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PeproTech recombinant human vegf
Analysis of the effect of cellular SULF‐2 levels on Wnt, <t>VEGF</t> or FGF regulation of cell invasion. Cells invading the BD Matrigel Basement Membrane Matrix are shown (a). The effect of cellular SULF‐2 level on Wnt (b), VEGF (c) or basic FGF (d) regulation of cell invasion was determined using a cell invasion assay. Fold change in cell invasion compared to non‐treated control is shown. For (C), * P
Recombinant Human Vegf, supplied by PeproTech, used in various techniques. Bioz Stars score: 86/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Impact of Sulfatase‐2 on cancer progression and prognosis in patients with renal cell carcinoma"

Article Title: Impact of Sulfatase‐2 on cancer progression and prognosis in patients with renal cell carcinoma

Journal: Cancer Science

doi: 10.1111/cas.13074

Analysis of the effect of cellular SULF‐2 levels on Wnt, VEGF or FGF regulation of cell invasion. Cells invading the BD Matrigel Basement Membrane Matrix are shown (a). The effect of cellular SULF‐2 level on Wnt (b), VEGF (c) or basic FGF (d) regulation of cell invasion was determined using a cell invasion assay. Fold change in cell invasion compared to non‐treated control is shown. For (C), * P
Figure Legend Snippet: Analysis of the effect of cellular SULF‐2 levels on Wnt, VEGF or FGF regulation of cell invasion. Cells invading the BD Matrigel Basement Membrane Matrix are shown (a). The effect of cellular SULF‐2 level on Wnt (b), VEGF (c) or basic FGF (d) regulation of cell invasion was determined using a cell invasion assay. Fold change in cell invasion compared to non‐treated control is shown. For (C), * P

Techniques Used: Invasion Assay

Analysis of the effect of cellular SULF‐2 levels on Wnt, VEGF or FGF regulation of cell viability. The effect of cellular SULF‐2 levels on Wnt (a), VEGF (b) or basic FGF (c) regulation of cell viability was determined by MTT assay. Fold change in cell viability compared to non‐treated control is shown. For (a), * P
Figure Legend Snippet: Analysis of the effect of cellular SULF‐2 levels on Wnt, VEGF or FGF regulation of cell viability. The effect of cellular SULF‐2 levels on Wnt (a), VEGF (b) or basic FGF (c) regulation of cell viability was determined by MTT assay. Fold change in cell viability compared to non‐treated control is shown. For (a), * P

Techniques Used: MTT Assay

Analysis of the effect of cellular SULF‐2 levels on VEGF and FGF signaling pathways. VEGF (a, b) or basic FGF (c, d) signaling in the RCC cell lines was assayed by western blot analysis. Activation of VEGF (a, b) or basic FGF (c, d) signaling following incubation of the indicated cells with (+) or without (−) 50 ng/mL of VEGF or 50 ng/mL of basic FGF, respectively, was determined by p‐ERK expression level (a, c). Quantification of the relative p‐ERK levels of treated versus non‐treated cells (which were assigned a value of 1) is shown (b, d). For (b), * P = 0.001, ** P
Figure Legend Snippet: Analysis of the effect of cellular SULF‐2 levels on VEGF and FGF signaling pathways. VEGF (a, b) or basic FGF (c, d) signaling in the RCC cell lines was assayed by western blot analysis. Activation of VEGF (a, b) or basic FGF (c, d) signaling following incubation of the indicated cells with (+) or without (−) 50 ng/mL of VEGF or 50 ng/mL of basic FGF, respectively, was determined by p‐ERK expression level (a, c). Quantification of the relative p‐ERK levels of treated versus non‐treated cells (which were assigned a value of 1) is shown (b, d). For (b), * P = 0.001, ** P

Techniques Used: Western Blot, Activation Assay, Incubation, Expressing

2) Product Images from "Hypoxia Enhances Proliferation of Human Adipose-Derived Stem Cells via HIF-1ɑ Activation"

Article Title: Hypoxia Enhances Proliferation of Human Adipose-Derived Stem Cells via HIF-1ɑ Activation

Journal: PLoS ONE

doi: 10.1371/journal.pone.0139890

Effects of hypoxia on mRNA expression of VEGF and FGF–2 in ASCs. After incubation for 24 hours, the mRNA expression of the indicated genes was analyzed using real-time RT-PCR. The fold-change during hypoxia is expressed relative to the level in normoxia. VEGF and FGF–2 expression in hypoxia was significantly higher than in normoxia. Data are the means ± SD. * p
Figure Legend Snippet: Effects of hypoxia on mRNA expression of VEGF and FGF–2 in ASCs. After incubation for 24 hours, the mRNA expression of the indicated genes was analyzed using real-time RT-PCR. The fold-change during hypoxia is expressed relative to the level in normoxia. VEGF and FGF–2 expression in hypoxia was significantly higher than in normoxia. Data are the means ± SD. * p

Techniques Used: Expressing, Incubation, Quantitative RT-PCR

Effects of hypoxia on the secretion of VEGF and FGF–2 from ASCs. The secretion of VEGF and FGF–2 into the medium in hypoxia was significantly higher than in normoxia. Data are the means ± SD. * p
Figure Legend Snippet: Effects of hypoxia on the secretion of VEGF and FGF–2 from ASCs. The secretion of VEGF and FGF–2 into the medium in hypoxia was significantly higher than in normoxia. Data are the means ± SD. * p

Techniques Used:

Influence of HIF–1α knockdown by siRNA in ASCs under hypoxia (A) The relative mRNA expression levels of HIF–1α in ASCs after transfection for 48 h under hypoxia. HIF–1α level was suppressed significantly compared with that in the control. (B) The relative mRNA expression levels of FGF–2 in ASCs after transfection for 48 h under hypoxia. FGF–2 level was suppressed significantly compared with that in the control. (C) The relative mRNA expression levels of VEGF in ASCs after transfection for 48 h under hypoxia. VEGF level was suppressed significantly compared with that in the control. Data are the means ± SD. *p
Figure Legend Snippet: Influence of HIF–1α knockdown by siRNA in ASCs under hypoxia (A) The relative mRNA expression levels of HIF–1α in ASCs after transfection for 48 h under hypoxia. HIF–1α level was suppressed significantly compared with that in the control. (B) The relative mRNA expression levels of FGF–2 in ASCs after transfection for 48 h under hypoxia. FGF–2 level was suppressed significantly compared with that in the control. (C) The relative mRNA expression levels of VEGF in ASCs after transfection for 48 h under hypoxia. VEGF level was suppressed significantly compared with that in the control. Data are the means ± SD. *p

Techniques Used: Expressing, Transfection

Effects of VEGF and FGF–2 on proliferation of ASCs. Proliferation was measured using Cell Counting Kit–8 1 day after addition growth factors according to the manufacturer’s instructions. Compared with the control group that was not treated with VEGF and FGF–2, no significant difference in ASC proliferation was observed in groups treated with VEGF. In contrast, FGF–2 significantly promoted cell proliferation in a dose-dependent manner.
Figure Legend Snippet: Effects of VEGF and FGF–2 on proliferation of ASCs. Proliferation was measured using Cell Counting Kit–8 1 day after addition growth factors according to the manufacturer’s instructions. Compared with the control group that was not treated with VEGF and FGF–2, no significant difference in ASC proliferation was observed in groups treated with VEGF. In contrast, FGF–2 significantly promoted cell proliferation in a dose-dependent manner.

Techniques Used: Cell Counting

3) Product Images from "Macroporous Hydrogels for Stable Sequestration and Sustained Release of Vascular Endothelial Growth Factor and Basic Fibroblast Growth Factor Using Nucleic Acid Aptamers"

Article Title: Macroporous Hydrogels for Stable Sequestration and Sustained Release of Vascular Endothelial Growth Factor and Basic Fibroblast Growth Factor Using Nucleic Acid Aptamers

Journal: ACS biomaterials science & engineering

doi: 10.1021/acsbiomaterials.9b00423

Comparison of apparent diffusivity. A) A summary of calculated diffusivity for bFGF and VEGF released from blank, single aptamer-functionalized and dual aptamer-functionalized macroporous hydrogels. B) Normalized apparent diffusivity. The calculated apparent diffusivity was divided by diffusivity of growth factors in aqueous solution (Do) for normalization.
Figure Legend Snippet: Comparison of apparent diffusivity. A) A summary of calculated diffusivity for bFGF and VEGF released from blank, single aptamer-functionalized and dual aptamer-functionalized macroporous hydrogels. B) Normalized apparent diffusivity. The calculated apparent diffusivity was divided by diffusivity of growth factors in aqueous solution (Do) for normalization.

Techniques Used:

Synthesis and characterization of dual aptamer-functionalized macroporous hydrogels. A. Schematic illustration. B. Photographic image of the entire hydrogel. C. SEM images. Blank: hydrogel without aptamers; A-VEGF: anti-VEGF aptamer-functionalized hydrogel; A-bFGF: anti-bFGF aptamer-functionalized hydrogel; Dual: hydrogel functionalized with both anti-VEGF and anti-bFGF aptamers. D. Fluorescence (left) and confocal (right) microscopy images. The anti-VEGF and anti-bFGF aptamers were stained with FAM and Cy-5 labeled complementary sequences of the two aptamers, respectively.
Figure Legend Snippet: Synthesis and characterization of dual aptamer-functionalized macroporous hydrogels. A. Schematic illustration. B. Photographic image of the entire hydrogel. C. SEM images. Blank: hydrogel without aptamers; A-VEGF: anti-VEGF aptamer-functionalized hydrogel; A-bFGF: anti-bFGF aptamer-functionalized hydrogel; Dual: hydrogel functionalized with both anti-VEGF and anti-bFGF aptamers. D. Fluorescence (left) and confocal (right) microscopy images. The anti-VEGF and anti-bFGF aptamers were stained with FAM and Cy-5 labeled complementary sequences of the two aptamers, respectively.

Techniques Used: Fluorescence, Microscopy, Staining, Labeling

Growth factor sequestration in aptamer-functionalized macroporous hydrogel. A) Secondary structure of anti-VEGF (A-VEGF) and anti-bFGF (A-bFGF) aptamers. B) Schematic illustration of growth factor loading and binding in aptamer-functionalized macroporous hydrogel. C) VEGF retention in macroporous hydrogels. D) bFGF retention in macroporous hydrogels. Blank: macroporous hydrogel without aptamers. Dual: macroporous hydrogel functionalized with both A-VEGF and A-bFGF aptamers. (NS: Non-significant. ** p
Figure Legend Snippet: Growth factor sequestration in aptamer-functionalized macroporous hydrogel. A) Secondary structure of anti-VEGF (A-VEGF) and anti-bFGF (A-bFGF) aptamers. B) Schematic illustration of growth factor loading and binding in aptamer-functionalized macroporous hydrogel. C) VEGF retention in macroporous hydrogels. D) bFGF retention in macroporous hydrogels. Blank: macroporous hydrogel without aptamers. Dual: macroporous hydrogel functionalized with both A-VEGF and A-bFGF aptamers. (NS: Non-significant. ** p

Techniques Used: Binding Assay

Evaluation of dual aptamer-functionalized macroporous hydrogel in stimulating angiogenic response in vitro and in vivo. Hydrogels were incubated in the release medium for 3 days to mimic a potential in vivo release microenvironment before conducting the studies. A) Visualization of cell migration before and after treatment for all groups. The cells were stained with Calcein AM. B) Quantitative analysis of cell migration distance. C) Image of CAM at day 3 after implantation of hydrogels (Embryonic day 11). D) Quantitative analysis of new blood vessels formed after treatment. E) H E staining of CAM treated with dual aptamer-functionalized hydrogels loaded with VEGF and bFGF (Red arrows point at small blood vessels. * hydrogel). Blank: hydrogel without aptamers (VEGF and bFGF loaded); A-VEGF: anti-VEGF aptamer-functionalized hydrogel (VEGF loaded); A-bFGF: anti-bFGF aptamer-functionalized hydrogel (bFGF loaded); Dual: hydrogel functionalized with both anti-VEGF and anti-bFGF aptamers (VEGF and bFGF loaded). (NS- Non-significant, *p
Figure Legend Snippet: Evaluation of dual aptamer-functionalized macroporous hydrogel in stimulating angiogenic response in vitro and in vivo. Hydrogels were incubated in the release medium for 3 days to mimic a potential in vivo release microenvironment before conducting the studies. A) Visualization of cell migration before and after treatment for all groups. The cells were stained with Calcein AM. B) Quantitative analysis of cell migration distance. C) Image of CAM at day 3 after implantation of hydrogels (Embryonic day 11). D) Quantitative analysis of new blood vessels formed after treatment. E) H E staining of CAM treated with dual aptamer-functionalized hydrogels loaded with VEGF and bFGF (Red arrows point at small blood vessels. * hydrogel). Blank: hydrogel without aptamers (VEGF and bFGF loaded); A-VEGF: anti-VEGF aptamer-functionalized hydrogel (VEGF loaded); A-bFGF: anti-bFGF aptamer-functionalized hydrogel (bFGF loaded); Dual: hydrogel functionalized with both anti-VEGF and anti-bFGF aptamers (VEGF and bFGF loaded). (NS- Non-significant, *p

Techniques Used: In Vitro, In Vivo, Incubation, Migration, Staining, Chick Chorioallantoic Membrane Assay

