies: Anti-B-cell lymphoma 2 (Bcl-2; cat. no. sc-509; 1:1,000, Santa Cruz Biotechnology, Inc.), anti-Bcl-2-associated X protein (Bax; cat. no. sc-20067; 1:1,000, Santa Cruz Biotechnology, Inc.), anti-VEGF (cat. no. sc-81670; 1:500, Santa Cruz Biotechnology, Inc.), anti-phosphorylated (p)-p38 MAPK (cat. no. sc-17852-R; 1:1,000, Santa Cruz Biotechnology, Inc.), anti-p38 MAPK (cat. no. 8690S; 1:1,000, Cell Signaling Technology, Inc.), anti-MMP-2 (cat. no. sc-53630; 1:1,000, Santa Cruz Biotechnology, Inc.) and anti-GAPDH (cat. no. sc-51631; 1:5,000, Santa Cruz Biotechnology, Inc.). .. The membranes were washed with TBST and then incubated with horseradish peroxidase-conjugated secondary antibody (cat. no. sc-2004, 1:5,000, Santa Cruz Biotechnology, Inc.) for 1 h at room temperature.

Article Title: Sarpogrelate hydrochloride ameliorates diabetic nephropathy associated with inhibition of macrophage activity and inflammatory reaction in db/db mice
Article Snippet: .. The blots were incubated with primary antibodies, including anti-Claudin1 (Cldn1), anti-NOS2, anti-PGC1ɑ, anti-Sirt1, anti-VEGF, anti-5-HT2A receptor (5-HT2AR) (Santa Cruz Biotechnology), anti-β-actin, anti-nephrin, anti-TGFβ, anti-TNFα (Abcam), anti-p-AMPK, anti-p-p38, anti-p38, anti-p-JNK, and anti-JNK, (Cell Signaling, Danvers, MA, USA) antibodies. .. Blots were visualized using a Biospectrum 600 imaging system (UVP, Upland, CA, USA).

other:

Article Title: Cyclin A1 Modulates the Expression of Vascular Endothelial Growth Factor and Promotes Hormone-Dependent Growth and Angiogenesis of Breast Cancer
Article Snippet: Polyclonal human anti-CD31 and CDK1 (BD Pharmingen), anti-β-actin, anti-VEGF, anti-VEGF-R1 and VEGF-R2 (Santa Cruz Biotechnology, CA), anti-ER-α, Ki67 (Dako, Golstrup, Denmark) and anti-cyclin D1 (Cell Signaling Technology Inc, Danvers, MA).

Western Blot:

Article Title: Activation of STAT3 in Human Gastric Cancer Cells via Interleukin (IL)-6-Type Cytokine Signaling Correlates with Clinical Implications
Article Snippet: .. Western blotting was performed using an anti-IL-6, anti-VEGF, anti-survivin, anti-STAT3 and phosphorylated STAT3 (Tyr705) antibodies (Santa Cruz Biotechnology, Santa Cruz, CA) [ ]. ..

Staining:

Article Title: β-arrestin1 over-expression is associated with an unfavorable prognosis in lung adenocarcinomas and correlated with vascular endothelial growth factor
Article Snippet: .. Immunohistochemical staining was performed on formalin-fixed paraffin-embedded tissue sections with anti-beta-arrestin1 (E274, rabbit monoclonal; Ab-32099, Abcam), anti-VEGF (A-20, rabbit polyclonal, Santa Cruz) diluted at 1:100, 1:100 respectively. .. The immunohistochemical procedures were performed using serial sections from the same paraffin-embedded blocks by previously described methods [ , ].