4) Product Images from "Homocysteine inhibits the viability and migration ability of human umbilical vein endothelial cells by downregulating the expression of vascular endothelial growth factor"

Article Title: Homocysteine inhibits the viability and migration ability of human umbilical vein endothelial cells by downregulating the expression of vascular endothelial growth factor

Journal: Experimental and Therapeutic Medicine

doi: 10.3892/etm.2019.8043

Hcy downregulated the expression of VEGF to inhibit the viability and migration of HUVECs. The effects of Hcy (20 mmol/l) on the (A) viability and (B) migration ability of HUVECs subsequent to VEGF expression knockdown by VEGF-siRNA were assessed by CCK-8 and Transwell migration assays, respectively. The effects of Hcy (20 mmol/l) on the (C) viability and (D) migration ability of HUVECs subsequent to addition of exogenous recombinant VEGF were examined by CCK-8 and Transwell migration assays, respectively. **P
Figure Legend Snippet: Hcy downregulated the expression of VEGF to inhibit the viability and migration of HUVECs. The effects of Hcy (20 mmol/l) on the (A) viability and (B) migration ability of HUVECs subsequent to VEGF expression knockdown by VEGF-siRNA were assessed by CCK-8 and Transwell migration assays, respectively. The effects of Hcy (20 mmol/l) on the (C) viability and (D) migration ability of HUVECs subsequent to addition of exogenous recombinant VEGF were examined by CCK-8 and Transwell migration assays, respectively. **P

Techniques Used: Expressing, Migration, CCK-8 Assay, Recombinant

Hcy downregulated the expression of VEGF in HUVECs. The effect of different concentrations of Hcy on the (A) mRNA and (B) protein expression levels of VEGF in HUVECs was detected by reverse transcription-quantitative polymerase chain reaction and western blot analysis, respectively. (C) Quantified results of western blot analysis are shown. (D) Expression of VEGF-A in the HUVEC culture supernatant treated with different concentrations of Hcy was detected by ELISA. *P
Figure Legend Snippet: Hcy downregulated the expression of VEGF in HUVECs. The effect of different concentrations of Hcy on the (A) mRNA and (B) protein expression levels of VEGF in HUVECs was detected by reverse transcription-quantitative polymerase chain reaction and western blot analysis, respectively. (C) Quantified results of western blot analysis are shown. (D) Expression of VEGF-A in the HUVEC culture supernatant treated with different concentrations of Hcy was detected by ELISA. *P

Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Western Blot, Enzyme-linked Immunosorbent Assay

5) Product Images from "Blood-brain-barrier spheroids as an in vitro screening platform for brain-penetrating agents"

Article Title: Blood-brain-barrier spheroids as an in vitro screening platform for brain-penetrating agents

Journal: Nature Communications

doi: 10.1038/ncomms15623

Surface permeability of BBB spheroid to high molecular weight dextran and intact tight junctions are modulated by VEGF. ( a ) Fluorescence images showing the expression of tight junction markers, claudin 5 and occludin (white). Nuclei of spheroids were stained with Hoechst dye (blue). Scale bar, 100 μm (× 20 objective). ( b ) Magnified fluorescence images showing claudin 5 and occluding expression. Scale bar, 100 μm (× 60 objective). ( c ) Fluorescence images showing decreased expression of tight junction marker (ZO-1: green) with increasing VEGF-A concentration (at 5, 20 and 50 ng ml −1 ) in primary HBMEC (pre-labelled with CellTracker Red dye) and ( d ) immortalized hCMEC/D3 ECs. Cell nuclei were labelled with Hoechst dye (blue). Scale bar: 50 μm in lower-magnification images; 10 μm in magnified images. ( e ) Dextran permeability assay showing that VEGF-A (at 25, 50 and 100 ng ml −1 ) increased spheroid permeability to TRITC-Dextran (155 kDa; red; 10 mg ml −1 ) using spheroids established using primary HBMEC ECs. The image panels above the graph depict a representation of how permeability was assessed. The white dotted line marks the area within the core of the spheroid, where the mean fluorescence intensity was quantified. Scale bar, 50 μm; n =8. ( f ) Dextran permeability study (as in e ) using spheroids established using immortalized hCMEC/D3 ECs. n spheroid =3–5. Both graphs show mean TRITC fluorescence intensity quantified at 88 μm depth from the surface of the spheroid with s.d. error bars (** P
Figure Legend Snippet: Surface permeability of BBB spheroid to high molecular weight dextran and intact tight junctions are modulated by VEGF. ( a ) Fluorescence images showing the expression of tight junction markers, claudin 5 and occludin (white). Nuclei of spheroids were stained with Hoechst dye (blue). Scale bar, 100 μm (× 20 objective). ( b ) Magnified fluorescence images showing claudin 5 and occluding expression. Scale bar, 100 μm (× 60 objective). ( c ) Fluorescence images showing decreased expression of tight junction marker (ZO-1: green) with increasing VEGF-A concentration (at 5, 20 and 50 ng ml −1 ) in primary HBMEC (pre-labelled with CellTracker Red dye) and ( d ) immortalized hCMEC/D3 ECs. Cell nuclei were labelled with Hoechst dye (blue). Scale bar: 50 μm in lower-magnification images; 10 μm in magnified images. ( e ) Dextran permeability assay showing that VEGF-A (at 25, 50 and 100 ng ml −1 ) increased spheroid permeability to TRITC-Dextran (155 kDa; red; 10 mg ml −1 ) using spheroids established using primary HBMEC ECs. The image panels above the graph depict a representation of how permeability was assessed. The white dotted line marks the area within the core of the spheroid, where the mean fluorescence intensity was quantified. Scale bar, 50 μm; n =8. ( f ) Dextran permeability study (as in e ) using spheroids established using immortalized hCMEC/D3 ECs. n spheroid =3–5. Both graphs show mean TRITC fluorescence intensity quantified at 88 μm depth from the surface of the spheroid with s.d. error bars (** P

Techniques Used: Permeability, Molecular Weight, Fluorescence, Expressing, Staining, Marker, Concentration Assay, FITC-Dextran Permeability Assay

6) Product Images from "Self-assembling Nanostructures to Deliver Angiogenic Factors to Pancreatic Islets"

Article Title: Self-assembling Nanostructures to Deliver Angiogenic Factors to Pancreatic Islets

Journal: Biomaterials

doi:

Fluorescence microscopy images of murine islets at Day 7 showing live (green) and dead (red) cells after culture in (a) media only (control) or media supplemented with (b) VEGF and FGF2 (GF), (c) HBPA and heparin (HBPA), and (d) HBPA, heparin, VEGF, and FGF2 (HBPA-GF). Islets in (c) and (d) appeared to have more live cells and maintained their normal rounded morphology. (e) Viability quantified using a fluorometric assay and normalized to DNA content. Viability is represented as percent of freshly isolated islets on day 0. Overall islet viability is significantly enhanced when islets are cultured in HBPA or HBPA-GF compared to GF at Day 1 and compared to control and GF at Days 3 and 7 (* p
Figure Legend Snippet: Fluorescence microscopy images of murine islets at Day 7 showing live (green) and dead (red) cells after culture in (a) media only (control) or media supplemented with (b) VEGF and FGF2 (GF), (c) HBPA and heparin (HBPA), and (d) HBPA, heparin, VEGF, and FGF2 (HBPA-GF). Islets in (c) and (d) appeared to have more live cells and maintained their normal rounded morphology. (e) Viability quantified using a fluorometric assay and normalized to DNA content. Viability is represented as percent of freshly isolated islets on day 0. Overall islet viability is significantly enhanced when islets are cultured in HBPA or HBPA-GF compared to GF at Day 1 and compared to control and GF at Days 3 and 7 (* p

Techniques Used: Fluorescence, Microscopy, Isolation, Cell Culture

7) Product Images from "Apatinib affect VEGF-mediated cell proliferation, migration, invasion via blocking VEGFR2/RAF/MEK/ERK and PI3K/AKT pathways in cholangiocarcinoma cell"

Article Title: Apatinib affect VEGF-mediated cell proliferation, migration, invasion via blocking VEGFR2/RAF/MEK/ERK and PI3K/AKT pathways in cholangiocarcinoma cell

Journal: BMC Gastroenterology

doi: 10.1186/s12876-018-0870-3

Apatinib inhibits VEGF- induced cell invasion. a Representative images of transwell (up) and quantification of invasion cell number (bottom). si-Control and and si-KDR cells grown in six-well plates were scratched and treated with PBS, VEGF (100 ng/ml), or VEGF (100 ng/ml) combined with apatinib (100 nM) for 24 h. Data are representative of three independent experiments. ** P
Figure Legend Snippet: Apatinib inhibits VEGF- induced cell invasion. a Representative images of transwell (up) and quantification of invasion cell number (bottom). si-Control and and si-KDR cells grown in six-well plates were scratched and treated with PBS, VEGF (100 ng/ml), or VEGF (100 ng/ml) combined with apatinib (100 nM) for 24 h. Data are representative of three independent experiments. ** P

Techniques Used:

a Protein expression of p-VEGFR2, VEGFR2, RAF, p-MEK, MEK, p-ERK1/2, ERK1/2, p-AKT and AKT in transfected QBC939 cells post 100 ng/ml rhVEGF or 100 ng/ml rhVEGF + 100 ng/ml apatinib treatment. GAPDH was detected as reference. b Densitometric analysis of the autoradiographic plaques of these proteins is shown on the Fig. 6a . * P
Figure Legend Snippet: a Protein expression of p-VEGFR2, VEGFR2, RAF, p-MEK, MEK, p-ERK1/2, ERK1/2, p-AKT and AKT in transfected QBC939 cells post 100 ng/ml rhVEGF or 100 ng/ml rhVEGF + 100 ng/ml apatinib treatment. GAPDH was detected as reference. b Densitometric analysis of the autoradiographic plaques of these proteins is shown on the Fig. 6a . * P

Techniques Used: Expressing, Transfection

Effects of si-KDR or si-Control on rhVEGF-induced VEGFR2 expression in QBC939 and TFK-1 cells.QBC939 and TFK-1 cells were treated with 0, 20, 50, 100 and 200 ng/ml of rhVEGF for 2 h and obtained from another 24-h incubation in medium, the mRNA level ( a ) and protein expression of VEGFR2 ( b ) was detected. GAPDH was detected as reference. c Relative cell viability of QBC939 and TFK-1 cells post 100 ng/ml rhVEGF treatment compared to control group. Data shown are means ± SD ( n = 3). * P
Figure Legend Snippet: Effects of si-KDR or si-Control on rhVEGF-induced VEGFR2 expression in QBC939 and TFK-1 cells.QBC939 and TFK-1 cells were treated with 0, 20, 50, 100 and 200 ng/ml of rhVEGF for 2 h and obtained from another 24-h incubation in medium, the mRNA level ( a ) and protein expression of VEGFR2 ( b ) was detected. GAPDH was detected as reference. c Relative cell viability of QBC939 and TFK-1 cells post 100 ng/ml rhVEGF treatment compared to control group. Data shown are means ± SD ( n = 3). * P

Techniques Used: Expressing, Incubation

Apatinib inhibits VEGF- induced cell migration and invasion ( a - b ) Cell viability of QBC939 (A) and TFK-1 ( b ) cells. Cells were treated with 100 ng/ml rhVEGF for 2 h and then treated with 10, 100, 1,000 and 10,000 nM of apatinib for 24 h. 100 ng/ml rhVEGF significantly increased relative cell viability (compared with 0 ng/ml rhVEGF+ 0 nM apatinib group)and 10–100 nM of apatinib reverses this increase (compared with 100 ng/ml rhVEGF group). Furthermore, 1,000 and 10,000 nM of apatinib inhibite relative cell viability compared with 0 ng/ml rhVEGF+ 0 nM apatinib group. Data are representative of three independent experiments.* P
Figure Legend Snippet: Apatinib inhibits VEGF- induced cell migration and invasion ( a - b ) Cell viability of QBC939 (A) and TFK-1 ( b ) cells. Cells were treated with 100 ng/ml rhVEGF for 2 h and then treated with 10, 100, 1,000 and 10,000 nM of apatinib for 24 h. 100 ng/ml rhVEGF significantly increased relative cell viability (compared with 0 ng/ml rhVEGF+ 0 nM apatinib group)and 10–100 nM of apatinib reverses this increase (compared with 100 ng/ml rhVEGF group). Furthermore, 1,000 and 10,000 nM of apatinib inhibite relative cell viability compared with 0 ng/ml rhVEGF+ 0 nM apatinib group. Data are representative of three independent experiments.* P

Techniques Used: Migration

8) Product Images from "Apatinib affect VEGF-mediated cell proliferation, migration, invasion via blocking VEGFR2/RAF/MEK/ERK and PI3K/AKT pathways in cholangiocarcinoma cell"

Article Title: Apatinib affect VEGF-mediated cell proliferation, migration, invasion via blocking VEGFR2/RAF/MEK/ERK and PI3K/AKT pathways in cholangiocarcinoma cell

Journal: BMC Gastroenterology

doi: 10.1186/s12876-018-0870-3

Apatinib inhibits VEGF- induced cell migration and invasion ( a - b ) Cell viability of QBC939 (A) and TFK-1 ( b ) cells. Cells were treated with 100 ng/ml rhVEGF for 2 h and then treated with 10, 100, 1,000 and 10,000 nM of apatinib for 24 h. 100 ng/ml rhVEGF significantly increased relative cell viability (compared with 0 ng/ml rhVEGF+ 0 nM apatinib group)and 10–100 nM of apatinib reverses this increase (compared with 100 ng/ml rhVEGF group). Furthermore, 1,000 and 10,000 nM of apatinib inhibite relative cell viability compared with 0 ng/ml rhVEGF+ 0 nM apatinib group. Data are representative of three independent experiments.* P
Figure Legend Snippet: Apatinib inhibits VEGF- induced cell migration and invasion ( a - b ) Cell viability of QBC939 (A) and TFK-1 ( b ) cells. Cells were treated with 100 ng/ml rhVEGF for 2 h and then treated with 10, 100, 1,000 and 10,000 nM of apatinib for 24 h. 100 ng/ml rhVEGF significantly increased relative cell viability (compared with 0 ng/ml rhVEGF+ 0 nM apatinib group)and 10–100 nM of apatinib reverses this increase (compared with 100 ng/ml rhVEGF group). Furthermore, 1,000 and 10,000 nM of apatinib inhibite relative cell viability compared with 0 ng/ml rhVEGF+ 0 nM apatinib group. Data are representative of three independent experiments.* P

Techniques Used: Migration

9) Product Images from "Syndecan-1 Overexpressing Mesothelioma Cells Inhibit Proliferation, Wound Healing, and Tube Formation of Endothelial Cells"

Article Title: Syndecan-1 Overexpressing Mesothelioma Cells Inhibit Proliferation, Wound Healing, and Tube Formation of Endothelial Cells

Journal: Cancers

doi: 10.3390/cancers13040655

Syndecan-1 overexpression inhibits the proliferation of Human Umbilical Vein Endothelial Cells (HUVEC) cells. Proliferation of HUVEC cells is significantly inhibited after incubation with conditioned medium from SDC-1 over-expressing mesothelioma cells supplemented with 10 ng/mL Vascular Endothelial Growth Factor (VEGF) compared to the controls. Black bars denote HUVEC cells treated with control medium and gray bars show HUVEC cells treated with conditioned medium from SDC-1 over-expressing cells. Proliferation was measured using WST1 proliferation assay. Values represent mean cell number ± SEM, obtained from three independent experiments in triplicates. All cell numbers were normalized to the initial cell numbers after four hours incubation with conditioned medium. Paired t -test was performed to test the statistical significance. Asterisks (*) indicate statistically significant differences (* = p ≤ 0.05).
Figure Legend Snippet: Syndecan-1 overexpression inhibits the proliferation of Human Umbilical Vein Endothelial Cells (HUVEC) cells. Proliferation of HUVEC cells is significantly inhibited after incubation with conditioned medium from SDC-1 over-expressing mesothelioma cells supplemented with 10 ng/mL Vascular Endothelial Growth Factor (VEGF) compared to the controls. Black bars denote HUVEC cells treated with control medium and gray bars show HUVEC cells treated with conditioned medium from SDC-1 over-expressing cells. Proliferation was measured using WST1 proliferation assay. Values represent mean cell number ± SEM, obtained from three independent experiments in triplicates. All cell numbers were normalized to the initial cell numbers after four hours incubation with conditioned medium. Paired t -test was performed to test the statistical significance. Asterisks (*) indicate statistically significant differences (* = p ≤ 0.05).

Techniques Used: Over Expression, Incubation, Expressing, Proliferation Assay

10) Product Images from "Procyanidin B2 inhibits angiogenesis and cell growth in oral squamous cell carcinoma cells through the vascular endothelial growth factor (VEGF)/VEGF receptor 2 (VEGFR2) pathway"

Article Title: Procyanidin B2 inhibits angiogenesis and cell growth in oral squamous cell carcinoma cells through the vascular endothelial growth factor (VEGF)/VEGF receptor 2 (VEGFR2) pathway

Journal: Bioengineered

doi: 10.1080/21655979.2022.2033013

Activation of VEGF/VEGFR2 signaling reduced the effect of PB2 on growth and metastasis of OSCC cells. (a) The viability of SCC-25 cells treated with PB2 with or without VEGF was detected by CCK-8 assay. The apoptosis (B/C) and related proteins (d) in SCC-25 cells treated with PB2 with or without VEGF were respectively analyzed by Tunel assay and Western blot. The migration (e) and invasion (f) of SCC-25 cells treated with PB2 with or without VEGF were detected by wound healing assay and transwell assay. The expression of metastasis associated proteins (g) and EMT related proteins (h) was analyzed by Western.
Figure Legend Snippet: Activation of VEGF/VEGFR2 signaling reduced the effect of PB2 on growth and metastasis of OSCC cells. (a) The viability of SCC-25 cells treated with PB2 with or without VEGF was detected by CCK-8 assay. The apoptosis (B/C) and related proteins (d) in SCC-25 cells treated with PB2 with or without VEGF were respectively analyzed by Tunel assay and Western blot. The migration (e) and invasion (f) of SCC-25 cells treated with PB2 with or without VEGF were detected by wound healing assay and transwell assay. The expression of metastasis associated proteins (g) and EMT related proteins (h) was analyzed by Western.

Techniques Used: Activation Assay, CCK-8 Assay, TUNEL Assay, Western Blot, Migration, Wound Healing Assay, Transwell Assay, Expressing

PB2 inhibited VEGF/VEGFR2 signaling and tumor angiogenesis in OSCC. (a) The related genes of PB2 were analyzed by STTICH database. (b/c) The expression of VEGF/VEGFR2 signaling in SCC-25 cells treated with PB2 was analyzed by Western blot. (d) The angiogenesis of SCC-25 cells treated with PB2 was detected by tube formation assay. *P
Figure Legend Snippet: PB2 inhibited VEGF/VEGFR2 signaling and tumor angiogenesis in OSCC. (a) The related genes of PB2 were analyzed by STTICH database. (b/c) The expression of VEGF/VEGFR2 signaling in SCC-25 cells treated with PB2 was analyzed by Western blot. (d) The angiogenesis of SCC-25 cells treated with PB2 was detected by tube formation assay. *P

Techniques Used: Expressing, Western Blot, Tube Formation Assay

11) Product Images from "Arnebin-1 promotes angiogenesis by inducing eNOS, VEGF and HIF-1α expression through the PI3K-dependent pathway"

Article Title: Arnebin-1 promotes angiogenesis by inducing eNOS, VEGF and HIF-1α expression through the PI3K-dependent pathway

Journal: International Journal of Molecular Medicine

doi: 10.3892/ijmm.2015.2292

Hypoxia-inducible factor (HIF)-1α is essential for arnebin-1-induced (A) cell proliferation, (B and C) cell migration and (D–E) tube formation of human umbilical vein endothelial cells (HUVECs) in the presence of vascular endothelial growth factor (VEGF). HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 24 h. (A) Cell proliferation was assessed by MTT assay. HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 8 h. (B and C) Cell migration was assessed by Transwell assay. HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 12 h. (D–E) HUVECs were plated on Matrigel to form tubular structures. Bars represent the means ± SEM. * P
Figure Legend Snippet: Hypoxia-inducible factor (HIF)-1α is essential for arnebin-1-induced (A) cell proliferation, (B and C) cell migration and (D–E) tube formation of human umbilical vein endothelial cells (HUVECs) in the presence of vascular endothelial growth factor (VEGF). HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 24 h. (A) Cell proliferation was assessed by MTT assay. HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 8 h. (B and C) Cell migration was assessed by Transwell assay. HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 12 h. (D–E) HUVECs were plated on Matrigel to form tubular structures. Bars represent the means ± SEM. * P

Techniques Used: Migration, MTT Assay, Transwell Assay

Arnebin-1 promotes vascular endothelial growth factor (VEGF) receptor 2 (VEGFR2) kinase activity and its downstream signaling molecules. (A) Arnebin-1 increased the phosphorylation of VEGFR2 induced by VEGF in human umbilical vein endothelial cells (HUVECs). Total protein was isolated and subjected to western blot analysis. Upper panel shows representative blots of the protein levels of phosphorylated (p-)VEGFR2 and total (t-)VEGFR2 proteins. Lower panel shows the quantification of the p-VEGFR2 protein level. (B–D) Arnebin-1 also increased VEGFR2-mediated protein kinase activation of focal adhesion kinase (FAK), extracellular signal-regulated kinase (Erk) and Src. (B) Upper panel shows representative blots of the protein levels of p-FAK and t-FAK. Lower panel shows the quantification of the p-FAK protein level. (C) Upper panel shows the representative blots of the levels of p-Erk and t-Erk proteins. Lower panel shows the quantification of the p-Erk protein level. (D) Upper panel shows representative blots of the protein levels of p-Src and t-Src proteins. Lower panel shows the quantification of the p-Src protein level. (E) Diagram of signaling pathways involved in arnebin-1-induced angiogenesis. α-tubulin was used as a loading control. Bars represent the means ± SEM. * P
Figure Legend Snippet: Arnebin-1 promotes vascular endothelial growth factor (VEGF) receptor 2 (VEGFR2) kinase activity and its downstream signaling molecules. (A) Arnebin-1 increased the phosphorylation of VEGFR2 induced by VEGF in human umbilical vein endothelial cells (HUVECs). Total protein was isolated and subjected to western blot analysis. Upper panel shows representative blots of the protein levels of phosphorylated (p-)VEGFR2 and total (t-)VEGFR2 proteins. Lower panel shows the quantification of the p-VEGFR2 protein level. (B–D) Arnebin-1 also increased VEGFR2-mediated protein kinase activation of focal adhesion kinase (FAK), extracellular signal-regulated kinase (Erk) and Src. (B) Upper panel shows representative blots of the protein levels of p-FAK and t-FAK. Lower panel shows the quantification of the p-FAK protein level. (C) Upper panel shows the representative blots of the levels of p-Erk and t-Erk proteins. Lower panel shows the quantification of the p-Erk protein level. (D) Upper panel shows representative blots of the protein levels of p-Src and t-Src proteins. Lower panel shows the quantification of the p-Src protein level. (E) Diagram of signaling pathways involved in arnebin-1-induced angiogenesis. α-tubulin was used as a loading control. Bars represent the means ± SEM. * P

Techniques Used: Activity Assay, Isolation, Western Blot, Activation Assay

The expression levels of endothelial nitric oxide synthase (eNOS), vascular endothelial growth factor (VEGF) and hypoxia-inducible factor (HIF)-1α were increased by arnebin-1 in a phosphoinositide 3-kinase (PI3K)-dependent manner. (A–C) Human umbilical vein endothelial cells (HUVECs) were treated with arnebin-1 only at various concentrations (10 −3 , 10 −2 and 10 −1 µ M) for 24 h. Cell lysates were subjected to western blot analysis. (A) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (B) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. (C) The secretion level of VEGF in the culture supernatants was determined by ELISA. (D) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (E–H) HUVECs were treated with or without LY294002 for 1 h, and then stimulated with arnebin-1 in the presence or absence of VEGF for 24 h. (E) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (F) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (G) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. (H) The secretion level of VEGF in the culture supernatants was determined by ELISA. Bars represent the means ± SEM. * P
Figure Legend Snippet: The expression levels of endothelial nitric oxide synthase (eNOS), vascular endothelial growth factor (VEGF) and hypoxia-inducible factor (HIF)-1α were increased by arnebin-1 in a phosphoinositide 3-kinase (PI3K)-dependent manner. (A–C) Human umbilical vein endothelial cells (HUVECs) were treated with arnebin-1 only at various concentrations (10 −3 , 10 −2 and 10 −1 µ M) for 24 h. Cell lysates were subjected to western blot analysis. (A) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (B) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. (C) The secretion level of VEGF in the culture supernatants was determined by ELISA. (D) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (E–H) HUVECs were treated with or without LY294002 for 1 h, and then stimulated with arnebin-1 in the presence or absence of VEGF for 24 h. (E) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (F) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (G) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. (H) The secretion level of VEGF in the culture supernatants was determined by ELISA. Bars represent the means ± SEM. * P

Techniques Used: Expressing, Western Blot, Enzyme-linked Immunosorbent Assay

(A) Structure of arnebin-1 [5,8-dihydroxy-2-(1′-b,b-dimethylaryoxy-4′-methylpent-3-enyl)-1,4-naphthoquinone]. (B) Human umbilical vein endothelial cells (HUVECs) were treated with arnebin-1 only at various concentrations for 24 h. Cell lysates were subjected to western blot analysis. Upper panel shows representative blots of the protein expression of proliferating cell nuclear antigen (PCNA). Lower panel shows the quantification of the PCNA protein level. (C) The HUVECs were treated with arnebin-1 at various concentrations in the absence or presence of vascular endothelial growth factor (VEGF; 1 ng/ml) for 24 h. Cell lysates were subjected to western blot analysis. Upper panel shows representative blots of the protein expression of PCNA. Lower panel shows the quantification of the PCNA protein level. α-tubulin was used as a loading control. Bars represent the means ± SEM. * P
Figure Legend Snippet: (A) Structure of arnebin-1 [5,8-dihydroxy-2-(1′-b,b-dimethylaryoxy-4′-methylpent-3-enyl)-1,4-naphthoquinone]. (B) Human umbilical vein endothelial cells (HUVECs) were treated with arnebin-1 only at various concentrations for 24 h. Cell lysates were subjected to western blot analysis. Upper panel shows representative blots of the protein expression of proliferating cell nuclear antigen (PCNA). Lower panel shows the quantification of the PCNA protein level. (C) The HUVECs were treated with arnebin-1 at various concentrations in the absence or presence of vascular endothelial growth factor (VEGF; 1 ng/ml) for 24 h. Cell lysates were subjected to western blot analysis. Upper panel shows representative blots of the protein expression of PCNA. Lower panel shows the quantification of the PCNA protein level. α-tubulin was used as a loading control. Bars represent the means ± SEM. * P

Techniques Used: Western Blot, Expressing

Schematic diagram of the mechanisms through which arnebin-1 promotes vascularization and wound healing. Arnebin-1 treatment leads to the accumulation of hypoxia-inducible factor (HIF)-1α, and the consequent upregulation of VEGF and endothelial nitric oxide synthase (eNOS). The expression of HIF-1α target genes in turn promotes neovascularization in diabetic wounds through angiogenesis and vasculogenesis.
Figure Legend Snippet: Schematic diagram of the mechanisms through which arnebin-1 promotes vascularization and wound healing. Arnebin-1 treatment leads to the accumulation of hypoxia-inducible factor (HIF)-1α, and the consequent upregulation of VEGF and endothelial nitric oxide synthase (eNOS). The expression of HIF-1α target genes in turn promotes neovascularization in diabetic wounds through angiogenesis and vasculogenesis.