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    Santa Cruz Biotechnology anti vegf c
    sPLA 2 s induce the release of <t>VEGF-A</t> and <t>VEGF-C</t> from HLMs. A and B , HLMs were incubated (37°C, 24 h) with RPMI 1640 alone (Control) or with the indicated concentrations of hGIIA, hGX, or LPS. VEGF-A ( A ) and VEGF-C ( B ) release was determined by ELISA. Data are mean ± SEM of four experiments. * p
    Anti Vegf C, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 89/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Immunohistochemical localisation of <t>VEGF‐C</t> in paraffin‐embedded uterine sections of day 4 ( a – f ) and ( g – k ) of gestation. The growth factor strongly expressed in endometrial surface epithelium (ESE) and glandular epithelium (GE), and moderately in stromal cells in control females ( a – c ) on day 4 of gestation. The myometrium (M) and perimetrium (P) in control females showed moderate and strong expression of VEGF‐C, respectively. CBE administration ( d – f ) caused diffused expression in ESE, in stromal cells, and in the endometrial glands. Control females’ uteri on day 5 ( g – i ) of gestation showed strong expression in ESE, GE, certain regions of sub‐epithelial stromal (S) cells and blood vessels (BV). Administration of CBE caused structural aberration in uteri of day 5 gestation ( j – k ). Expression of VEGF‐C was diffused in the desquamated endometrial surface epithelium (DESE) and degenerated glandular epithelium (DGE). Expression was lesser in the vacuolated (V) epithelial cells. The expression of growth factor was indicated by arrow ( thick arrow ). The negative control (L) was immunostained with normal <t>IgG.</t> Original magnification ( a – l ) ×40
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    Santa Cruz Biotechnology anti vegf
    Effect of cyclin A1 expression on tumor invasion is associated with its effect on <t>VEGF</t> expression in MCF-7 cells. (A) Evaluation of cyclin A1 and VEGF expression in metastatic lesions from lymph nodes from patients with breast cancer metastasis using immunohistochemical analysis. Representative pictures show the cancer cells are strongly positive to cyclin A1 and VEGF expression. Upper panels represent cores at 20x magnificantion and lower panels represent the higher magnification (40x) of the selected areas. (B) MCF-7 cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP vectors were applied on the Matrigel-coated invasion chamber and were assessed after 48 or 72 hours. Data in graphs are the mean ± SD represents two independent experiments, each performed in duplicates. P value is indicated. (C) MDA-MB-231 cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP were applied on the Matrigel-coated invasion chamber and were analyzed after 48 or 72 hours. Data in graphs are the mean of two independent experiments, each performed in duplicate, p=0.002 for 48 h and p=0.02 for 72 h. (D) Cell cycle distribution of the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Data in graphs are the mean ± SD represents three independent experiments from flow cytometry analysis. The percentage of cells at onset of each cell cycle phase is indicated. (E) Western blot analysis shows the levels of cyclin D1 and <t>CDK1</t> protein expression in the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. (F) Representative picture shows the VEGF mRNA expression in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP (upper panel). Quantification of VEGF mRNA level in the samples is indicated. P value is shown (lower panel). (G) ELISA assay of VEGF secretion in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Mean ± SD represents three independent experiments (lower panel). Breast cancer cell lines used for these studies are T47D, MCF-7 and MDA-MB231 as indicated.
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    Santa Cruz Biotechnology rabbit anti vegf
    Endogenous neurogenesis was increased in the NSC-transplanted Tg2576 mice. ( a ) At 2.5 months after transplantation, endogenous neurogenesis was observed in the DG of hippocampus by immunohistochemisty using anti-DCX antibody. DCX-positive cells were calculated in mm 2 area of DG. Graph represents that endogenous neurogenesis was enhanced by NSC transplantation. ( b ) The levels of <t>PSA-NCAM</t> were analyzed by immunohistochemistry. In Tg-NSC group, the levels of PSA-NCAM were increased compared with the Tg-sham group. Graph represents that PSA-NCAM was enhanced by NSC transplantation. ( c ) In Tg-NSC group, the levels of PSA-NCAM and <t>VEGF</t> were increased compared with the Tg-sham group. Quantitative analysis shows that NSC transplantation significantly increased the level of PSA-NCAM and VEGF expressions. * P
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    sPLA 2 s induce the release of VEGF-A and VEGF-C from HLMs. A and B , HLMs were incubated (37°C, 24 h) with RPMI 1640 alone (Control) or with the indicated concentrations of hGIIA, hGX, or LPS. VEGF-A ( A ) and VEGF-C ( B ) release was determined by ELISA. Data are mean ± SEM of four experiments. * p