Techniques Used: Expressing

Effects of arnebin-1 on the hypoxia-inducible factor (HIF)-1α, vascular endothelial growth factor (VEGF) and endothelial nitric oxide synthase (eNOS) expression levels in diabetic rats. (A–C) Effects of arnebin-1 on the protein expression levels of HIF-1α, VEGF and eNOS. (A) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (B) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (C) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. Bars represent the means ± SEM. * P
Figure Legend Snippet: Effects of arnebin-1 on the hypoxia-inducible factor (HIF)-1α, vascular endothelial growth factor (VEGF) and endothelial nitric oxide synthase (eNOS) expression levels in diabetic rats. (A–C) Effects of arnebin-1 on the protein expression levels of HIF-1α, VEGF and eNOS. (A) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (B) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (C) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. Bars represent the means ± SEM. * P

Techniques Used: Expressing

12) Product Images from "Interruption of tumor dormancy by a transient angiogenic burst within the tumor microenvironment"

Article Title: Interruption of tumor dormancy by a transient angiogenic burst within the tumor microenvironment

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.0506200103

Effects of angiogenic factors on MOLT-3 cell engraftment. ( A ) Effect of angiogenic factors on MOLT-3 tumorigenicity in NOD/SCID mice. MOLT-3 cells (5 × 10 6 cells per injection, n = 6 mice per group) were injected in Matrigel either without (▿) or with (▾) bFGF (100 ng/ml), VEGF (•) (100 ng/ml), or irradiated KS-IMM cells (○). The tumor volume (mm 3 ) was plotted as a function of time (weeks after transplantation). ( B ) Immunohistochemical analysis of 7-week-old dormant and progressively growing tumors. Shown is a representative CD31 staining of microvessels of dormant and progressively growing MOLT-3 tumors, induced by KS-IMM cell coadministration, recombinant VEGF, or bFGF. (Scale bars, 100 μm.) ( C ) Tumor growth curves of retroviral-vector-transduced MOLT-3 cells in NOD/SCID mice. Parental MOLT-3 cells or its derivatives, releasing either bFGF (▾) or VEGF (•) (5 × 10 6 cells per injection, n = 6 mice per group), were injected either alone or in combination with irradiated MOLT-3-GFP + (■), MOLT-3-bFGF (▿), or MOLT-3-VEGF (○) cells in a 1:1 ratio. The tumor volume was plotted as a function of time (weeks after transplantation). The tumor volumes of the experimental groups (▾), (•), (▿), and (○) evaluated 6 weeks after the beginning of the experiment significantly differed ( P = 0.021) compared with the control groups. ( D ) Hematoxylin and eosin staining of tumors generated in the presence of sustained (MOLT-3bFGF) or short-term (MOLT-3 plus MOLT-3bFGF irr) bFGF release; one representative sample of three analyzed is shown. (Scale bars, 100 μm.)
Figure Legend Snippet: Effects of angiogenic factors on MOLT-3 cell engraftment. ( A ) Effect of angiogenic factors on MOLT-3 tumorigenicity in NOD/SCID mice. MOLT-3 cells (5 × 10 6 cells per injection, n = 6 mice per group) were injected in Matrigel either without (▿) or with (▾) bFGF (100 ng/ml), VEGF (•) (100 ng/ml), or irradiated KS-IMM cells (○). The tumor volume (mm 3 ) was plotted as a function of time (weeks after transplantation). ( B ) Immunohistochemical analysis of 7-week-old dormant and progressively growing tumors. Shown is a representative CD31 staining of microvessels of dormant and progressively growing MOLT-3 tumors, induced by KS-IMM cell coadministration, recombinant VEGF, or bFGF. (Scale bars, 100 μm.) ( C ) Tumor growth curves of retroviral-vector-transduced MOLT-3 cells in NOD/SCID mice. Parental MOLT-3 cells or its derivatives, releasing either bFGF (▾) or VEGF (•) (5 × 10 6 cells per injection, n = 6 mice per group), were injected either alone or in combination with irradiated MOLT-3-GFP + (■), MOLT-3-bFGF (▿), or MOLT-3-VEGF (○) cells in a 1:1 ratio. The tumor volume was plotted as a function of time (weeks after transplantation). The tumor volumes of the experimental groups (▾), (•), (▿), and (○) evaluated 6 weeks after the beginning of the experiment significantly differed ( P = 0.021) compared with the control groups. ( D ) Hematoxylin and eosin staining of tumors generated in the presence of sustained (MOLT-3bFGF) or short-term (MOLT-3 plus MOLT-3bFGF irr) bFGF release; one representative sample of three analyzed is shown. (Scale bars, 100 μm.)

Techniques Used: Mouse Assay, Injection, Irradiation, Transplantation Assay, Immunohistochemistry, Staining, Recombinant, Plasmid Preparation, Generated

13) Product Images from "Apatinib affect VEGF-mediated cell proliferation, migration, invasion via blocking VEGFR2/RAF/MEK/ERK and PI3K/AKT pathways in cholangiocarcinoma cell"

Article Title: Apatinib affect VEGF-mediated cell proliferation, migration, invasion via blocking VEGFR2/RAF/MEK/ERK and PI3K/AKT pathways in cholangiocarcinoma cell

Journal: BMC Gastroenterology

doi: 10.1186/s12876-018-0870-3

Apatinib inhibits VEGF- induced cell migration and invasion ( a - b ) Cell viability of QBC939 (A) and TFK-1 ( b ) cells. Cells were treated with 100 ng/ml rhVEGF for 2 h and then treated with 10, 100, 1,000 and 10,000 nM of apatinib for 24 h. 100 ng/ml rhVEGF significantly increased relative cell viability (compared with 0 ng/ml rhVEGF+ 0 nM apatinib group)and 10–100 nM of apatinib reverses this increase (compared with 100 ng/ml rhVEGF group). Furthermore, 1,000 and 10,000 nM of apatinib inhibite relative cell viability compared with 0 ng/ml rhVEGF+ 0 nM apatinib group. Data are representative of three independent experiments.* P
Figure Legend Snippet: Apatinib inhibits VEGF- induced cell migration and invasion ( a - b ) Cell viability of QBC939 (A) and TFK-1 ( b ) cells. Cells were treated with 100 ng/ml rhVEGF for 2 h and then treated with 10, 100, 1,000 and 10,000 nM of apatinib for 24 h. 100 ng/ml rhVEGF significantly increased relative cell viability (compared with 0 ng/ml rhVEGF+ 0 nM apatinib group)and 10–100 nM of apatinib reverses this increase (compared with 100 ng/ml rhVEGF group). Furthermore, 1,000 and 10,000 nM of apatinib inhibite relative cell viability compared with 0 ng/ml rhVEGF+ 0 nM apatinib group. Data are representative of three independent experiments.* P

Techniques Used: Migration

14) Product Images from "P18 peptide, a functional fragment of pigment epithelial-derived factor, inhibits angiogenesis in hepatocellular carcinoma via modulating VEGF/VEGFR2 signalling pathway"

Article Title: P18 peptide, a functional fragment of pigment epithelial-derived factor, inhibits angiogenesis in hepatocellular carcinoma via modulating VEGF/VEGFR2 signalling pathway

Journal: Oncology Reports

doi: 10.3892/or.2017.5719

P18 peptide blocked VEGF/VEGFR2 signalling pathway and it induced the PI3K/Akt cascade. (A) P18 peptide inhibited the phosphorylation of VEGFR2 in a manner similar to that of SU1498. Data represent relative band density and percent of p-VEGFR2/VEGFR2 expressed as the mean ± SD. (B and C) The P18 peptide inhibited VEGF-induced phosphorylation of PI3K and Akt, which could be reversed by IGF-1. The data represent relative band density and are normalized to GAPDH (mean ± SD, ***P
Figure Legend Snippet: P18 peptide blocked VEGF/VEGFR2 signalling pathway and it induced the PI3K/Akt cascade. (A) P18 peptide inhibited the phosphorylation of VEGFR2 in a manner similar to that of SU1498. Data represent relative band density and percent of p-VEGFR2/VEGFR2 expressed as the mean ± SD. (B and C) The P18 peptide inhibited VEGF-induced phosphorylation of PI3K and Akt, which could be reversed by IGF-1. The data represent relative band density and are normalized to GAPDH (mean ± SD, ***P

Techniques Used:

15) Product Images from "Syndecan-1 Overexpressing Mesothelioma Cells Inhibit Proliferation, Wound Healing, and Tube Formation of Endothelial Cells"

Article Title: Syndecan-1 Overexpressing Mesothelioma Cells Inhibit Proliferation, Wound Healing, and Tube Formation of Endothelial Cells

Journal: Cancers

doi: 10.3390/cancers13040655

Syndecan-1 overexpression inhibits the proliferation of Human Umbilical Vein Endothelial Cells (HUVEC) cells. Proliferation of HUVEC cells is significantly inhibited after incubation with conditioned medium from SDC-1 over-expressing mesothelioma cells supplemented with 10 ng/mL Vascular Endothelial Growth Factor (VEGF) compared to the controls. Black bars denote HUVEC cells treated with control medium and gray bars show HUVEC cells treated with conditioned medium from SDC-1 over-expressing cells. Proliferation was measured using WST1 proliferation assay. Values represent mean cell number ± SEM, obtained from three independent experiments in triplicates. All cell numbers were normalized to the initial cell numbers after four hours incubation with conditioned medium. Paired t -test was performed to test the statistical significance. Asterisks (*) indicate statistically significant differences (* = p ≤ 0.05).
Figure Legend Snippet: Syndecan-1 overexpression inhibits the proliferation of Human Umbilical Vein Endothelial Cells (HUVEC) cells. Proliferation of HUVEC cells is significantly inhibited after incubation with conditioned medium from SDC-1 over-expressing mesothelioma cells supplemented with 10 ng/mL Vascular Endothelial Growth Factor (VEGF) compared to the controls. Black bars denote HUVEC cells treated with control medium and gray bars show HUVEC cells treated with conditioned medium from SDC-1 over-expressing cells. Proliferation was measured using WST1 proliferation assay. Values represent mean cell number ± SEM, obtained from three independent experiments in triplicates. All cell numbers were normalized to the initial cell numbers after four hours incubation with conditioned medium. Paired t -test was performed to test the statistical significance. Asterisks (*) indicate statistically significant differences (* = p ≤ 0.05).

Techniques Used: Over Expression, Incubation, Expressing, Proliferation Assay

Prognostic value of SDC-1 and VEGF. Soluble VEGF correlates to soluble SDC-1 levels in pleural effusions and has prognostic roles in patients with malignant mesothelioma. ( A ) Spearman correlation analysis was used to assess the relationship between soluble VEGF and SDC-1 in paired sample effusions from 38 mesothelioma patients. ( B ) Cutoffs for “high” (n = 19) and “low” (n = 11) VEGF were identified by the online web application Cutoff Finder (2.125 ng/mL). The effect is presented in corresponding Kaplan–Meier plots. X axis is time in months and Y axis is survival percentage. p value is
Figure Legend Snippet: Prognostic value of SDC-1 and VEGF. Soluble VEGF correlates to soluble SDC-1 levels in pleural effusions and has prognostic roles in patients with malignant mesothelioma. ( A ) Spearman correlation analysis was used to assess the relationship between soluble VEGF and SDC-1 in paired sample effusions from 38 mesothelioma patients. ( B ) Cutoffs for “high” (n = 19) and “low” (n = 11) VEGF were identified by the online web application Cutoff Finder (2.125 ng/mL). The effect is presented in corresponding Kaplan–Meier plots. X axis is time in months and Y axis is survival percentage. p value is

Techniques Used:

16) Product Images from "Sinensetin suppresses angiogenesis in liver cancer by targeting the VEGF/VEGFR2/AKT signaling pathway"

Article Title: Sinensetin suppresses angiogenesis in liver cancer by targeting the VEGF/VEGFR2/AKT signaling pathway

Journal: Experimental and Therapeutic Medicine

doi: 10.3892/etm.2022.11287

Schematic diagram summarizing the signaling pathway by which SIN inhibits liver cancer angiogenesis. SIN represses VEGF expression by downregulating HIF-1α expression. SIN inhibits VEGF-induced VEGFR2 phosphorylation and sequentially inhibits the levels of p-AKT leading to inhibition of EC proliferation, migration, tube formation and angiogenesis. SIN, sinensetin; VEGF, vascular endothelial growth factor; HIF, hypoxia-inducible factors; VEGFR, vascular endothelial growth factor receptor; EC, endothelial cell; p, phosphorylated.
Figure Legend Snippet: Schematic diagram summarizing the signaling pathway by which SIN inhibits liver cancer angiogenesis. SIN represses VEGF expression by downregulating HIF-1α expression. SIN inhibits VEGF-induced VEGFR2 phosphorylation and sequentially inhibits the levels of p-AKT leading to inhibition of EC proliferation, migration, tube formation and angiogenesis. SIN, sinensetin; VEGF, vascular endothelial growth factor; HIF, hypoxia-inducible factors; VEGFR, vascular endothelial growth factor receptor; EC, endothelial cell; p, phosphorylated.

Techniques Used: Expressing, Inhibition, Migration

SIN inhibits phosphorylation of VEGFR2 and AKT in HUVECs. (A) SIN inhibits the phosphorylation of VEGFR2 induced by VEGF. The expression levels of p-VEGFR2 and VEGFR2 in HUVECs treated with SIN were analyzed by western blotting. n=3, * P
Figure Legend Snippet: SIN inhibits phosphorylation of VEGFR2 and AKT in HUVECs. (A) SIN inhibits the phosphorylation of VEGFR2 induced by VEGF. The expression levels of p-VEGFR2 and VEGFR2 in HUVECs treated with SIN were analyzed by western blotting. n=3, * P

Techniques Used: Expressing, Western Blot

SIN suppresses angiogenesis by inhibiting the activity of VEGF in HepG2/C3A cells. (A) SIN down regulated the expression levels of VEGF and HIF-1α under hypoxic conditions as determined by western blot analysis. n=3, * P
Figure Legend Snippet: SIN suppresses angiogenesis by inhibiting the activity of VEGF in HepG2/C3A cells. (A) SIN down regulated the expression levels of VEGF and HIF-1α under hypoxic conditions as determined by western blot analysis. n=3, * P

Techniques Used: Activity Assay, Expressing, Western Blot

17) Product Images from "Endoglin, a novel biomarker and therapeutical target to prevent malignant peripheral nerve sheath tumor growth and metastasis"

Article Title: Endoglin, a novel biomarker and therapeutical target to prevent malignant peripheral nerve sheath tumor growth and metastasis

Journal: bioRxiv

doi: 10.1101/2022.08.12.503580

Dual inhibition of ENG and MEK efficiently blocks ENG-Smad1/5 and MAPK/ERK pathway activation in ST88-14 cells. A, B) Western blot analysis ( A ) and quantification ( B ) of ENG expression and Smad1/5, MEK and ERK phosphorylation in ST88-14 cells stimulated with BMP-9/VEGF in the presence of IgG control, the anti-human ENG mAb TRC105, the MEKi PD-0325901 (PD-901) or the combination of both drugs (combo). Cells without neither the pre-treatment nor BMP-9/VEGF stimulation were used as a control. Phosphorylated protein levels were normalized to the corresponding total protein levels. Data are presented as the fold change compared to IgG. Mean ± s.e.m. of at least four biological replicates; * P
Figure Legend Snippet: Dual inhibition of ENG and MEK efficiently blocks ENG-Smad1/5 and MAPK/ERK pathway activation in ST88-14 cells. A, B) Western blot analysis ( A ) and quantification ( B ) of ENG expression and Smad1/5, MEK and ERK phosphorylation in ST88-14 cells stimulated with BMP-9/VEGF in the presence of IgG control, the anti-human ENG mAb TRC105, the MEKi PD-0325901 (PD-901) or the combination of both drugs (combo). Cells without neither the pre-treatment nor BMP-9/VEGF stimulation were used as a control. Phosphorylated protein levels were normalized to the corresponding total protein levels. Data are presented as the fold change compared to IgG. Mean ± s.e.m. of at least four biological replicates; * P

Techniques Used: Inhibition, Activation Assay, Western Blot, Expressing

Dual inhibition of ENG and MEK cooperates to reduce Smad1/5 and MAPK/ERK signaling activity, proliferation and angiogenesis. A, B) Representative Western blot imagesp > ( A ) and quantification ( B ) of ENG expression and Smad1/5, MEK and ERK activation in STS26T cells pre-treated overnight with a IgG control, the anti-human ENG mAb TRC105 alone, the MEKi PD-0325901 (PD-901) alone or the combination of both drugs (combo) and then stimulated with BMP-9/VEGF for 1 hour. Cells without neither the pre-treatment nor BMP-9/VEGF stimulation were used as a control. Phosphorylated protein levels were normalized to the corresponding total protein levels. Data are presented as the fold change compared to IgG. Mean ± s.e.m. of four biological replicates; * P
Figure Legend Snippet: Dual inhibition of ENG and MEK cooperates to reduce Smad1/5 and MAPK/ERK signaling activity, proliferation and angiogenesis. A, B) Representative Western blot imagesp > ( A ) and quantification ( B ) of ENG expression and Smad1/5, MEK and ERK activation in STS26T cells pre-treated overnight with a IgG control, the anti-human ENG mAb TRC105 alone, the MEKi PD-0325901 (PD-901) alone or the combination of both drugs (combo) and then stimulated with BMP-9/VEGF for 1 hour. Cells without neither the pre-treatment nor BMP-9/VEGF stimulation were used as a control. Phosphorylated protein levels were normalized to the corresponding total protein levels. Data are presented as the fold change compared to IgG. Mean ± s.e.m. of four biological replicates; * P

Techniques Used: Inhibition, Activity Assay, Western Blot, Expressing, Activation Assay

18) Product Images from "Arnebin-1 promotes angiogenesis by inducing eNOS, VEGF and HIF-1α expression through the PI3K-dependent pathway"

Article Title: Arnebin-1 promotes angiogenesis by inducing eNOS, VEGF and HIF-1α expression through the PI3K-dependent pathway

Journal: International Journal of Molecular Medicine

doi: 10.3892/ijmm.2015.2292

Hypoxia-inducible factor (HIF)-1α is essential for arnebin-1-induced (A) cell proliferation, (B and C) cell migration and (D–E) tube formation of human umbilical vein endothelial cells (HUVECs) in the presence of vascular endothelial growth factor (VEGF). HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 24 h. (A) Cell proliferation was assessed by MTT assay. HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 8 h. (B and C) Cell migration was assessed by Transwell assay. HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 12 h. (D–E) HUVECs were plated on Matrigel to form tubular structures. Bars represent the means ± SEM. * P
Figure Legend Snippet: Hypoxia-inducible factor (HIF)-1α is essential for arnebin-1-induced (A) cell proliferation, (B and C) cell migration and (D–E) tube formation of human umbilical vein endothelial cells (HUVECs) in the presence of vascular endothelial growth factor (VEGF). HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 24 h. (A) Cell proliferation was assessed by MTT assay. HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 8 h. (B and C) Cell migration was assessed by Transwell assay. HUVECs were treated with or without LY294002 (2 µ M) for 1 h, and then stimulated with arnebin-1 (10 −1 µ M) in the presence or absence of VEGF (1 ng/ml) for 12 h. (D–E) HUVECs were plated on Matrigel to form tubular structures. Bars represent the means ± SEM. * P

Techniques Used: Migration, MTT Assay, Transwell Assay

Arnebin-1 promotes vascular endothelial growth factor (VEGF) receptor 2 (VEGFR2) kinase activity and its downstream signaling molecules. (A) Arnebin-1 increased the phosphorylation of VEGFR2 induced by VEGF in human umbilical vein endothelial cells (HUVECs). Total protein was isolated and subjected to western blot analysis. Upper panel shows representative blots of the protein levels of phosphorylated (p-)VEGFR2 and total (t-)VEGFR2 proteins. Lower panel shows the quantification of the p-VEGFR2 protein level. (B–D) Arnebin-1 also increased VEGFR2-mediated protein kinase activation of focal adhesion kinase (FAK), extracellular signal-regulated kinase (Erk) and Src. (B) Upper panel shows representative blots of the protein levels of p-FAK and t-FAK. Lower panel shows the quantification of the p-FAK protein level. (C) Upper panel shows the representative blots of the levels of p-Erk and t-Erk proteins. Lower panel shows the quantification of the p-Erk protein level. (D) Upper panel shows representative blots of the protein levels of p-Src and t-Src proteins. Lower panel shows the quantification of the p-Src protein level. (E) Diagram of signaling pathways involved in arnebin-1-induced angiogenesis. α-tubulin was used as a loading control. Bars represent the means ± SEM. * P
Figure Legend Snippet: Arnebin-1 promotes vascular endothelial growth factor (VEGF) receptor 2 (VEGFR2) kinase activity and its downstream signaling molecules. (A) Arnebin-1 increased the phosphorylation of VEGFR2 induced by VEGF in human umbilical vein endothelial cells (HUVECs). Total protein was isolated and subjected to western blot analysis. Upper panel shows representative blots of the protein levels of phosphorylated (p-)VEGFR2 and total (t-)VEGFR2 proteins. Lower panel shows the quantification of the p-VEGFR2 protein level. (B–D) Arnebin-1 also increased VEGFR2-mediated protein kinase activation of focal adhesion kinase (FAK), extracellular signal-regulated kinase (Erk) and Src. (B) Upper panel shows representative blots of the protein levels of p-FAK and t-FAK. Lower panel shows the quantification of the p-FAK protein level. (C) Upper panel shows the representative blots of the levels of p-Erk and t-Erk proteins. Lower panel shows the quantification of the p-Erk protein level. (D) Upper panel shows representative blots of the protein levels of p-Src and t-Src proteins. Lower panel shows the quantification of the p-Src protein level. (E) Diagram of signaling pathways involved in arnebin-1-induced angiogenesis. α-tubulin was used as a loading control. Bars represent the means ± SEM. * P

Techniques Used: Activity Assay, Isolation, Western Blot, Activation Assay

The expression levels of endothelial nitric oxide synthase (eNOS), vascular endothelial growth factor (VEGF) and hypoxia-inducible factor (HIF)-1α were increased by arnebin-1 in a phosphoinositide 3-kinase (PI3K)-dependent manner. (A–C) Human umbilical vein endothelial cells (HUVECs) were treated with arnebin-1 only at various concentrations (10 −3 , 10 −2 and 10 −1 µ M) for 24 h. Cell lysates were subjected to western blot analysis. (A) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (B) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. (C) The secretion level of VEGF in the culture supernatants was determined by ELISA. (D) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (E–H) HUVECs were treated with or without LY294002 for 1 h, and then stimulated with arnebin-1 in the presence or absence of VEGF for 24 h. (E) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (F) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (G) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. (H) The secretion level of VEGF in the culture supernatants was determined by ELISA. Bars represent the means ± SEM. * P
Figure Legend Snippet: The expression levels of endothelial nitric oxide synthase (eNOS), vascular endothelial growth factor (VEGF) and hypoxia-inducible factor (HIF)-1α were increased by arnebin-1 in a phosphoinositide 3-kinase (PI3K)-dependent manner. (A–C) Human umbilical vein endothelial cells (HUVECs) were treated with arnebin-1 only at various concentrations (10 −3 , 10 −2 and 10 −1 µ M) for 24 h. Cell lysates were subjected to western blot analysis. (A) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (B) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. (C) The secretion level of VEGF in the culture supernatants was determined by ELISA. (D) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (E–H) HUVECs were treated with or without LY294002 for 1 h, and then stimulated with arnebin-1 in the presence or absence of VEGF for 24 h. (E) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (F) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (G) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. (H) The secretion level of VEGF in the culture supernatants was determined by ELISA. Bars represent the means ± SEM. * P

Techniques Used: Expressing, Western Blot, Enzyme-linked Immunosorbent Assay

(A) Structure of arnebin-1 [5,8-dihydroxy-2-(1′-b,b-dimethylaryoxy-4′-methylpent-3-enyl)-1,4-naphthoquinone]. (B) Human umbilical vein endothelial cells (HUVECs) were treated with arnebin-1 only at various concentrations for 24 h. Cell lysates were subjected to western blot analysis. Upper panel shows representative blots of the protein expression of proliferating cell nuclear antigen (PCNA). Lower panel shows the quantification of the PCNA protein level. (C) The HUVECs were treated with arnebin-1 at various concentrations in the absence or presence of vascular endothelial growth factor (VEGF; 1 ng/ml) for 24 h. Cell lysates were subjected to western blot analysis. Upper panel shows representative blots of the protein expression of PCNA. Lower panel shows the quantification of the PCNA protein level. α-tubulin was used as a loading control. Bars represent the means ± SEM. * P
Figure Legend Snippet: (A) Structure of arnebin-1 [5,8-dihydroxy-2-(1′-b,b-dimethylaryoxy-4′-methylpent-3-enyl)-1,4-naphthoquinone]. (B) Human umbilical vein endothelial cells (HUVECs) were treated with arnebin-1 only at various concentrations for 24 h. Cell lysates were subjected to western blot analysis. Upper panel shows representative blots of the protein expression of proliferating cell nuclear antigen (PCNA). Lower panel shows the quantification of the PCNA protein level. (C) The HUVECs were treated with arnebin-1 at various concentrations in the absence or presence of vascular endothelial growth factor (VEGF; 1 ng/ml) for 24 h. Cell lysates were subjected to western blot analysis. Upper panel shows representative blots of the protein expression of PCNA. Lower panel shows the quantification of the PCNA protein level. α-tubulin was used as a loading control. Bars represent the means ± SEM. * P

Techniques Used: Western Blot, Expressing

Schematic diagram of the mechanisms through which arnebin-1 promotes vascularization and wound healing. Arnebin-1 treatment leads to the accumulation of hypoxia-inducible factor (HIF)-1α, and the consequent upregulation of VEGF and endothelial nitric oxide synthase (eNOS). The expression of HIF-1α target genes in turn promotes neovascularization in diabetic wounds through angiogenesis and vasculogenesis.
Figure Legend Snippet: Schematic diagram of the mechanisms through which arnebin-1 promotes vascularization and wound healing. Arnebin-1 treatment leads to the accumulation of hypoxia-inducible factor (HIF)-1α, and the consequent upregulation of VEGF and endothelial nitric oxide synthase (eNOS). The expression of HIF-1α target genes in turn promotes neovascularization in diabetic wounds through angiogenesis and vasculogenesis.