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: Production of Vascular Endothelial Growth Factors from Human Lung Macrophages Induced by Group IIA and Group X Secreted Phospholipases A2

    doi: 10.4049/jimmunol.0902501

    Figure Lengend Snippet: sPLA 2 s induce the release of VEGF-A and VEGF-C from HLMs. A and B , HLMs were incubated (37°C, 24 h) with RPMI 1640 alone (Control) or with the indicated concentrations of hGIIA, hGX, or LPS. VEGF-A ( A ) and VEGF-C ( B ) release was determined by ELISA. Data are mean ± SEM of four experiments. * p

    Article Snippet: The following were purchased: LPS (from Escherichia coli serotype 026:B6), 5′-(N-ethylcarboxamido)-adenosine (NECA), 2- p -(2-Carboxyethyl)phenethylamino-5′-N-ethylcarboxamidoadenosine , 2-Chloro-N6 -(3-iodobenzyl)-adenosine-5′-N-methyluronamide (Cl-IB-MECA), Pipes, BSA, Percoll, l -glutamine, antibiotic-antimycotic solution (10,000 UI/ml penicillin, 10 mg/ml streptomycin, and 25 μg/ml amphotericin B), Triton X-100, Polymyxin B (Sigma-Aldrich, St. Louis, MO); RPMI 1640, FCS, and guanidine hydrochloride (MP Biomedicals Europe, Illkirch, France); rabbit polyclonal anti–VEGF-B (H-70), anti–VEGF-C (H-190), and anti–VEGF-D (H-144) Abs, goat polyclonal anti-PlGF (C-20) and anti-GAPDH (V-18) Abs, normal rabbit and goat IgG Abs, HRP-conjugated donkey anti-rabbit and anti-goat IgG Abs (Santa Cruz Biotechnology, Santa Cruz, CA); goat polyclonal anti–VEGF-A Ab, human recombinant VEGF-A165 , and VEGF-A121 (R & D System, Minneapolis, MN); SB203580 (Calbiochem, La Jolla, CA); PD98059 (Cell Signaling, Beverly, MA).

    Techniques: Incubation, Enzyme-linked Immunosorbent Assay

    HLMs constitutively express different forms of VEGF. A , Expression of VEGF mRNAs. RNA extraction from resting HLMs and RT-PCR was performed as described under Materials and Methods . Specific RT-PCR amplification products for VEGFA (isoforms 189, 165, and 121), VEGFB (isoforms 186 and 167), VEGFC, VEGFD, PlGF , and GAPDH were separated on 2% agarose gel, stained with ethidium bromide, and visualized with an image analysis system. The experiment shown is representative of three separate experiments. B , Detection of VEGF proteins. HLM protein extracts (40 μg per sample) were immunoblotted with anti–VEGF-A (gel I and II), anti-PlGF (gel III), anti–VEGF-B (gel IV), anti–VEGF-C (gel V), and anti–VEGF-D (gel VI) Abs. rhVEGF-A 165 , MCF-7 cells, EBNA expressing PlGF-1, RAW 264.7 cells were used as positive controls. Stripped membranes were reprobed with anti-GAPDH Ab to confirm equal protein content of each sample. Each Western blot shown is representative of three separate experiments.

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: Production of Vascular Endothelial Growth Factors from Human Lung Macrophages Induced by Group IIA and Group X Secreted Phospholipases A2

    doi: 10.4049/jimmunol.0902501

    Figure Lengend Snippet: HLMs constitutively express different forms of VEGF. A , Expression of VEGF mRNAs. RNA extraction from resting HLMs and RT-PCR was performed as described under Materials and Methods . Specific RT-PCR amplification products for VEGFA (isoforms 189, 165, and 121), VEGFB (isoforms 186 and 167), VEGFC, VEGFD, PlGF , and GAPDH were separated on 2% agarose gel, stained with ethidium bromide, and visualized with an image analysis system. The experiment shown is representative of three separate experiments. B , Detection of VEGF proteins. HLM protein extracts (40 μg per sample) were immunoblotted with anti–VEGF-A (gel I and II), anti-PlGF (gel III), anti–VEGF-B (gel IV), anti–VEGF-C (gel V), and anti–VEGF-D (gel VI) Abs. rhVEGF-A 165 , MCF-7 cells, EBNA expressing PlGF-1, RAW 264.7 cells were used as positive controls. Stripped membranes were reprobed with anti-GAPDH Ab to confirm equal protein content of each sample. Each Western blot shown is representative of three separate experiments.

    Article Snippet: The following were purchased: LPS (from Escherichia coli serotype 026:B6), 5′-(N-ethylcarboxamido)-adenosine (NECA), 2- p -(2-Carboxyethyl)phenethylamino-5′-N-ethylcarboxamidoadenosine , 2-Chloro-N6 -(3-iodobenzyl)-adenosine-5′-N-methyluronamide (Cl-IB-MECA), Pipes, BSA, Percoll, l -glutamine, antibiotic-antimycotic solution (10,000 UI/ml penicillin, 10 mg/ml streptomycin, and 25 μg/ml amphotericin B), Triton X-100, Polymyxin B (Sigma-Aldrich, St. Louis, MO); RPMI 1640, FCS, and guanidine hydrochloride (MP Biomedicals Europe, Illkirch, France); rabbit polyclonal anti–VEGF-B (H-70), anti–VEGF-C (H-190), and anti–VEGF-D (H-144) Abs, goat polyclonal anti-PlGF (C-20) and anti-GAPDH (V-18) Abs, normal rabbit and goat IgG Abs, HRP-conjugated donkey anti-rabbit and anti-goat IgG Abs (Santa Cruz Biotechnology, Santa Cruz, CA); goat polyclonal anti–VEGF-A Ab, human recombinant VEGF-A165 , and VEGF-A121 (R & D System, Minneapolis, MN); SB203580 (Calbiochem, La Jolla, CA); PD98059 (Cell Signaling, Beverly, MA).

    Techniques: Expressing, RNA Extraction, Reverse Transcription Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis, Staining, Western Blot

    Immunohistochemical localisation of VEGF‐C in paraffin‐embedded uterine sections of day 4 ( a – f ) and ( g – k ) of gestation. The growth factor strongly expressed in endometrial surface epithelium (ESE) and glandular epithelium (GE), and moderately in stromal cells in control females ( a – c ) on day 4 of gestation. The myometrium (M) and perimetrium (P) in control females showed moderate and strong expression of VEGF‐C, respectively. CBE administration ( d – f ) caused diffused expression in ESE, in stromal cells, and in the endometrial glands. Control females’ uteri on day 5 ( g – i ) of gestation showed strong expression in ESE, GE, certain regions of sub‐epithelial stromal (S) cells and blood vessels (BV). Administration of CBE caused structural aberration in uteri of day 5 gestation ( j – k ). Expression of VEGF‐C was diffused in the desquamated endometrial surface epithelium (DESE) and degenerated glandular epithelium (DGE). Expression was lesser in the vacuolated (V) epithelial cells. The expression of growth factor was indicated by arrow ( thick arrow ). The negative control (L) was immunostained with normal IgG. Original magnification ( a – l ) ×40