Techniques Used: Expressing

Effects of arnebin-1 on the hypoxia-inducible factor (HIF)-1α, vascular endothelial growth factor (VEGF) and endothelial nitric oxide synthase (eNOS) expression levels in diabetic rats. (A–C) Effects of arnebin-1 on the protein expression levels of HIF-1α, VEGF and eNOS. (A) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (B) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (C) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. Bars represent the means ± SEM. * P
Figure Legend Snippet: Effects of arnebin-1 on the hypoxia-inducible factor (HIF)-1α, vascular endothelial growth factor (VEGF) and endothelial nitric oxide synthase (eNOS) expression levels in diabetic rats. (A–C) Effects of arnebin-1 on the protein expression levels of HIF-1α, VEGF and eNOS. (A) Upper panel shows representative blots of the protein level of HIF-1α. Lower panel shows the quantification of the HIF-1α protein level. (B) Upper panel shows representative blots of the protein level of eNOS. Lower panel shows the quantification of the eNOS protein level. (C) Upper panel shows representative blots of the protein level of VEGF. Lower panel shows the quantification of the VEGF protein level. Bars represent the means ± SEM. * P

Techniques Used: Expressing

19) Product Images from "Epac1 inhibition ameliorates pathological angiogenesis through coordinated activation of Notch and suppression of VEGF signaling"

Article Title: Epac1 inhibition ameliorates pathological angiogenesis through coordinated activation of Notch and suppression of VEGF signaling

Journal: Science Advances

doi: 10.1126/sciadv.aay3566

Epac1 deficiency impairs pathological neovascularization. ( A ) Hematoxylin and eosin (H E) staining of ligated carotid artery sections from WT and Epac1 −/− mice. ( B ) Immunofluorescence-stained ligated carotid artery sections from WT and Epac1 −/− mice. Green, BS1 lectin-FITC; red, α-SMA; blue, DAPI. Arrows indicate neovascularization. Scale bars, 50 μm. ( C ) Quantification of neovascularization in ligated carotid artery sections from WT and Epac1 −/− mice ( n = 7). ( D ) Images of subcutaneously implanted Matrigel plugs retrieved from WT and Epac1 −/− mice. ( E ) H E staining of sectioned Matrigel plugs harvested from WT and Epac1 −/− mice. Note the presence of microvessel-like structures and abundant blood cells (arrows) in WT Matrigel plugs, which were mostly absent in Epac1 −/− Matrigel plugs. Scale bars, 200 μm. ( F ) Confocal images of immunofluorescence-stained, sectioned Matrigel plug slides harvested from WT and EPAC1 −/− mice. Green, BS1 lectin-FITC; red, α-SMA; blue, DAPI. Arrows, microvessel-like structures. Scale bars, 200 μm. ( G ) Representative images of microvessel outgrowths in VEGF/FGF-treated aortic rings isolated from WT and Epac1 −/− mice. ( H ) Quantification of main microvessel sprouts observed from WT ( n = 24) and Epac1 −/− ( n = 26) aortic rings.
Figure Legend Snippet: Epac1 deficiency impairs pathological neovascularization. ( A ) Hematoxylin and eosin (H E) staining of ligated carotid artery sections from WT and Epac1 −/− mice. ( B ) Immunofluorescence-stained ligated carotid artery sections from WT and Epac1 −/− mice. Green, BS1 lectin-FITC; red, α-SMA; blue, DAPI. Arrows indicate neovascularization. Scale bars, 50 μm. ( C ) Quantification of neovascularization in ligated carotid artery sections from WT and Epac1 −/− mice ( n = 7). ( D ) Images of subcutaneously implanted Matrigel plugs retrieved from WT and Epac1 −/− mice. ( E ) H E staining of sectioned Matrigel plugs harvested from WT and Epac1 −/− mice. Note the presence of microvessel-like structures and abundant blood cells (arrows) in WT Matrigel plugs, which were mostly absent in Epac1 −/− Matrigel plugs. Scale bars, 200 μm. ( F ) Confocal images of immunofluorescence-stained, sectioned Matrigel plug slides harvested from WT and EPAC1 −/− mice. Green, BS1 lectin-FITC; red, α-SMA; blue, DAPI. Arrows, microvessel-like structures. Scale bars, 200 μm. ( G ) Representative images of microvessel outgrowths in VEGF/FGF-treated aortic rings isolated from WT and Epac1 −/− mice. ( H ) Quantification of main microvessel sprouts observed from WT ( n = 24) and Epac1 −/− ( n = 26) aortic rings.

Techniques Used: Staining, Mouse Assay, Immunofluorescence, Isolation

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    PeproTech human vegf
    Total Tubule Length built by investigated implants. <t>VEGF-functionalized</t> titanium-PCL implants showed significantly the best results for the characteristic Total Tubule Length. VEGF + <t>HMGB1-functionalized</t> titanium-PCL implants showed a significantly higher Total Tubule Length than titanium-PCL implants and HMGB1-functionalized titanium-PCL implants, but comparable results to pure titanium implants. Pure titanium implants were significantly better than titanium-PCL implants and HMGB1-functionalized titanium-PCL implants. F -test from the analyses of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).
    Human Vegf, supplied by PeproTech, used in various techniques. Bioz Stars score: 96/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human vegf/product/PeproTech
    Average 96 stars, based on 5 article reviews
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    human vegf - by Bioz Stars, 2022-10
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    94
    PeproTech recombinant human vegf c
    Effect of MSC‐CM on LEC sprouting. LEC spheroids were embedded in collagen or fibrin gels and treated with <t>VEGF‐C</t> combined with bFGF and 100% MSC‐CM. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control. (A) Spheroids were grown in hanging drop culture. (B) Representative images of spheroids treated with different stimulations after 24 h. (C) Sprout length and number of spheroids treated with different stimulations ( x ‐axis) were quantified and displayed in bar graphs. (n = 2, duplicates, * P ≤ .05 compared to negative control)
    Recombinant Human Vegf C, supplied by PeproTech, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human vegf c/product/PeproTech
    Average 94 stars, based on 2 article reviews
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    recombinant human vegf c - by Bioz Stars, 2022-10
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    Total Tubule Length built by investigated implants. VEGF-functionalized titanium-PCL implants showed significantly the best results for the characteristic Total Tubule Length. VEGF + HMGB1-functionalized titanium-PCL implants showed a significantly higher Total Tubule Length than titanium-PCL implants and HMGB1-functionalized titanium-PCL implants, but comparable results to pure titanium implants. Pure titanium implants were significantly better than titanium-PCL implants and HMGB1-functionalized titanium-PCL implants. F -test from the analyses of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).

    Journal: Materials

    Article Title: Evaluation of Functionalized Porous Titanium Implants for Enhancing Angiogenesis in Vitro

    doi: 10.3390/ma9040304

    Figure Lengend Snippet: Total Tubule Length built by investigated implants. VEGF-functionalized titanium-PCL implants showed significantly the best results for the characteristic Total Tubule Length. VEGF + HMGB1-functionalized titanium-PCL implants showed a significantly higher Total Tubule Length than titanium-PCL implants and HMGB1-functionalized titanium-PCL implants, but comparable results to pure titanium implants. Pure titanium implants were significantly better than titanium-PCL implants and HMGB1-functionalized titanium-PCL implants. F -test from the analyses of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).

    Article Snippet: Human VEGF (450-32, Peprotech, Hamburg, Germany) and HMGB1 (H4652, Sigma-Aldrich, Taufkirchen, Germany) were incorporated in polymer coatings by sorption.

    Techniques:

    Released amounts of VEGF. Releasing kinetics of VEGF from titanium implants coated with PCL and functionalized with VEGF and from titanium implants coated with PCL and functionalized with VEGF and HMGB1 (dashed lines).

    Journal: Materials

    Article Title: Evaluation of Functionalized Porous Titanium Implants for Enhancing Angiogenesis in Vitro

    doi: 10.3390/ma9040304

    Figure Lengend Snippet: Released amounts of VEGF. Releasing kinetics of VEGF from titanium implants coated with PCL and functionalized with VEGF and from titanium implants coated with PCL and functionalized with VEGF and HMGB1 (dashed lines).

    Article Snippet: Human VEGF (450-32, Peprotech, Hamburg, Germany) and HMGB1 (H4652, Sigma-Aldrich, Taufkirchen, Germany) were incorporated in polymer coatings by sorption.

    Techniques:

    Results of Angiogenesis Assay with proangiogenic cytokines VEGF and HMGB1. Angiogenesis Assay with VEGF at a steady concentration of 10 ng/mL ( n = 4) and a declining concentration of 117 ng/mL on day 2, 16 ng/mL on day 5, 7 ng/mL on day 8 and 6 ng/mL on day 11 ( n = 4), respectively. HMGB1 was used at a steady concentration of 100 ng/mL ( n = 4) and a declining concentration of 924 ng/mL at day 2, 130 ng/mL at day 5, 76 ng/mL at day 8 and 24 ng/mL at day 11, respectively. Results for Total Number of Junctions ( A ); Total Number of Tubules ( B ); Total Tubule Length (µm) ( C ); and Total Number of Nets ( D ) were analyzed using F -test from the analysis of variance followed by pairwise multiple means comparisons with the use of the Least Significant Difference ( p ≤ 0.05). Both, VEGF using a concentration of 10 ng/mL and the declining concentrations, showed an angiogenesis stimulating effect. The steady concentration of 10 ng/mL showed significantly more tubules and junction formation than the declining concentrations. Neither the constant concentration of 100 ng/mL HMGB1 nor the declining concentrations of HMGB1 showed an angiogenesis stimulating effect.

    Journal: Materials

    Article Title: Evaluation of Functionalized Porous Titanium Implants for Enhancing Angiogenesis in Vitro

    doi: 10.3390/ma9040304

    Figure Lengend Snippet: Results of Angiogenesis Assay with proangiogenic cytokines VEGF and HMGB1. Angiogenesis Assay with VEGF at a steady concentration of 10 ng/mL ( n = 4) and a declining concentration of 117 ng/mL on day 2, 16 ng/mL on day 5, 7 ng/mL on day 8 and 6 ng/mL on day 11 ( n = 4), respectively. HMGB1 was used at a steady concentration of 100 ng/mL ( n = 4) and a declining concentration of 924 ng/mL at day 2, 130 ng/mL at day 5, 76 ng/mL at day 8 and 24 ng/mL at day 11, respectively. Results for Total Number of Junctions ( A ); Total Number of Tubules ( B ); Total Tubule Length (µm) ( C ); and Total Number of Nets ( D ) were analyzed using F -test from the analysis of variance followed by pairwise multiple means comparisons with the use of the Least Significant Difference ( p ≤ 0.05). Both, VEGF using a concentration of 10 ng/mL and the declining concentrations, showed an angiogenesis stimulating effect. The steady concentration of 10 ng/mL showed significantly more tubules and junction formation than the declining concentrations. Neither the constant concentration of 100 ng/mL HMGB1 nor the declining concentrations of HMGB1 showed an angiogenesis stimulating effect.

    Article Snippet: Human VEGF (450-32, Peprotech, Hamburg, Germany) and HMGB1 (H4652, Sigma-Aldrich, Taufkirchen, Germany) were incorporated in polymer coatings by sorption.

    Techniques: Angiogenesis Assay, Concentration Assay

    Migration Assay with GM7373 and supernatants from functionalized implants. Comparison of chemotactic behavior of the endothelial cell line (GM7373) using supernatants from implants functionalized with VEGF (vascular endothelial growth factor), HMGB1 (high mobility group box 1) and a combination of HMGB1/VEGF. All of the functionalized implants showed significantly higher chemotaxis than DMEM with 20% FCS or 0.1% FCS. VEGF was significantly more chemotactic than the combination of VEGF + HMGB1. F -test from the analyses of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).