    Journal: Reproductive Medicine and Biology

    Article Title: Crude bark extract of Dysozylum alliarium induces alteration in histological structures and VEGF‐C expression in uterus during days 4–7 of gestation in albino rat

    doi: 10.1007/s12522-012-0143-8

    Figure Lengend Snippet: Immunohistochemical localisation of VEGF‐C in paraffin‐embedded uterine sections of day 4 ( a – f ) and ( g – k ) of gestation. The growth factor strongly expressed in endometrial surface epithelium (ESE) and glandular epithelium (GE), and moderately in stromal cells in control females ( a – c ) on day 4 of gestation. The myometrium (M) and perimetrium (P) in control females showed moderate and strong expression of VEGF‐C, respectively. CBE administration ( d – f ) caused diffused expression in ESE, in stromal cells, and in the endometrial glands. Control females’ uteri on day 5 ( g – i ) of gestation showed strong expression in ESE, GE, certain regions of sub‐epithelial stromal (S) cells and blood vessels (BV). Administration of CBE caused structural aberration in uteri of day 5 gestation ( j – k ). Expression of VEGF‐C was diffused in the desquamated endometrial surface epithelium (DESE) and degenerated glandular epithelium (DGE). Expression was lesser in the vacuolated (V) epithelial cells. The expression of growth factor was indicated by arrow ( thick arrow ). The negative control (L) was immunostained with normal IgG. Original magnification ( a – l ) ×40

    Article Snippet: Cat No.Optitran BA‐S 85, 200 × 3 mm) were blocked for one and half hour in 3 % BSA in Tris‐buffered saline (Santa Cruz Biotechnology) and then incubated with mouse monoclonal anti VEGF IgG at 1.5 μg/ml (Santa Cruz Biotechnology, Santa Cruz, USA Cat No. sc‐7269) concentration in TBS–BSA overnight at 4 °C.

    Techniques: Immunohistochemistry, Expressing, Negative Control

    Effect of cyclin A1 expression on tumor invasion is associated with its effect on VEGF expression in MCF-7 cells. (A) Evaluation of cyclin A1 and VEGF expression in metastatic lesions from lymph nodes from patients with breast cancer metastasis using immunohistochemical analysis. Representative pictures show the cancer cells are strongly positive to cyclin A1 and VEGF expression. Upper panels represent cores at 20x magnificantion and lower panels represent the higher magnification (40x) of the selected areas. (B) MCF-7 cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP vectors were applied on the Matrigel-coated invasion chamber and were assessed after 48 or 72 hours. Data in graphs are the mean ± SD represents two independent experiments, each performed in duplicates. P value is indicated. (C) MDA-MB-231 cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP were applied on the Matrigel-coated invasion chamber and were analyzed after 48 or 72 hours. Data in graphs are the mean of two independent experiments, each performed in duplicate, p=0.002 for 48 h and p=0.02 for 72 h. (D) Cell cycle distribution of the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Data in graphs are the mean ± SD represents three independent experiments from flow cytometry analysis. The percentage of cells at onset of each cell cycle phase is indicated. (E) Western blot analysis shows the levels of cyclin D1 and CDK1 protein expression in the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. (F) Representative picture shows the VEGF mRNA expression in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP (upper panel). Quantification of VEGF mRNA level in the samples is indicated. P value is shown (lower panel). (G) ELISA assay of VEGF secretion in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Mean ± SD represents three independent experiments (lower panel). Breast cancer cell lines used for these studies are T47D, MCF-7 and MDA-MB231 as indicated.

    Journal: PLoS ONE

    Article Title: Cyclin A1 Modulates the Expression of Vascular Endothelial Growth Factor and Promotes Hormone-Dependent Growth and Angiogenesis of Breast Cancer

    doi: 10.1371/journal.pone.0072210

    Figure Lengend Snippet: Effect of cyclin A1 expression on tumor invasion is associated with its effect on VEGF expression in MCF-7 cells. (A) Evaluation of cyclin A1 and VEGF expression in metastatic lesions from lymph nodes from patients with breast cancer metastasis using immunohistochemical analysis. Representative pictures show the cancer cells are strongly positive to cyclin A1 and VEGF expression. Upper panels represent cores at 20x magnificantion and lower panels represent the higher magnification (40x) of the selected areas. (B) MCF-7 cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP vectors were applied on the Matrigel-coated invasion chamber and were assessed after 48 or 72 hours. Data in graphs are the mean ± SD represents two independent experiments, each performed in duplicates. P value is indicated. (C) MDA-MB-231 cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP were applied on the Matrigel-coated invasion chamber and were analyzed after 48 or 72 hours. Data in graphs are the mean of two independent experiments, each performed in duplicate, p=0.002 for 48 h and p=0.02 for 72 h. (D) Cell cycle distribution of the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Data in graphs are the mean ± SD represents three independent experiments from flow cytometry analysis. The percentage of cells at onset of each cell cycle phase is indicated. (E) Western blot analysis shows the levels of cyclin D1 and CDK1 protein expression in the cells that were transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. (F) Representative picture shows the VEGF mRNA expression in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP (upper panel). Quantification of VEGF mRNA level in the samples is indicated. P value is shown (lower panel). (G) ELISA assay of VEGF secretion in the cells transfected with cyclin A1pCMS-EGFP or pCMS-EGFP. Mean ± SD represents three independent experiments (lower panel). Breast cancer cell lines used for these studies are T47D, MCF-7 and MDA-MB231 as indicated.

    Article Snippet: Polyclonal human anti-CD31 and CDK1 (BD Pharmingen), anti-β-actin, anti-VEGF, anti-VEGF-R1 and VEGF-R2 (Santa Cruz Biotechnology, CA), anti-ER-α, Ki67 (Dako, Golstrup, Denmark) and anti-cyclin D1 (Cell Signaling Technology Inc, Danvers, MA).

    Techniques: Expressing, Immunohistochemistry, Transfection, Multiple Displacement Amplification, Flow Cytometry, Cytometry, Western Blot, Enzyme-linked Immunosorbent Assay

    Long-term effect of elevated level of cyclin A1 on growth and angiogenesis phenotype of xenograft tumors in mice. MCF-7 cells stable expressing pcDNA–cyclin A1 or pcDNA vectors were subcutaneous implanted into female nude mice with E2 supplementation. (A, B) Representative microphotographs of xenograft tumor sections stained with Haematoxylin and Eosin are shown. (C, D) Representative pictures show the xenograft tumors stained with antibody against human CD31, the CD31 positive vessels are indicated. The control tumor “control-pcDNA” and cyclin A1 expressing tumors “cyclin A1-pcDNA” are indicated. (E) Growth curves of the two groups of xenograft tumors are indicated. The time is indicated in x-axis and tumor volume in mm 3 is indicated in y-axis. (F) Quantification of the tumor vascularizations in cyclin A1 expressing xenograft tumors “cyclin A1-pcDNA” and in control xenograft tumors “control-pcDNA”. The numbers of CD31-positive blood vessels in the central vs. edge regions of the tumor areas are shown. P values are indicated. Mean ± SD represents three independent experiments. (G–N) Xenograft tumors from “cyclin A1-pcDNA” and “control-pcDNA” groups were immunostained with antibodies against VEGF, VEGFR1, ER-α and Ki67. The representative microphotographs are shown.

    Journal: PLoS ONE

    Article Title: Cyclin A1 Modulates the Expression of Vascular Endothelial Growth Factor and Promotes Hormone-Dependent Growth and Angiogenesis of Breast Cancer

    doi: 10.1371/journal.pone.0072210

    Figure Lengend Snippet: Long-term effect of elevated level of cyclin A1 on growth and angiogenesis phenotype of xenograft tumors in mice. MCF-7 cells stable expressing pcDNA–cyclin A1 or pcDNA vectors were subcutaneous implanted into female nude mice with E2 supplementation. (A, B) Representative microphotographs of xenograft tumor sections stained with Haematoxylin and Eosin are shown. (C, D) Representative pictures show the xenograft tumors stained with antibody against human CD31, the CD31 positive vessels are indicated. The control tumor “control-pcDNA” and cyclin A1 expressing tumors “cyclin A1-pcDNA” are indicated. (E) Growth curves of the two groups of xenograft tumors are indicated. The time is indicated in x-axis and tumor volume in mm 3 is indicated in y-axis. (F) Quantification of the tumor vascularizations in cyclin A1 expressing xenograft tumors “cyclin A1-pcDNA” and in control xenograft tumors “control-pcDNA”. The numbers of CD31-positive blood vessels in the central vs. edge regions of the tumor areas are shown. P values are indicated. Mean ± SD represents three independent experiments. (G–N) Xenograft tumors from “cyclin A1-pcDNA” and “control-pcDNA” groups were immunostained with antibodies against VEGF, VEGFR1, ER-α and Ki67. The representative microphotographs are shown.