    Journal: Materials

    Article Title: Evaluation of Functionalized Porous Titanium Implants for Enhancing Angiogenesis in Vitro

    doi: 10.3390/ma9040304

    Figure Lengend Snippet: Migration Assay with GM7373 and supernatants from functionalized implants. Comparison of chemotactic behavior of the endothelial cell line (GM7373) using supernatants from implants functionalized with VEGF (vascular endothelial growth factor), HMGB1 (high mobility group box 1) and a combination of HMGB1/VEGF. All of the functionalized implants showed significantly higher chemotaxis than DMEM with 20% FCS or 0.1% FCS. VEGF was significantly more chemotactic than the combination of VEGF + HMGB1. F -test from the analyses of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).

    Article Snippet: Human VEGF (450-32, Peprotech, Hamburg, Germany) and HMGB1 (H4652, Sigma-Aldrich, Taufkirchen, Germany) were incorporated in polymer coatings by sorption.

    Techniques: Migration, Chemotaxis Assay

    Number of Tubules built by investigated implants. VEGF-functionalized titanium-PCL implants built significantly more tubules than all of the other implants. VEGF + HMGB1-functionalized titanium-PCL implants showed significantly more tubules than titanium-PCL implants and HMGB1 functionalized titanium-PCL implants. Pure titanium implants showed better results than titanium-PCL implants. F -test from the analysis of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).

    Journal: Materials

    Article Title: Evaluation of Functionalized Porous Titanium Implants for Enhancing Angiogenesis in Vitro

    doi: 10.3390/ma9040304

    Figure Lengend Snippet: Number of Tubules built by investigated implants. VEGF-functionalized titanium-PCL implants built significantly more tubules than all of the other implants. VEGF + HMGB1-functionalized titanium-PCL implants showed significantly more tubules than titanium-PCL implants and HMGB1 functionalized titanium-PCL implants. Pure titanium implants showed better results than titanium-PCL implants. F -test from the analysis of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).

    Article Snippet: Human VEGF (450-32, Peprotech, Hamburg, Germany) and HMGB1 (H4652, Sigma-Aldrich, Taufkirchen, Germany) were incorporated in polymer coatings by sorption.

    Techniques:

    Tubuli and Nets visible after Angiogenesis Assay. After staining with BCIP/NBT-Substrate, tubuli and net-structures became visible. ( A ) Titanium implant functionalized with VEGF; ( B ) titanium implant functionalized with HMGB1; and ( C ) titanium implant functionalized with a combination of VEGF + HMGB1.

    Journal: Materials

    Article Title: Evaluation of Functionalized Porous Titanium Implants for Enhancing Angiogenesis in Vitro

    doi: 10.3390/ma9040304

    Figure Lengend Snippet: Tubuli and Nets visible after Angiogenesis Assay. After staining with BCIP/NBT-Substrate, tubuli and net-structures became visible. ( A ) Titanium implant functionalized with VEGF; ( B ) titanium implant functionalized with HMGB1; and ( C ) titanium implant functionalized with a combination of VEGF + HMGB1.

    Article Snippet: Human VEGF (450-32, Peprotech, Hamburg, Germany) and HMGB1 (H4652, Sigma-Aldrich, Taufkirchen, Germany) were incorporated in polymer coatings by sorption.

    Techniques: Angiogenesis Assay, Staining

    Number of Junctions built due to the investigated implant. VEGF-functionalized titanium-PCL implants showed significantly more junctions than all of the other implants. VEGF + HMGB1-functionalized titanium-PCL implants built significantly more junctions than pure titanium implants, titanium implants coated with PCL and HMGB1-functionalized titanium-PCL implants. Significantly more junctions could be seen in wells with pure titanium implants than in wells with titanium-PCL implants. F -test from the analyses of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).

    Journal: Materials

    Article Title: Evaluation of Functionalized Porous Titanium Implants for Enhancing Angiogenesis in Vitro

    doi: 10.3390/ma9040304

    Figure Lengend Snippet: Number of Junctions built due to the investigated implant. VEGF-functionalized titanium-PCL implants showed significantly more junctions than all of the other implants. VEGF + HMGB1-functionalized titanium-PCL implants built significantly more junctions than pure titanium implants, titanium implants coated with PCL and HMGB1-functionalized titanium-PCL implants. Significantly more junctions could be seen in wells with pure titanium implants than in wells with titanium-PCL implants. F -test from the analyses of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).

    Article Snippet: Human VEGF (450-32, Peprotech, Hamburg, Germany) and HMGB1 (H4652, Sigma-Aldrich, Taufkirchen, Germany) were incorporated in polymer coatings by sorption.

    Techniques:

    Released amounts of HMGB1. Releasing kinetics of HMGB1 from titanium implants coated with PCL and functionalized with HMGB1 and from titanium implants coated with PCL and functionalized with VEGF and HMGB1 (dashed lines). The concentration of HMGB1 released from titanium PCL scaffold HMGB1 3 (green line) was above the detection limit of 1668 ng/mL at day 5. Therefore, no result for this day can be shown.

    Journal: Materials

    Article Title: Evaluation of Functionalized Porous Titanium Implants for Enhancing Angiogenesis in Vitro

    doi: 10.3390/ma9040304

    Figure Lengend Snippet: Released amounts of HMGB1. Releasing kinetics of HMGB1 from titanium implants coated with PCL and functionalized with HMGB1 and from titanium implants coated with PCL and functionalized with VEGF and HMGB1 (dashed lines). The concentration of HMGB1 released from titanium PCL scaffold HMGB1 3 (green line) was above the detection limit of 1668 ng/mL at day 5. Therefore, no result for this day can be shown.

    Article Snippet: Human VEGF (450-32, Peprotech, Hamburg, Germany) and HMGB1 (H4652, Sigma-Aldrich, Taufkirchen, Germany) were incorporated in polymer coatings by sorption.

    Techniques: Concentration Assay

    Number of Nets built by investigated implants. VEGF-functionalized titanium-PCL implants lead to significantly more building of net-like structures than all of the other titanium implants with or without cytokines in the assay. VEGF + HMGB1-functionalized titanium-PCL implants built significantly more nets than pure titanium implants, titanium-PCL implants and HMGB1-functionalized titanium-PCL implants. F -test from the analysis of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).

    Journal: Materials

    Article Title: Evaluation of Functionalized Porous Titanium Implants for Enhancing Angiogenesis in Vitro

    doi: 10.3390/ma9040304

    Figure Lengend Snippet: Number of Nets built by investigated implants. VEGF-functionalized titanium-PCL implants lead to significantly more building of net-like structures than all of the other titanium implants with or without cytokines in the assay. VEGF + HMGB1-functionalized titanium-PCL implants built significantly more nets than pure titanium implants, titanium-PCL implants and HMGB1-functionalized titanium-PCL implants. F -test from the analysis of variance followed by pairwise multiple means comparisons with the Least Significant Difference test were used ( p ≤ 0.05).

    Article Snippet: Human VEGF (450-32, Peprotech, Hamburg, Germany) and HMGB1 (H4652, Sigma-Aldrich, Taufkirchen, Germany) were incorporated in polymer coatings by sorption.

    Techniques:

    DMOG induces pro-angiogenic responses without cell toxicity in MDPC-23 cells. (A) MDPC-23 cells were incubated for 24 h in the presence or absence of DMOG, and cytotoxicity was evaluated. DMOG does not induce cytotoxic effects at concentrations lower than 1 mM in MDPC-23 cells. The data represent the mean ± SD of quadruplicates. (B, C) MDPC-23 cells were incubated for 24 h in the presence or absence of DMOG, and western blot analyses for HIF-1α (B) and VEGF (C, lower) and RT-qPCR for VEGF (C, upper) were performed. The data are presented as the mean ± SD of triplicates. *Significantly different from control (Student's t-test, p

    Journal: PLoS ONE

    Article Title: The Prolyl Hydroxylase Inhibitor Dimethyloxalylglycine Enhances Dentin Sialophoshoprotein Expression through VEGF-Induced Runx2 Stabilization

    doi: 10.1371/journal.pone.0112078

    Figure Lengend Snippet: DMOG induces pro-angiogenic responses without cell toxicity in MDPC-23 cells. (A) MDPC-23 cells were incubated for 24 h in the presence or absence of DMOG, and cytotoxicity was evaluated. DMOG does not induce cytotoxic effects at concentrations lower than 1 mM in MDPC-23 cells. The data represent the mean ± SD of quadruplicates. (B, C) MDPC-23 cells were incubated for 24 h in the presence or absence of DMOG, and western blot analyses for HIF-1α (B) and VEGF (C, lower) and RT-qPCR for VEGF (C, upper) were performed. The data are presented as the mean ± SD of triplicates. *Significantly different from control (Student's t-test, p

    Article Snippet: To induce odontoblast differentiation, we cultured the cells in a differentiation medium (growth medium supplemented with 10 mM β-glycerophosphate and 50 µg/ml ascorbic acid) in the presence or absence of DMOG (Cayman Chemical, Ann Arbor, MI, USA) or of recombinant murine VEGF (PeproTech, Rocky Hill, NJ, USA) for the indicated periods.

    Techniques: Incubation, Western Blot, Quantitative RT-PCR

    DMOG-induced VEGF stabilizes the Runx2 protein in MDPC-23 cells. (A) DMOG-enhanced Runx2 protein is VEGF-dependent. MDPC-23 cells were transiently transfected with Vegf siRNA or with control siRNA and incubated in the presence or absence of DMOG for 48 h. Western blots for Runx2 protein and for VEGF and RT-qPCRs for Runx2 and for Histone H3 were performed. Western blot quantification was performed by measuring bands intensities, and the relative levels were normalized by β-actin. (B) Recombinant VEGF increases the Runx2 protein levels (upper) but not Runx2 transcripts (lower). MDPC-23 cells were treated with VEGF (50 ng/ml), and a western blot and RT-qPCR were performed. Western blot quantification was performed by measuring bands intensities, and the relative levels were normalized by β-actin. (C) Transcriptional activity of Runx2 upon VEGF treatment. The Runx2 reporter 6XOSE-Luc was transfected into MDPC-23 cells, and the cells were cultured for 48 h in the presence or absence of VEGF. Runx2 reporter luciferase activity was measured and normalized by Renilla luciferase activity. The data are presented as the mean ± SD (n = 6). *Significantly different from control (Student's t-test, p

    Journal: PLoS ONE

    Article Title: The Prolyl Hydroxylase Inhibitor Dimethyloxalylglycine Enhances Dentin Sialophoshoprotein Expression through VEGF-Induced Runx2 Stabilization

    doi: 10.1371/journal.pone.0112078

    Figure Lengend Snippet: DMOG-induced VEGF stabilizes the Runx2 protein in MDPC-23 cells. (A) DMOG-enhanced Runx2 protein is VEGF-dependent. MDPC-23 cells were transiently transfected with Vegf siRNA or with control siRNA and incubated in the presence or absence of DMOG for 48 h. Western blots for Runx2 protein and for VEGF and RT-qPCRs for Runx2 and for Histone H3 were performed. Western blot quantification was performed by measuring bands intensities, and the relative levels were normalized by β-actin. (B) Recombinant VEGF increases the Runx2 protein levels (upper) but not Runx2 transcripts (lower). MDPC-23 cells were treated with VEGF (50 ng/ml), and a western blot and RT-qPCR were performed. Western blot quantification was performed by measuring bands intensities, and the relative levels were normalized by β-actin. (C) Transcriptional activity of Runx2 upon VEGF treatment. The Runx2 reporter 6XOSE-Luc was transfected into MDPC-23 cells, and the cells were cultured for 48 h in the presence or absence of VEGF. Runx2 reporter luciferase activity was measured and normalized by Renilla luciferase activity. The data are presented as the mean ± SD (n = 6). *Significantly different from control (Student's t-test, p

    Article Snippet: To induce odontoblast differentiation, we cultured the cells in a differentiation medium (growth medium supplemented with 10 mM β-glycerophosphate and 50 µg/ml ascorbic acid) in the presence or absence of DMOG (Cayman Chemical, Ann Arbor, MI, USA) or of recombinant murine VEGF (PeproTech, Rocky Hill, NJ, USA) for the indicated periods.

    Techniques: Transfection, Incubation, Western Blot, Recombinant, Quantitative RT-PCR, Activity Assay, Cell Culture, Luciferase

    Effect of MSC‐CM on LEC sprouting. LEC spheroids were embedded in collagen or fibrin gels and treated with VEGF‐C combined with bFGF and 100% MSC‐CM. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control. (A) Spheroids were grown in hanging drop culture. (B) Representative images of spheroids treated with different stimulations after 24 h. (C) Sprout length and number of spheroids treated with different stimulations ( x ‐axis) were quantified and displayed in bar graphs. (n = 2, duplicates, * P ≤ .05 compared to negative control)

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells. Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells

    doi: 10.1111/jcmm.13590

    Figure Lengend Snippet: Effect of MSC‐CM on LEC sprouting. LEC spheroids were embedded in collagen or fibrin gels and treated with VEGF‐C combined with bFGF and 100% MSC‐CM. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control. (A) Spheroids were grown in hanging drop culture. (B) Representative images of spheroids treated with different stimulations after 24 h. (C) Sprout length and number of spheroids treated with different stimulations ( x ‐axis) were quantified and displayed in bar graphs. (n = 2, duplicates, * P ≤ .05 compared to negative control)

    Article Snippet: The lower chambers were filled with 600 μL ECBM supplemented with 0.5% FBS and 400 ng/mL recombinant human VEGF‐C in combination with 200 ng/mL recombinant human bFGF.