    Article Snippet: Polyclonal human anti-CD31 and CDK1 (BD Pharmingen), anti-β-actin, anti-VEGF, anti-VEGF-R1 and VEGF-R2 (Santa Cruz Biotechnology, CA), anti-ER-α, Ki67 (Dako, Golstrup, Denmark) and anti-cyclin D1 (Cell Signaling Technology Inc, Danvers, MA).

    Techniques: Mouse Assay, Expressing, Staining

    Endogenous neurogenesis was increased in the NSC-transplanted Tg2576 mice. ( a ) At 2.5 months after transplantation, endogenous neurogenesis was observed in the DG of hippocampus by immunohistochemisty using anti-DCX antibody. DCX-positive cells were calculated in mm 2 area of DG. Graph represents that endogenous neurogenesis was enhanced by NSC transplantation. ( b ) The levels of PSA-NCAM were analyzed by immunohistochemistry. In Tg-NSC group, the levels of PSA-NCAM were increased compared with the Tg-sham group. Graph represents that PSA-NCAM was enhanced by NSC transplantation. ( c ) In Tg-NSC group, the levels of PSA-NCAM and VEGF were increased compared with the Tg-sham group. Quantitative analysis shows that NSC transplantation significantly increased the level of PSA-NCAM and VEGF expressions. * P

    Journal: Cell Death & Disease

    Article Title: Neural stem cell transplantation at critical period improves learning and memory through restoring synaptic impairment in Alzheimer's disease mouse model

    doi: 10.1038/cddis.2015.138

    Figure Lengend Snippet: Endogenous neurogenesis was increased in the NSC-transplanted Tg2576 mice. ( a ) At 2.5 months after transplantation, endogenous neurogenesis was observed in the DG of hippocampus by immunohistochemisty using anti-DCX antibody. DCX-positive cells were calculated in mm 2 area of DG. Graph represents that endogenous neurogenesis was enhanced by NSC transplantation. ( b ) The levels of PSA-NCAM were analyzed by immunohistochemistry. In Tg-NSC group, the levels of PSA-NCAM were increased compared with the Tg-sham group. Graph represents that PSA-NCAM was enhanced by NSC transplantation. ( c ) In Tg-NSC group, the levels of PSA-NCAM and VEGF were increased compared with the Tg-sham group. Quantitative analysis shows that NSC transplantation significantly increased the level of PSA-NCAM and VEGF expressions. * P

    Article Snippet: Antibodies Primary antibodies were used as follows: goat anti-DCX (1 : 100; Santa Cruz, Dallas, TX, USA), mouse anti-MAP2 (1 : 100; Millipore, Billerica, MA, USA), rabbit anti-Iba1 (1 : 2000; Wako, Richmond, VA, USA), mouse anti-6E10 (1 : 1000, Covance, San Diego, CA, USA), mouse anti-phospho tau (1 : 1000, Pierce, Rockford, IL, USA), goat anti-tau (C17) (1 : 1000, Santa Cruz), rat anti-neprilysin (1 : 500, R & D Systems, Inc.), mouse anti PSA-NCAM (1 : 2000, Millipore), rabbit anti-VEGF (1 : 1000, Santa Cruz), mouse anti-PSD-95 (1 : 2000, Thermo Scientific, Waltham, MA, USA), rabbit anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; 1 : 10000, Ab Frontier, Seoul, South Korea).

    Techniques: Mouse Assay, Transplantation Assay, Immunohistochemistry