    Techniques: Positive Control, Negative Control

    Effect of MSC‐CM on LEC tube formation. LEC were treated with VEGF‐C combined with bFGF, 100% MSC‐CM or co‐cultured with 1,000 or 2,000 MSC. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control. (n = 3, singles, * P ≤ .05 compared to negative control) (A) Representative images of LEC tube formation. LEC were labelled in red, MSC in green. (B) Bar graphs show the total tube length (left y ‐axis) and the number of tubes (right y ‐axis) of LEC treated with different stimulations ( x ‐axis). (C) Bar graphs show the tube‐covered area (left) and the number of branching points (right) of LEC treated with different stimulations ( x ‐axis)

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells. Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells

    doi: 10.1111/jcmm.13590

    Figure Lengend Snippet: Effect of MSC‐CM on LEC tube formation. LEC were treated with VEGF‐C combined with bFGF, 100% MSC‐CM or co‐cultured with 1,000 or 2,000 MSC. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control. (n = 3, singles, * P ≤ .05 compared to negative control) (A) Representative images of LEC tube formation. LEC were labelled in red, MSC in green. (B) Bar graphs show the total tube length (left y ‐axis) and the number of tubes (right y ‐axis) of LEC treated with different stimulations ( x ‐axis). (C) Bar graphs show the tube‐covered area (left) and the number of branching points (right) of LEC treated with different stimulations ( x ‐axis)

    Article Snippet: The lower chambers were filled with 600 μL ECBM supplemented with 0.5% FBS and 400 ng/mL recombinant human VEGF‐C in combination with 200 ng/mL recombinant human bFGF.

    Techniques: Cell Culture, Positive Control, Negative Control

    Effect of MSC‐CM on LEC transmigration in a modified Boyden chamber assay. The lower compartment of the transwell chamber was loaded with VEGF‐C combined with bFGF, 100% MSC‐CM or 750,000 MSC. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control. (A) Bar graphs show a comparison of migratory activity represented in the average number of transmigrated LEC per field of vision ( y ‐axis) of cells treated with different stimulations ( x ‐axis). (n = 3, duplicates, * P ≤ .05) (B) Representative images of LEC transmigration

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells. Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells

    doi: 10.1111/jcmm.13590

    Figure Lengend Snippet: Effect of MSC‐CM on LEC transmigration in a modified Boyden chamber assay. The lower compartment of the transwell chamber was loaded with VEGF‐C combined with bFGF, 100% MSC‐CM or 750,000 MSC. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control. (A) Bar graphs show a comparison of migratory activity represented in the average number of transmigrated LEC per field of vision ( y ‐axis) of cells treated with different stimulations ( x ‐axis). (n = 3, duplicates, * P ≤ .05) (B) Representative images of LEC transmigration

    Article Snippet: The lower chambers were filled with 600 μL ECBM supplemented with 0.5% FBS and 400 ng/mL recombinant human VEGF‐C in combination with 200 ng/mL recombinant human bFGF.

    Techniques: Transmigration Assay, Modification, Boyden Chamber Assay, Positive Control, Negative Control, Activity Assay

    Effect of MSC‐CM on LEC migration in the scratch assay. LEC were treated with VEGF‐C combined with bFGF and 100% MSC‐CM. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control. (A) Bar graphs show a comparison of migratory activity represented in uncovered scratch area ( y ‐axis) of LEC treated with different stimulations ( x ‐axis) at 12 and 24 h. (n = 3, duplicates, * P ≤ .05; only the significances of 24 h are marked) (B) Representative images of LEC migration

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells. Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells

    doi: 10.1111/jcmm.13590

    Figure Lengend Snippet: Effect of MSC‐CM on LEC migration in the scratch assay. LEC were treated with VEGF‐C combined with bFGF and 100% MSC‐CM. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control. (A) Bar graphs show a comparison of migratory activity represented in uncovered scratch area ( y ‐axis) of LEC treated with different stimulations ( x ‐axis) at 12 and 24 h. (n = 3, duplicates, * P ≤ .05; only the significances of 24 h are marked) (B) Representative images of LEC migration

    Article Snippet: The lower chambers were filled with 600 μL ECBM supplemented with 0.5% FBS and 400 ng/mL recombinant human VEGF‐C in combination with 200 ng/mL recombinant human bFGF.

    Techniques: Migration, Wound Healing Assay, Positive Control, Negative Control, Activity Assay

    Effect of MSC‐conditioned medium (CM) on LEC proliferation in the MTT assay. Bar graphs show a comparison of viability represented in absorbance ( y ‐axis) of LEC treated with different stimulations ( x ‐axis) at 24‐72 h. (n = 3, triplicate, * P ≤ .05, ** P ≤ .01; only the significances of 72 h are marked) (A) Cells were treated with different dilutions of MSC‐CM. (B) Cells were treated with 100% MSC‐CM, VEGF‐C, bFGF and the combination of both growth factors. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells. Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells

    doi: 10.1111/jcmm.13590

    Figure Lengend Snippet: Effect of MSC‐conditioned medium (CM) on LEC proliferation in the MTT assay. Bar graphs show a comparison of viability represented in absorbance ( y ‐axis) of LEC treated with different stimulations ( x ‐axis) at 24‐72 h. (n = 3, triplicate, * P ≤ .05, ** P ≤ .01; only the significances of 72 h are marked) (A) Cells were treated with different dilutions of MSC‐CM. (B) Cells were treated with 100% MSC‐CM, VEGF‐C, bFGF and the combination of both growth factors. PMA served as positive control, basal medium supplemented with 0.5% FCS as negative control

    Article Snippet: The lower chambers were filled with 600 μL ECBM supplemented with 0.5% FBS and 400 ng/mL recombinant human VEGF‐C in combination with 200 ng/mL recombinant human bFGF.

    Techniques: MTT Assay, Positive Control, Negative Control

    Concentration of different growth factors in MSC‐CM. ELISA analyses of MSC‐CM and basal medium as negative control for VEGF‐C, VEGF‐D, HGF and bFGF are displayed in bar graphs. CM was generated with MSC obtained from 3 different donors. (2 replicates, * P ≤ .05 compared to negative control)

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells. Mesenchymal stem cells promote lymphangiogenic properties of lymphatic endothelial cells

    doi: 10.1111/jcmm.13590

    Figure Lengend Snippet: Concentration of different growth factors in MSC‐CM. ELISA analyses of MSC‐CM and basal medium as negative control for VEGF‐C, VEGF‐D, HGF and bFGF are displayed in bar graphs. CM was generated with MSC obtained from 3 different donors. (2 replicates, * P ≤ .05 compared to negative control)

    Article Snippet: The lower chambers were filled with 600 μL ECBM supplemented with 0.5% FBS and 400 ng/mL recombinant human VEGF‐C in combination with 200 ng/mL recombinant human bFGF.

    Techniques: Concentration Assay, Enzyme-linked Immunosorbent Assay, Negative Control, Generated

    Sequential phosphorylation of ERK and p38 MAPK in response to VEGF-C stimulation in NRP-2-overexpressing thyroid cancer cells. NRP-2-overexpressing (A-C) K1 and (D-F) WRO cells were treated with 100 ng/ml VEGF-C at different time intervals, as indicated.

    Journal: Oncology Letters

    Article Title: Promotion of metastasis of thyroid cancer cells via NRP-2-mediated induction

    doi: 10.3892/ol.2016.5153

    Figure Lengend Snippet: Sequential phosphorylation of ERK and p38 MAPK in response to VEGF-C stimulation in NRP-2-overexpressing thyroid cancer cells. NRP-2-overexpressing (A-C) K1 and (D-F) WRO cells were treated with 100 ng/ml VEGF-C at different time intervals, as indicated.

    Article Snippet: In brief, cells were seeded in 6-well culture plates (0.5–1.0×106 cells/ml/well) and transfected with 8 µg expression plasmid for 36 h. Transfected cells were starved in 4% (v/v) FBS medium for the next 16 h. To stimulate the VEGF-C/NRP-2 axis, the cells were treated with 100 ng/ml human recombinant VEGF-C (PeproTech Inc., Rocky Hill, NJ, USA) for the indicated times.

    Techniques:

    Effect of the inhibition of the VEGF-C/NRP-2 axis on the metastasis of thyroid cancer cells. NRP-2-overexpressing (A and B) K1 and (C and D) WRO cells were treated with VEGF-C (100 ng/ml) plus or minus PD98059, SB203580 or SB202190. Bar graphs represent

    Journal: Oncology Letters

    Article Title: Promotion of metastasis of thyroid cancer cells via NRP-2-mediated induction

    doi: 10.3892/ol.2016.5153

    Figure Lengend Snippet: Effect of the inhibition of the VEGF-C/NRP-2 axis on the metastasis of thyroid cancer cells. NRP-2-overexpressing (A and B) K1 and (C and D) WRO cells were treated with VEGF-C (100 ng/ml) plus or minus PD98059, SB203580 or SB202190. Bar graphs represent

    Article Snippet: In brief, cells were seeded in 6-well culture plates (0.5–1.0×106 cells/ml/well) and transfected with 8 µg expression plasmid for 36 h. Transfected cells were starved in 4% (v/v) FBS medium for the next 16 h. To stimulate the VEGF-C/NRP-2 axis, the cells were treated with 100 ng/ml human recombinant VEGF-C (PeproTech Inc., Rocky Hill, NJ, USA) for the indicated times.

    Techniques: Inhibition

    Effect of the VEGF-C/NRP-2 axis on cell proliferation of thyroid cancer cells. NRP-2-overexpressing (A and B) K1 and (C and D) WRO cells were treated with VEGF-C (100 ng/ml) plus or minus PD98059, SB203580 or SB202190 for (A and C) 8 h or (B and D) 24

    Journal: Oncology Letters

    Article Title: Promotion of metastasis of thyroid cancer cells via NRP-2-mediated induction

    doi: 10.3892/ol.2016.5153

    Figure Lengend Snippet: Effect of the VEGF-C/NRP-2 axis on cell proliferation of thyroid cancer cells. NRP-2-overexpressing (A and B) K1 and (C and D) WRO cells were treated with VEGF-C (100 ng/ml) plus or minus PD98059, SB203580 or SB202190 for (A and C) 8 h or (B and D) 24

    Article Snippet: In brief, cells were seeded in 6-well culture plates (0.5–1.0×106 cells/ml/well) and transfected with 8 µg expression plasmid for 36 h. Transfected cells were starved in 4% (v/v) FBS medium for the next 16 h. To stimulate the VEGF-C/NRP-2 axis, the cells were treated with 100 ng/ml human recombinant VEGF-C (PeproTech Inc., Rocky Hill, NJ, USA) for the indicated times.

    Techniques:

    NRP-2 blocking signals suppress VEGF-C-induced metastasis. NRP-2-overexpressing (A) K1 and (B) WRO cells were pretreated with an NRP-2 function-blocking antibody (0.5 µg/ml) for 1.5 h, and then stimulated with VEGF-C (100 ng/ml) for 10 min. The

    Journal: Oncology Letters

    Article Title: Promotion of metastasis of thyroid cancer cells via NRP-2-mediated induction

    doi: 10.3892/ol.2016.5153

    Figure Lengend Snippet: NRP-2 blocking signals suppress VEGF-C-induced metastasis. NRP-2-overexpressing (A) K1 and (B) WRO cells were pretreated with an NRP-2 function-blocking antibody (0.5 µg/ml) for 1.5 h, and then stimulated with VEGF-C (100 ng/ml) for 10 min. The

    Article Snippet: In brief, cells were seeded in 6-well culture plates (0.5–1.0×106 cells/ml/well) and transfected with 8 µg expression plasmid for 36 h. Transfected cells were starved in 4% (v/v) FBS medium for the next 16 h. To stimulate the VEGF-C/NRP-2 axis, the cells were treated with 100 ng/ml human recombinant VEGF-C (PeproTech Inc., Rocky Hill, NJ, USA) for the indicated times.

    Techniques: Blocking Assay

    Effect of PD, SB and SB2 on the VEGF-C/NRP-2 axis. NRP-2-overexpressing K1 and WRO cells were either pretreated with (A and B) PD (25 µM), (C and D) SB (10 µM), (E and F) SB2 (20 µM) or DMSO for 30 min, and then stimulated with

    Journal: Oncology Letters

    Article Title: Promotion of metastasis of thyroid cancer cells via NRP-2-mediated induction

    doi: 10.3892/ol.2016.5153

    Figure Lengend Snippet: Effect of PD, SB and SB2 on the VEGF-C/NRP-2 axis. NRP-2-overexpressing K1 and WRO cells were either pretreated with (A and B) PD (25 µM), (C and D) SB (10 µM), (E and F) SB2 (20 µM) or DMSO for 30 min, and then stimulated with

    Article Snippet: In brief, cells were seeded in 6-well culture plates (0.5–1.0×106 cells/ml/well) and transfected with 8 µg expression plasmid for 36 h. Transfected cells were starved in 4% (v/v) FBS medium for the next 16 h. To stimulate the VEGF-C/NRP-2 axis, the cells were treated with 100 ng/ml human recombinant VEGF-C (PeproTech Inc., Rocky Hill, NJ, USA) for the indicated times.

    Techniques: