cleaved caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cleaved caspase 3
    Galectin-3 knockdown induced cell cycle arrest and apoptosis in T24 cells. a Comparison of normalized galectin-3 mRNA expression levels in patients without lymph node metastasis (N0, n  = 73) and with lymph node metastasis ( ≥ N1, n  = 43) in the TCGA Nature 2014 cohort. b Kaplan-Meier plots of cumulative overall survival (OS) were calculated for patients with low and high levels of galectin-3 expression in TCGA Nature 2014 cohort ( n  = 129, left panel) and TCGA provisional cohort ( n  = 405, right panel). Lower quartile was determined as the cut-point. c Knockdown of galectin-3 by two different siRNAs (siGal3-1 and siGal3-2), using nontarget siRNA as a negative control (siNC). d Galectin-3 knockdown impaired the viability of UBC cells. e – g Galectin-3 knockdown induced G 2 /M cell cycle arrest in UBC cells. Quantification of cell cycle distribution ( e ), a representative cell cycle distribution pattern ( f ) and expression levels of G 2 /M phase transition regulators ( g ) were shown for the T24 cells with galectin-3 siRNA treatment. h Galectin-3 knockdown triggered <t>Caspase-3</t> activities in UBC cells. i Effects of galectin-3 knockdown on apoptotic proteins and Akt signalings by Western blotting assay. j Galectin-3 knockdown partially rescued the inhibitory effect of MCP on cell viability in T24 cells. 48 h after siGal3-1 or siNC transfection, 1% MCP was applied to T24 cells for additional 48 h. Cell viability was assessed using the SRB assay. Bars represented mean ± SD. * P  
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    1) Product Images from "Modified citrus pectin inhibited bladder tumor growth through downregulation of galectin-3"

    Article Title: Modified citrus pectin inhibited bladder tumor growth through downregulation of galectin-3

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/s41401-018-0004-z

    Galectin-3 knockdown induced cell cycle arrest and apoptosis in T24 cells. a Comparison of normalized galectin-3 mRNA expression levels in patients without lymph node metastasis (N0, n  = 73) and with lymph node metastasis ( ≥ N1, n  = 43) in the TCGA Nature 2014 cohort. b Kaplan-Meier plots of cumulative overall survival (OS) were calculated for patients with low and high levels of galectin-3 expression in TCGA Nature 2014 cohort ( n  = 129, left panel) and TCGA provisional cohort ( n  = 405, right panel). Lower quartile was determined as the cut-point. c Knockdown of galectin-3 by two different siRNAs (siGal3-1 and siGal3-2), using nontarget siRNA as a negative control (siNC). d Galectin-3 knockdown impaired the viability of UBC cells. e – g Galectin-3 knockdown induced G 2 /M cell cycle arrest in UBC cells. Quantification of cell cycle distribution ( e ), a representative cell cycle distribution pattern ( f ) and expression levels of G 2 /M phase transition regulators ( g ) were shown for the T24 cells with galectin-3 siRNA treatment. h Galectin-3 knockdown triggered Caspase-3 activities in UBC cells. i Effects of galectin-3 knockdown on apoptotic proteins and Akt signalings by Western blotting assay. j Galectin-3 knockdown partially rescued the inhibitory effect of MCP on cell viability in T24 cells. 48 h after siGal3-1 or siNC transfection, 1% MCP was applied to T24 cells for additional 48 h. Cell viability was assessed using the SRB assay. Bars represented mean ± SD. * P  
    Figure Legend Snippet: Galectin-3 knockdown induced cell cycle arrest and apoptosis in T24 cells. a Comparison of normalized galectin-3 mRNA expression levels in patients without lymph node metastasis (N0, n  = 73) and with lymph node metastasis ( ≥ N1, n  = 43) in the TCGA Nature 2014 cohort. b Kaplan-Meier plots of cumulative overall survival (OS) were calculated for patients with low and high levels of galectin-3 expression in TCGA Nature 2014 cohort ( n  = 129, left panel) and TCGA provisional cohort ( n  = 405, right panel). Lower quartile was determined as the cut-point. c Knockdown of galectin-3 by two different siRNAs (siGal3-1 and siGal3-2), using nontarget siRNA as a negative control (siNC). d Galectin-3 knockdown impaired the viability of UBC cells. e – g Galectin-3 knockdown induced G 2 /M cell cycle arrest in UBC cells. Quantification of cell cycle distribution ( e ), a representative cell cycle distribution pattern ( f ) and expression levels of G 2 /M phase transition regulators ( g ) were shown for the T24 cells with galectin-3 siRNA treatment. h Galectin-3 knockdown triggered Caspase-3 activities in UBC cells. i Effects of galectin-3 knockdown on apoptotic proteins and Akt signalings by Western blotting assay. j Galectin-3 knockdown partially rescued the inhibitory effect of MCP on cell viability in T24 cells. 48 h after siGal3-1 or siNC transfection, 1% MCP was applied to T24 cells for additional 48 h. Cell viability was assessed using the SRB assay. Bars represented mean ± SD. * P  

    Techniques Used: Expressing, Negative Control, Sublimation, Western Blot, Transfection, Sulforhodamine B Assay

    MCP inhibited the growth of UBC xenografts in vivo. Tumor volume ( a ) and body weight ( b ) of T24 xenograft-bearing mice with MCP treatment for 6 weeks. Three experimental groups, including 700 mg/kg MCP, 350 mg/kg MCP and Vehicle control, were measured. Photograph ( c ) and the average weights ( d ) of T24 xenografts harvested at the endpoint. e Representative images of IHC staining for Ki67, cleaved Caspase-3 (cv Caspase-3) and Galectin-3 on tissue sections from MCP and vehicle-treated T24 xenografts. f Proliferation index and apoptosis index were quantified by the positive IHC staining for Ki67 and cleaved Caspase-3, respectively. Bars represented the mean ± SD. n.s. , P  ≥ 0.05; * P  
    Figure Legend Snippet: MCP inhibited the growth of UBC xenografts in vivo. Tumor volume ( a ) and body weight ( b ) of T24 xenograft-bearing mice with MCP treatment for 6 weeks. Three experimental groups, including 700 mg/kg MCP, 350 mg/kg MCP and Vehicle control, were measured. Photograph ( c ) and the average weights ( d ) of T24 xenografts harvested at the endpoint. e Representative images of IHC staining for Ki67, cleaved Caspase-3 (cv Caspase-3) and Galectin-3 on tissue sections from MCP and vehicle-treated T24 xenografts. f Proliferation index and apoptosis index were quantified by the positive IHC staining for Ki67 and cleaved Caspase-3, respectively. Bars represented the mean ± SD. n.s. , P  ≥ 0.05; * P  

    Techniques Used: In Vivo, Mouse Assay, Immunohistochemistry, Staining

    MCP induced apoptosis in UBC cells. a Caspase-3 activities in T24 and J82 cells treated with MCP at indicated concentrations for 48 h. Bars represented mean ± SD vs. vehicle control. * P  
    Figure Legend Snippet: MCP induced apoptosis in UBC cells. a Caspase-3 activities in T24 and J82 cells treated with MCP at indicated concentrations for 48 h. Bars represented mean ± SD vs. vehicle control. * P  

    Techniques Used:

    2) Product Images from "Re-investigating the Basement Membrane Zone of Psoriatic Epidermal Lesions: Is Laminin-511 a New Player in Psoriasis Pathogenesis?"

    Article Title: Re-investigating the Basement Membrane Zone of Psoriatic Epidermal Lesions: Is Laminin-511 a New Player in Psoriasis Pathogenesis?

    Journal: Journal of Histochemistry and Cytochemistry

    doi: 10.1369/0022155418782693

    The gene knockdown of laminin-α5 chain of laminin-511 decreases keratinocytes proliferation and increases their apoptosis. (A) Successful laminin-α5 gene knockdown was assessed by laminin-α5 immunofluorescence. (B, C) Laminin-α5 gene knockdown significantly decreased HaCaT cell proliferation (evaluated by Ki-67 immunofluorescence), whereas it increased apoptosis (evaluated by cleaved caspase-3 immunofluorescence). (D, E) The decreased proliferation of HaCaT cells by laminin-α5 gene knockdown was recovered by laminin-511 treatment (at 1 μg/ml), whereas the significantly increased apoptosis by laminin-α5 gene knockdown was partially diminished by the co-administration of laminin-511. (* p
    Figure Legend Snippet: The gene knockdown of laminin-α5 chain of laminin-511 decreases keratinocytes proliferation and increases their apoptosis. (A) Successful laminin-α5 gene knockdown was assessed by laminin-α5 immunofluorescence. (B, C) Laminin-α5 gene knockdown significantly decreased HaCaT cell proliferation (evaluated by Ki-67 immunofluorescence), whereas it increased apoptosis (evaluated by cleaved caspase-3 immunofluorescence). (D, E) The decreased proliferation of HaCaT cells by laminin-α5 gene knockdown was recovered by laminin-511 treatment (at 1 μg/ml), whereas the significantly increased apoptosis by laminin-α5 gene knockdown was partially diminished by the co-administration of laminin-511. (* p

    Techniques Used: Immunofluorescence

    Laminin-511 stimulates keratinocytes proliferation and inhibits their apoptosis. (A) (Upper images) Representative images of Ki-67 immunofluorescence. Green indicates Ki-67 positive immunoreactivity. (Lower graph) Laminin-511 at 1 μg/ml significantly increased HaCaT cells proliferation compared with the control evaluated by Ki-67 immunofluorescence. (B) (Upper images) Representative images of cleaved caspase-3 immunofluorescence. Green indicates cleaved caspase-3 positive immunoreactivity. (Lower graph) Laminin-511 at 0.1 μg/ml and 10 μg/ml significantly decreased apoptosis assessed by cleaved caspase-3 immunofluorescence. (** p
    Figure Legend Snippet: Laminin-511 stimulates keratinocytes proliferation and inhibits their apoptosis. (A) (Upper images) Representative images of Ki-67 immunofluorescence. Green indicates Ki-67 positive immunoreactivity. (Lower graph) Laminin-511 at 1 μg/ml significantly increased HaCaT cells proliferation compared with the control evaluated by Ki-67 immunofluorescence. (B) (Upper images) Representative images of cleaved caspase-3 immunofluorescence. Green indicates cleaved caspase-3 positive immunoreactivity. (Lower graph) Laminin-511 at 0.1 μg/ml and 10 μg/ml significantly decreased apoptosis assessed by cleaved caspase-3 immunofluorescence. (** p

    Techniques Used: Immunofluorescence

    3) Product Images from "Neuroprotective effects of lutein in a rat model of retinal detachment"

    Article Title: Neuroprotective effects of lutein in a rat model of retinal detachment

    Journal: Graefe's Archive for Clinical and Experimental Ophthalmology

    doi: 10.1007/s00417-012-2128-z

    a Cleaved caspase-3; b Cleaved caspase-8. Western blot analysis ( a ) with normalized densitometry quantifications of activity using eyes from experiment 1 ( b ) and experiment 3 ( c ). Veh-L vehicle left control eyes; Veh-R vehicle right RD eyes; Lut-L lutein left control eyes; Lut-R lutein right RD eyes. Significant reduction of cleaved caspase-3 level was seen in experiment 3, but the reduction was not statistically significant in experiment 1. Significant reduction of cleaved caspase-8 level was seen in experiment 1, but the reduction was not statistically significant in experiment 3. (* p
    Figure Legend Snippet: a Cleaved caspase-3; b Cleaved caspase-8. Western blot analysis ( a ) with normalized densitometry quantifications of activity using eyes from experiment 1 ( b ) and experiment 3 ( c ). Veh-L vehicle left control eyes; Veh-R vehicle right RD eyes; Lut-L lutein left control eyes; Lut-R lutein right RD eyes. Significant reduction of cleaved caspase-3 level was seen in experiment 3, but the reduction was not statistically significant in experiment 1. Significant reduction of cleaved caspase-8 level was seen in experiment 1, but the reduction was not statistically significant in experiment 3. (* p

    Techniques Used: Western Blot, Activity Assay

    4) Product Images from "Endoplasmic reticulum associated degradation is required for maintaining endoplasmic reticulum homeostasis and viability of mature Schwann cells in adults"

    Article Title: Endoplasmic reticulum associated degradation is required for maintaining endoplasmic reticulum homeostasis and viability of mature Schwann cells in adults

    Journal: Glia

    doi: 10.1002/glia.23910

    PERK inactivation exacerbated SC loss in the PNS of adult Sel1L cKO mice. A-D, M, N. S100 and cleaved caspase-3 (CC3) double immunostaining showed that the number of SCs was significantly reduced in the sciatic nerve of 16-w-old Sel1L cKO mice compared to PERK cKO mice and control mice, and was further reduced in Double cKO mice. Importantly, the number of cleaved-caspase 3 positive SCs (arrow) was significantly increased in Sel1L cKO mice compared to PERK cKO mice and control mice, and was further increased in Double cKO mice. ND, undetectable. E-H, O, P. Krox-20 and c-Jun double immunostaining showed that the number of Krox-20 positive cells was significantly decreased in the sciatic nerve of 16-w-old Sel1L cKO mice compared to PERK cKO mice and control mice, and was further decreased in Double cKO mice. The number of c-Jun positive cells in the sciatic nerve of 16-w-old Sel1L cKO mice was significantly increased compared to PERK cKO mice and control mice, but was not significantly changed compared to Double cKO mice. Arrow, Krox-20 and c-Jun double positive cells; arrowhead, c-Jun positive cells. I-L, Q. EM analysis showed that neither Sel1L deficiency nor PERK inactivation alter the morphology of SCs or the morphology of the ER (insets) in SCs in the sciatic nerve of 16-w-old mice. Importantly, double deficiency of Sel1L and PERK led to significantly enlarged ER lumen (insets) in SCs in the sciatic nerve of 16-w-old mice. Scale bars: A-D, 50 μm; G-J, 1.0 μm. N = 4 animals. Statistical analyses were done with a 1-way ANOVA with a Tukeys posttest. Error bars represent SD, P
    Figure Legend Snippet: PERK inactivation exacerbated SC loss in the PNS of adult Sel1L cKO mice. A-D, M, N. S100 and cleaved caspase-3 (CC3) double immunostaining showed that the number of SCs was significantly reduced in the sciatic nerve of 16-w-old Sel1L cKO mice compared to PERK cKO mice and control mice, and was further reduced in Double cKO mice. Importantly, the number of cleaved-caspase 3 positive SCs (arrow) was significantly increased in Sel1L cKO mice compared to PERK cKO mice and control mice, and was further increased in Double cKO mice. ND, undetectable. E-H, O, P. Krox-20 and c-Jun double immunostaining showed that the number of Krox-20 positive cells was significantly decreased in the sciatic nerve of 16-w-old Sel1L cKO mice compared to PERK cKO mice and control mice, and was further decreased in Double cKO mice. The number of c-Jun positive cells in the sciatic nerve of 16-w-old Sel1L cKO mice was significantly increased compared to PERK cKO mice and control mice, but was not significantly changed compared to Double cKO mice. Arrow, Krox-20 and c-Jun double positive cells; arrowhead, c-Jun positive cells. I-L, Q. EM analysis showed that neither Sel1L deficiency nor PERK inactivation alter the morphology of SCs or the morphology of the ER (insets) in SCs in the sciatic nerve of 16-w-old mice. Importantly, double deficiency of Sel1L and PERK led to significantly enlarged ER lumen (insets) in SCs in the sciatic nerve of 16-w-old mice. Scale bars: A-D, 50 μm; G-J, 1.0 μm. N = 4 animals. Statistical analyses were done with a 1-way ANOVA with a Tukeys posttest. Error bars represent SD, P

    Techniques Used: Mouse Assay, Double Immunostaining

    5) Product Images from "Vitamin K1 Exerts Antiproliferative Effects and Induces Apoptosis in Three Differently Graded Human Colon Cancer Cell Lines"

    Article Title: Vitamin K1 Exerts Antiproliferative Effects and Induces Apoptosis in Three Differently Graded Human Colon Cancer Cell Lines

    Journal: BioMed Research International

    doi: 10.1155/2015/296721

    Western blot analysis of caspase-3 and caspase-9 in Caco-2, HT-29, and SW480 cells after 48 h of vitamin K1 (VK1) treatment. The cells were exposed to increasing concentrations of VK1 (10 μ M, 50 μ M, 100 μ M, and 200 μ M). Immunoreactive bands were quantified using Quantity One program.
    Figure Legend Snippet: Western blot analysis of caspase-3 and caspase-9 in Caco-2, HT-29, and SW480 cells after 48 h of vitamin K1 (VK1) treatment. The cells were exposed to increasing concentrations of VK1 (10 μ M, 50 μ M, 100 μ M, and 200 μ M). Immunoreactive bands were quantified using Quantity One program.

    Techniques Used: Western Blot

    6) Product Images from "Baicalin provides neuroprotection in traumatic brain injury mice model through Akt/Nrf2 pathway"

    Article Title: Baicalin provides neuroprotection in traumatic brain injury mice model through Akt/Nrf2 pathway

    Journal: Drug Design, Development and Therapy

    doi: 10.2147/DDDT.S163951

    Effects of Akt on Baicalin-induced neuroprotection and activation of Nrf2. Notes: The Western blot bands and semiquantitative analysis of p-Akt, n-Nrf2, c-Nrf2, and t-Nrf2 ( A and B ). The Western blot bands and semiquantitative analysis of p-Akt, Bcl2, Bax, and cleaved-caspase 3 ( C and D ). The Western blot bands and semiquantitative analysis of GPx1 and SOD1 ( E and F ). Lipid peroxidation was represented by MDA level ( G ). Data are represented as mean ± SD (n=5 per group). ns P > 0.05, # P
    Figure Legend Snippet: Effects of Akt on Baicalin-induced neuroprotection and activation of Nrf2. Notes: The Western blot bands and semiquantitative analysis of p-Akt, n-Nrf2, c-Nrf2, and t-Nrf2 ( A and B ). The Western blot bands and semiquantitative analysis of p-Akt, Bcl2, Bax, and cleaved-caspase 3 ( C and D ). The Western blot bands and semiquantitative analysis of GPx1 and SOD1 ( E and F ). Lipid peroxidation was represented by MDA level ( G ). Data are represented as mean ± SD (n=5 per group). ns P > 0.05, # P

    Techniques Used: Activation Assay, Western Blot, Multiple Displacement Amplification

    Baicalin suppressed neural apoptosis induced by TBI. Notes: ( A ) Representative images of TUNEL staining surrounding injury site in four groups at 400× magnification. ( B ) The apoptotic index significantly increased in TBI and TBI + V groups, and Baicalin treatment reversed the change. ( C – E ) The Western blot bands and semiquantitative analysis of Bcl-2, Bax, and cleaved caspase 3. Data are represented as mean ± SD (n=5, per group). ## P
    Figure Legend Snippet: Baicalin suppressed neural apoptosis induced by TBI. Notes: ( A ) Representative images of TUNEL staining surrounding injury site in four groups at 400× magnification. ( B ) The apoptotic index significantly increased in TBI and TBI + V groups, and Baicalin treatment reversed the change. ( C – E ) The Western blot bands and semiquantitative analysis of Bcl-2, Bax, and cleaved caspase 3. Data are represented as mean ± SD (n=5, per group). ## P

    Techniques Used: TUNEL Assay, Staining, Western Blot

    7) Product Images from "Reoxygenation Reverses Hypoxic Pulmonary Arterial Remodeling by Inducing Smooth Muscle Cell Apoptosis via Reactive Oxygen Species–Mediated Mitochondrial Dysfunction"

    Article Title: Reoxygenation Reverses Hypoxic Pulmonary Arterial Remodeling by Inducing Smooth Muscle Cell Apoptosis via Reactive Oxygen Species–Mediated Mitochondrial Dysfunction

    Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

    doi: 10.1161/JAHA.117.005602

    Mitochondrial reactive oxygen species ( ROS ) facilitated the apoptosis of pulmonary arterial smooth muscle cells ( PASMC s) during reoxygenation in vitro. The total ROS in PASMC s ( > 2×10 4 cells/coverslip), in the absence or presence of indicated antioxidants, was detected by fluorescence microscopy after 2,7‐ dichlorodihydrofluorescein diacetate ( DCFH ‐ DA ) staining (A). At ×200 magnification; Bar, 50 μm. Flow cytometry analyzes mitochondrial ROS in PASMC s ( > 10 6 cells/test) with fluorescent dye Mito SOX red (B). The percentage of mitochondrial ROS ‐positive cells is normalized to the normoxia group and expressed as mean± SEM (n=3 independent experiments) (D). Mitochondrial ROS in isolated mitochondria was determined by assessing the fluorescence with the ROS detection dye DCFH ‐ DA (E). The apoptosis of PASMC s ( > 10 6 cells/test) was determined by flow cytometry with Annexin V‐ FITC / PI staining (C), and the percentage of apoptotic cells is expressed as mean ± SEM (n=3 independent experiments) (F). The expressions of cleaved caspase3 (G) and cleaved PARP (H) were examined by Western blotting. Densitometry analysis of protein abundance was conducted by normalizing to that of β‐actin. Data are normalized to the normoxia group and expressed as means± SEM (n=3 independent experiments). * P
    Figure Legend Snippet: Mitochondrial reactive oxygen species ( ROS ) facilitated the apoptosis of pulmonary arterial smooth muscle cells ( PASMC s) during reoxygenation in vitro. The total ROS in PASMC s ( > 2×10 4 cells/coverslip), in the absence or presence of indicated antioxidants, was detected by fluorescence microscopy after 2,7‐ dichlorodihydrofluorescein diacetate ( DCFH ‐ DA ) staining (A). At ×200 magnification; Bar, 50 μm. Flow cytometry analyzes mitochondrial ROS in PASMC s ( > 10 6 cells/test) with fluorescent dye Mito SOX red (B). The percentage of mitochondrial ROS ‐positive cells is normalized to the normoxia group and expressed as mean± SEM (n=3 independent experiments) (D). Mitochondrial ROS in isolated mitochondria was determined by assessing the fluorescence with the ROS detection dye DCFH ‐ DA (E). The apoptosis of PASMC s ( > 10 6 cells/test) was determined by flow cytometry with Annexin V‐ FITC / PI staining (C), and the percentage of apoptotic cells is expressed as mean ± SEM (n=3 independent experiments) (F). The expressions of cleaved caspase3 (G) and cleaved PARP (H) were examined by Western blotting. Densitometry analysis of protein abundance was conducted by normalizing to that of β‐actin. Data are normalized to the normoxia group and expressed as means± SEM (n=3 independent experiments). * P

    Techniques Used: In Vitro, Fluorescence, Microscopy, Staining, Flow Cytometry, Cytometry, Isolation, Western Blot

    Reoxygenation reversed hypoxia‐induced proliferation as well as apoptosis resistance and increased H 2 O 2 production in lungs. Western blotting analysis of Bax (A), Bcl‐2 (B), cleaved caspase3 (D), cleaved‐ PARP (E), and PCNA (F) expressions in rat lungs was performed with β‐actin as an internal control. The protein ratio of Bax to Bcl‐2 was also calculated (C). H 2 O 2 levels in lung tissues were examined (G). Data are normalized to those of the normoxia group and expressed as means± SEM (n=4 independent experiments). * P
    Figure Legend Snippet: Reoxygenation reversed hypoxia‐induced proliferation as well as apoptosis resistance and increased H 2 O 2 production in lungs. Western blotting analysis of Bax (A), Bcl‐2 (B), cleaved caspase3 (D), cleaved‐ PARP (E), and PCNA (F) expressions in rat lungs was performed with β‐actin as an internal control. The protein ratio of Bax to Bcl‐2 was also calculated (C). H 2 O 2 levels in lung tissues were examined (G). Data are normalized to those of the normoxia group and expressed as means± SEM (n=4 independent experiments). * P

    Techniques Used: Western Blot

    Reoxygenation‐induced pulmonary arterial smooth muscle cells ( PASMC ) apoptosis of periphery pulmonary arteries. Paraffin sections of peripheral rat lungs were subjected to TUNEL analysis (A) and immunostaining for cleaved caspase3 (B), Bax (E), and Bcl‐2 (F) to evaluate the apoptosis of PASMC s in pulmonary arterial medial layer (30 to 100 μm in diameter). Representative images of TUNEL at ×200 magnification. Bar, 100 μm. White arrows point to TUNEL ‐positive nuclei. The images of cleaved caspase3, Bax, and Bcl‐2 at ×400 magnification. Bar, 40 μm. Blinded quantitative analysis of the staining was performed. Bar charts showing the number of TUNEL ‐positive nuclei per vessel (C) and staining density ([integral optical density]/area; IOD /area) of cleaved caspase3 (D), Bax (G), and Bcl‐2 (H) of different groups. Data are expressed as means± SEM (n=3‐5 animals, 30 vessels/3 sections of an animal). * P
    Figure Legend Snippet: Reoxygenation‐induced pulmonary arterial smooth muscle cells ( PASMC ) apoptosis of periphery pulmonary arteries. Paraffin sections of peripheral rat lungs were subjected to TUNEL analysis (A) and immunostaining for cleaved caspase3 (B), Bax (E), and Bcl‐2 (F) to evaluate the apoptosis of PASMC s in pulmonary arterial medial layer (30 to 100 μm in diameter). Representative images of TUNEL at ×200 magnification. Bar, 100 μm. White arrows point to TUNEL ‐positive nuclei. The images of cleaved caspase3, Bax, and Bcl‐2 at ×400 magnification. Bar, 40 μm. Blinded quantitative analysis of the staining was performed. Bar charts showing the number of TUNEL ‐positive nuclei per vessel (C) and staining density ([integral optical density]/area; IOD /area) of cleaved caspase3 (D), Bax (G), and Bcl‐2 (H) of different groups. Data are expressed as means± SEM (n=3‐5 animals, 30 vessels/3 sections of an animal). * P

    Techniques Used: TUNEL Assay, Immunostaining, Staining

    The apoptosis and proliferation of pulmonary arterial smooth muscle cells ( PASMC s) increased during reoxygenation in vitro. The apoptosis of PASMC s ( > 10 6 cells/test) was measured by flow cytometry with Annexin V‐ FITC / PI staining (A). The proliferation of PASMC s ( > 2×10 4 cells/coverslip) was determined by BrdU (5‐bromo‐2′‐deoxyuridine) incorporation assay (B). At ×200 magnification; Bar, 100 μm. The black arrows point to the BrdU‐positive nuclei. Bar charts showing the percentages of apoptotic cells (C) and BrdU‐positive cells (D). The apoptosis was normalized to corresponding proliferation of PASMC s (E). Western blotting analysis of cleaved caspase3 (F), cleaved‐ PARP (G), and PCNA (H) expressions in PASMC s ( > 2×10 6 cells/sample) was performed with β‐actin as an internal control. Densitometry analysis of protein abundance was conducted by normalizing to that of β‐actin. Data are expressed as means ± SEM (n=3‐4 independent experiments). * P
    Figure Legend Snippet: The apoptosis and proliferation of pulmonary arterial smooth muscle cells ( PASMC s) increased during reoxygenation in vitro. The apoptosis of PASMC s ( > 10 6 cells/test) was measured by flow cytometry with Annexin V‐ FITC / PI staining (A). The proliferation of PASMC s ( > 2×10 4 cells/coverslip) was determined by BrdU (5‐bromo‐2′‐deoxyuridine) incorporation assay (B). At ×200 magnification; Bar, 100 μm. The black arrows point to the BrdU‐positive nuclei. Bar charts showing the percentages of apoptotic cells (C) and BrdU‐positive cells (D). The apoptosis was normalized to corresponding proliferation of PASMC s (E). Western blotting analysis of cleaved caspase3 (F), cleaved‐ PARP (G), and PCNA (H) expressions in PASMC s ( > 2×10 6 cells/sample) was performed with β‐actin as an internal control. Densitometry analysis of protein abundance was conducted by normalizing to that of β‐actin. Data are expressed as means ± SEM (n=3‐4 independent experiments). * P

    Techniques Used: In Vitro, Flow Cytometry, Cytometry, Staining, BrdU Incorporation Assay, Western Blot

    8) Product Images from "Restoration of Autophagic Flux Rescues Oxidative Damage and Mitochondrial Dysfunction to Protect against Intervertebral Disc Degeneration"

    Article Title: Restoration of Autophagic Flux Rescues Oxidative Damage and Mitochondrial Dysfunction to Protect against Intervertebral Disc Degeneration

    Journal: Oxidative Medicine and Cellular Longevity

    doi: 10.1155/2019/7810320

    CUR treatment inhibits TBHP-induced apoptosis and senescence in human NP cells. (a, b) Annexin V-APC/7-AAD staining results showing the rate of apoptosis in human NP cells. (c–i) The protein levels of mitochondrial Cyt-c, cytoplasmic Cyt-c, Bax, Bcl-2, cleaved caspase-3, and cleaved caspase-9 in human NP cells were measured by western blotting. (j, k) Immunofluorescence staining of cleaved caspase-3 in human NP cells. Scale bar: 20 μ m. (l–o) After the indicated treatment, cells were washed and then cultured under normal conditions for the indicated time. (l, m) After 24 h, the level of p16 protein in the human NP cells was measured by western blotting. (n, o) After 3 days, the SA- β -gal staining assay was performed in the human NP cells. Scale bar: 100 μ m. (p, q) Cell proliferation was detected by EdU staining under a fluorescence microscope, and the positive cells were quantitated. Scale bar: 50 μ m. GAPDH was used as an internal control. Data are represented as the mean ± SD. ∗∗ P
    Figure Legend Snippet: CUR treatment inhibits TBHP-induced apoptosis and senescence in human NP cells. (a, b) Annexin V-APC/7-AAD staining results showing the rate of apoptosis in human NP cells. (c–i) The protein levels of mitochondrial Cyt-c, cytoplasmic Cyt-c, Bax, Bcl-2, cleaved caspase-3, and cleaved caspase-9 in human NP cells were measured by western blotting. (j, k) Immunofluorescence staining of cleaved caspase-3 in human NP cells. Scale bar: 20 μ m. (l–o) After the indicated treatment, cells were washed and then cultured under normal conditions for the indicated time. (l, m) After 24 h, the level of p16 protein in the human NP cells was measured by western blotting. (n, o) After 3 days, the SA- β -gal staining assay was performed in the human NP cells. Scale bar: 100 μ m. (p, q) Cell proliferation was detected by EdU staining under a fluorescence microscope, and the positive cells were quantitated. Scale bar: 50 μ m. GAPDH was used as an internal control. Data are represented as the mean ± SD. ∗∗ P

    Techniques Used: Staining, Western Blot, Immunofluorescence, Cell Culture, Fluorescence, Microscopy

    CUR treatment ameliorates rat IDD in vivo . (a) The discs from the tails of rats obtained from different treatment groups were examined using MRI at T2-weighted signal (white arrows). (b, c) HE and SO staining of the whole rat tail disc. Scale bar: 1 mm. (d) Quantitative analysis of the degree of disc degeneration based on the Pfirrmann grade system using MRI images. (e) The histological scores of the tail discs according to the histological grading scale. (f–h) The levels of type II collagen, aggrecan, MMP-13, ADAMTS-4, ADAMTS-5, LC3, p62, and cleaved caspase-3 proteins in the disc samples obtained from the rat models were measured by western blotting. (i) Immunohistochemical staining showing the expression of type II collagen, MMP-13, LC3, p62, and cleaved-caspase3 proteins in the disc samples of the rat model. (j) The content of H 2 O 2 in the disc samples. Scale bar: 40 μ m. GAPDH was used as an internal control. Data are represented as the mean ± SD. ∗∗ P
    Figure Legend Snippet: CUR treatment ameliorates rat IDD in vivo . (a) The discs from the tails of rats obtained from different treatment groups were examined using MRI at T2-weighted signal (white arrows). (b, c) HE and SO staining of the whole rat tail disc. Scale bar: 1 mm. (d) Quantitative analysis of the degree of disc degeneration based on the Pfirrmann grade system using MRI images. (e) The histological scores of the tail discs according to the histological grading scale. (f–h) The levels of type II collagen, aggrecan, MMP-13, ADAMTS-4, ADAMTS-5, LC3, p62, and cleaved caspase-3 proteins in the disc samples obtained from the rat models were measured by western blotting. (i) Immunohistochemical staining showing the expression of type II collagen, MMP-13, LC3, p62, and cleaved-caspase3 proteins in the disc samples of the rat model. (j) The content of H 2 O 2 in the disc samples. Scale bar: 40 μ m. GAPDH was used as an internal control. Data are represented as the mean ± SD. ∗∗ P

    Techniques Used: In Vivo, Magnetic Resonance Imaging, Staining, Western Blot, Immunohistochemistry, Expressing

    CUR treatment inhibits TBHP-induced apoptosis and senescence in the human NP cells by facilitating autophagic flux. (a–c) The protein levels of LC3and p62 in the human NP cells were measured by western blotting. (d, e) Annexin V-APC/7-AAD staining results showing the apoptosis rate of the human NP cells. (f–l) The expression of mitochondrial Cyt-c, cytoplasmic Cyt-c, Bax, Bcl-2, cleaved caspase-3, and cleaved caspase-9 proteins was measured by western blotting. (f, m–o) Cells were treated as indicated in the legend of Figures 2(l) – 2(o) . (f, m) The expression of p16 protein was measured by western blotting. (n, o) SA- β -gal staining assay was performed in the human NP cells. Scale bar: 100 μ m. GAPDH was used as an internal control. Data are represented as the mean ± SD. ∗∗ P
    Figure Legend Snippet: CUR treatment inhibits TBHP-induced apoptosis and senescence in the human NP cells by facilitating autophagic flux. (a–c) The protein levels of LC3and p62 in the human NP cells were measured by western blotting. (d, e) Annexin V-APC/7-AAD staining results showing the apoptosis rate of the human NP cells. (f–l) The expression of mitochondrial Cyt-c, cytoplasmic Cyt-c, Bax, Bcl-2, cleaved caspase-3, and cleaved caspase-9 proteins was measured by western blotting. (f, m–o) Cells were treated as indicated in the legend of Figures 2(l) – 2(o) . (f, m) The expression of p16 protein was measured by western blotting. (n, o) SA- β -gal staining assay was performed in the human NP cells. Scale bar: 100 μ m. GAPDH was used as an internal control. Data are represented as the mean ± SD. ∗∗ P

    Techniques Used: Western Blot, Staining, Expressing

    9) Product Images from "Overexpression of colorectal cancer oncogene CHRDL2 predicts a poor prognosis"

    Article Title: Overexpression of colorectal cancer oncogene CHRDL2 predicts a poor prognosis

    Journal: Oncotarget

    doi: 10.18632/oncotarget.14039

    CHRDL2 blocks the BMP2 and attenuates the effect of promoting proliferation and inhibiting apoptosis induced by BMP2 in HCT116 cells A . Cell-cycle analysis by flow cytometry in HCT116 cells treated with 100 ng/ml BMP2 or 100 ng/ml CHRDL2. The histograms show the ratio of different cell phase populations (G0/G1, S and G2/M cells) in treated HCT116 cells.  B . Apoptosis analysis by flow cytometry in HCT116 cells treated with 100 ng/ml BMP2 or 100 ng/ml CHRDL2. The histograms show the apoptosis rate in treated HCT116 cells.  C . Western blot analysis was used to measure the P21, Cyclin D1, Cleaved caspase 9 and Cleaved caspase 3 in the lysis of HCT116 cells treated with 100 ng/ml BMP2 or 100 ng/ml CHRDL2.
    Figure Legend Snippet: CHRDL2 blocks the BMP2 and attenuates the effect of promoting proliferation and inhibiting apoptosis induced by BMP2 in HCT116 cells A . Cell-cycle analysis by flow cytometry in HCT116 cells treated with 100 ng/ml BMP2 or 100 ng/ml CHRDL2. The histograms show the ratio of different cell phase populations (G0/G1, S and G2/M cells) in treated HCT116 cells. B . Apoptosis analysis by flow cytometry in HCT116 cells treated with 100 ng/ml BMP2 or 100 ng/ml CHRDL2. The histograms show the apoptosis rate in treated HCT116 cells. C . Western blot analysis was used to measure the P21, Cyclin D1, Cleaved caspase 9 and Cleaved caspase 3 in the lysis of HCT116 cells treated with 100 ng/ml BMP2 or 100 ng/ml CHRDL2.

    Techniques Used: Cell Cycle Assay, Flow Cytometry, Western Blot, Lysis

    10) Product Images from "The Src homology-2 protein Shb modulates focal adhesion kinase signaling in a BCR-ABL myeloproliferative disorder causing accelerated progression of disease"

    Article Title: The Src homology-2 protein Shb modulates focal adhesion kinase signaling in a BCR-ABL myeloproliferative disorder causing accelerated progression of disease

    Journal: Journal of Hematology & Oncology

    doi: 10.1186/1756-8722-7-45

    Proliferation and apoptosis in BCR-ABL + hematopoietic progenitors assessed by flow cytometric analysis of Ki-67 and cleaved Caspase-3. (a, b and c) The cell cycle status in BCR-ABL + Lin - c-Kit + and BCR-ABL + Lin + bone marrow was examined by staining for proliferation marker Ki-67 in combination with the DNA binding dye Hoechst 33342. FACS plots are representative of an average experiment. (a and d) The staining for presence of cleaved Caspase-3 was used to determine the percentage of apoptotic cells within the BCR-ABL + Lin - c-Kit + population. FACS plots are representative of a typical experiment. Data are presented as mean values ± SEM with 9 mice from each genotype from 3 independent experiments. *denotes p
    Figure Legend Snippet: Proliferation and apoptosis in BCR-ABL + hematopoietic progenitors assessed by flow cytometric analysis of Ki-67 and cleaved Caspase-3. (a, b and c) The cell cycle status in BCR-ABL + Lin - c-Kit + and BCR-ABL + Lin + bone marrow was examined by staining for proliferation marker Ki-67 in combination with the DNA binding dye Hoechst 33342. FACS plots are representative of an average experiment. (a and d) The staining for presence of cleaved Caspase-3 was used to determine the percentage of apoptotic cells within the BCR-ABL + Lin - c-Kit + population. FACS plots are representative of a typical experiment. Data are presented as mean values ± SEM with 9 mice from each genotype from 3 independent experiments. *denotes p

    Techniques Used: Flow Cytometry, Staining, Marker, Binding Assay, FACS, Mouse Assay

    11) Product Images from "Intrinsic Neuronal Activity during Migration Controls the Recruitment of Specific Interneuron Subtypes in the Postnatal Mouse Olfactory Bulb"

    Article Title: Intrinsic Neuronal Activity during Migration Controls the Recruitment of Specific Interneuron Subtypes in the Postnatal Mouse Olfactory Bulb

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.1960-20.2021

    Effect of Kir2.1 expression on neuronal cell death.  A , P0 CD1 animals received lateral or medial electroporation with either a Kir2.1 mutant or a functional Kir2.1 encoding plasmid. Mice were then killed at 8 or 12 dpe and the level of apoptotic cell death in tdTomato cells was quantified.  B , OB coronal sections of Kir mutant and Kir2.1 labeled with c-caspase 3 at 12 dpe. Note the presence of a double-labeled cell in the Kir condition.  C ,  D , Quantification of the percentage of c-caspase 3-positive cells among lateral ( C ) or medial ( D ) electroporation of Kir2.1 (Kir) or Kir2.1 mutant (Mut) cells per OB region at 8 dpe (lateral:  N  = 6 animals; medial:  N  = 6 animals) or 12 dpe (lateral:  N  = 7 animals; medial:  N  = 4 animals). There is an increase of c-caspase 3-positive cells after lateral electroporation of Kir2.1 in the GCL at 8 dpe (0.03 ± 0.07 vs 0.4 ± 0.24, Mann–Whitney–Wilcoxon test,  p  = 0.017) and 12 dpe (0.07 ± 0.08 vs 2.5 ± 0.9, Mann–Whitney–Wilcoxon test,  p  = 0.029) but not after medial electroporation.
    Figure Legend Snippet: Effect of Kir2.1 expression on neuronal cell death. A , P0 CD1 animals received lateral or medial electroporation with either a Kir2.1 mutant or a functional Kir2.1 encoding plasmid. Mice were then killed at 8 or 12 dpe and the level of apoptotic cell death in tdTomato cells was quantified. B , OB coronal sections of Kir mutant and Kir2.1 labeled with c-caspase 3 at 12 dpe. Note the presence of a double-labeled cell in the Kir condition. C , D , Quantification of the percentage of c-caspase 3-positive cells among lateral ( C ) or medial ( D ) electroporation of Kir2.1 (Kir) or Kir2.1 mutant (Mut) cells per OB region at 8 dpe (lateral: N = 6 animals; medial: N = 6 animals) or 12 dpe (lateral: N = 7 animals; medial: N = 4 animals). There is an increase of c-caspase 3-positive cells after lateral electroporation of Kir2.1 in the GCL at 8 dpe (0.03 ± 0.07 vs 0.4 ± 0.24, Mann–Whitney–Wilcoxon test, p = 0.017) and 12 dpe (0.07 ± 0.08 vs 2.5 ± 0.9, Mann–Whitney–Wilcoxon test, p = 0.029) but not after medial electroporation.

    Techniques Used: Expressing, Electroporation, Mutagenesis, Functional Assay, Plasmid Preparation, Mouse Assay, Labeling, MANN-WHITNEY

    12) Product Images from "Sulforaphane Alleviates Particulate Matter-Induced Oxidative Stress in Human Retinal Pigment Epithelial Cells"

    Article Title: Sulforaphane Alleviates Particulate Matter-Induced Oxidative Stress in Human Retinal Pigment Epithelial Cells

    Journal: Frontiers in Medicine

    doi: 10.3389/fmed.2021.685032

    Effects of Sulforaphane (SFN) on PM 2.5 -induced changes in apoptosis-related protein levels. (A) ARPE-19 cells were treated with the indicated concentrations of SFN or DEX (1 μM) 24 h after PM 2.5 challenge (100 μg/mL). Subsequently, western blot analysis was conducted to measure Bax, Bcl-2, SGK1, cytochrome c, and cleaved caspase-3. β-actin was used as a loading control. Representative images from each group are shown ( n = 3). (B) The graphs show the densitometric intensities of each gene normalized to β-actin. n = 3 blots. * p
    Figure Legend Snippet: Effects of Sulforaphane (SFN) on PM 2.5 -induced changes in apoptosis-related protein levels. (A) ARPE-19 cells were treated with the indicated concentrations of SFN or DEX (1 μM) 24 h after PM 2.5 challenge (100 μg/mL). Subsequently, western blot analysis was conducted to measure Bax, Bcl-2, SGK1, cytochrome c, and cleaved caspase-3. β-actin was used as a loading control. Representative images from each group are shown ( n = 3). (B) The graphs show the densitometric intensities of each gene normalized to β-actin. n = 3 blots. * p

    Techniques Used: Western Blot

    13) Product Images from "Knockdown of KIF26B inhibits breast cancer cell proliferation, migration, and invasion"

    Article Title: Knockdown of KIF26B inhibits breast cancer cell proliferation, migration, and invasion

    Journal: OncoTargets and therapy

    doi: 10.2147/OTT.S163346

    Downregulation of KIF26B induced cell apoptosis in breast cancer cells. Notes: ( A ) Flow cytometry analysis of breast cancer cell apoptosis using annexin V-FITC and PI dual labeling with or without KIF26B knockdown. ( B ) The percentage of apoptotic cells was calculated. The data are shown as the mean±SD. ( C ) The expression levels of KIF26B, Bcl-2, Bax, and cleaved caspase-3 in MCF-7 cells (left panel) and MDA-MB-231 cells (right panel) were measured by western blotting. ( D ) qRT-PCR analysis of KIF26B, Bcl-2, and Bax expression in MCF-7 and MDA-MB-231 cells. Each experiment was repeated three times. * p
    Figure Legend Snippet: Downregulation of KIF26B induced cell apoptosis in breast cancer cells. Notes: ( A ) Flow cytometry analysis of breast cancer cell apoptosis using annexin V-FITC and PI dual labeling with or without KIF26B knockdown. ( B ) The percentage of apoptotic cells was calculated. The data are shown as the mean±SD. ( C ) The expression levels of KIF26B, Bcl-2, Bax, and cleaved caspase-3 in MCF-7 cells (left panel) and MDA-MB-231 cells (right panel) were measured by western blotting. ( D ) qRT-PCR analysis of KIF26B, Bcl-2, and Bax expression in MCF-7 and MDA-MB-231 cells. Each experiment was repeated three times. * p

    Techniques Used: Flow Cytometry, Cytometry, Labeling, Expressing, Multiple Displacement Amplification, Western Blot, Quantitative RT-PCR

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    Cell Signaling Technology Inc caspase 7
    Caspase-3, caspase-6 and <t>caspase-7</t> activations induced by GalXM in Jurkat cells
    Caspase 7, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc cleaved caspase 3
    Galectin-3 knockdown induced cell cycle arrest and apoptosis in T24 cells. a Comparison of normalized galectin-3 mRNA expression levels in patients without lymph node metastasis (N0, n  = 73) and with lymph node metastasis ( ≥ N1, n  = 43) in the TCGA Nature 2014 cohort. b Kaplan-Meier plots of cumulative overall survival (OS) were calculated for patients with low and high levels of galectin-3 expression in TCGA Nature 2014 cohort ( n  = 129, left panel) and TCGA provisional cohort ( n  = 405, right panel). Lower quartile was determined as the cut-point. c Knockdown of galectin-3 by two different siRNAs (siGal3-1 and siGal3-2), using nontarget siRNA as a negative control (siNC). d Galectin-3 knockdown impaired the viability of UBC cells. e – g Galectin-3 knockdown induced G 2 /M cell cycle arrest in UBC cells. Quantification of cell cycle distribution ( e ), a representative cell cycle distribution pattern ( f ) and expression levels of G 2 /M phase transition regulators ( g ) were shown for the T24 cells with galectin-3 siRNA treatment. h Galectin-3 knockdown triggered <t>Caspase-3</t> activities in UBC cells. i Effects of galectin-3 knockdown on apoptotic proteins and Akt signalings by Western blotting assay. j Galectin-3 knockdown partially rescued the inhibitory effect of MCP on cell viability in T24 cells. 48 h after siGal3-1 or siNC transfection, 1% MCP was applied to T24 cells for additional 48 h. Cell viability was assessed using the SRB assay. Bars represented mean ± SD. * P  
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    <t>Caspase-3</t> protein expression was significantly elevated in all extrinsic muscles of old rats compared to young adult rats (genioglossus, A; styloglossus, B; hyoglossus, C). (* signifies p
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    Caspase-3, caspase-6 and caspase-7 activations induced by GalXM in Jurkat cells

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

    Article Title: Involvement of glyco-receptors in Galactoxylomannan-induced T cell death

    doi: 10.4049/jimmunol.0803833

    Figure Lengend Snippet: Caspase-3, caspase-6 and caspase-7 activations induced by GalXM in Jurkat cells

    Article Snippet: The lysates (30 μg of each sample) were separated by sodium dodecyl-sulfate-10% PAGE, transferred to a nitrocellulose membrane (Pierce) for 1 h at 100 V in a blotting system (Bio-Rad, Hercules, CA) for western blot analysis, and the membranes were incubated overnight with rabbit polyclonal Abs to human FasL (1 μg/ml) (Calbiochem, VWR Int.), BID, caspase-3, caspase-6, caspase-7, caspase-9 and mouse polyclonal Ab to human caspase-8 (all dilution 1/1000) (all from Cell Signalling Technology) in blocking buffer.

    Techniques:

    Galectin-3 knockdown induced cell cycle arrest and apoptosis in T24 cells. a Comparison of normalized galectin-3 mRNA expression levels in patients without lymph node metastasis (N0, n  = 73) and with lymph node metastasis ( ≥ N1, n  = 43) in the TCGA Nature 2014 cohort. b Kaplan-Meier plots of cumulative overall survival (OS) were calculated for patients with low and high levels of galectin-3 expression in TCGA Nature 2014 cohort ( n  = 129, left panel) and TCGA provisional cohort ( n  = 405, right panel). Lower quartile was determined as the cut-point. c Knockdown of galectin-3 by two different siRNAs (siGal3-1 and siGal3-2), using nontarget siRNA as a negative control (siNC). d Galectin-3 knockdown impaired the viability of UBC cells. e – g Galectin-3 knockdown induced G 2 /M cell cycle arrest in UBC cells. Quantification of cell cycle distribution ( e ), a representative cell cycle distribution pattern ( f ) and expression levels of G 2 /M phase transition regulators ( g ) were shown for the T24 cells with galectin-3 siRNA treatment. h Galectin-3 knockdown triggered Caspase-3 activities in UBC cells. i Effects of galectin-3 knockdown on apoptotic proteins and Akt signalings by Western blotting assay. j Galectin-3 knockdown partially rescued the inhibitory effect of MCP on cell viability in T24 cells. 48 h after siGal3-1 or siNC transfection, 1% MCP was applied to T24 cells for additional 48 h. Cell viability was assessed using the SRB assay. Bars represented mean ± SD. * P  

    Journal: Acta Pharmacologica Sinica

    Article Title: Modified citrus pectin inhibited bladder tumor growth through downregulation of galectin-3

    doi: 10.1038/s41401-018-0004-z

    Figure Lengend Snippet: Galectin-3 knockdown induced cell cycle arrest and apoptosis in T24 cells. a Comparison of normalized galectin-3 mRNA expression levels in patients without lymph node metastasis (N0, n  = 73) and with lymph node metastasis ( ≥ N1, n  = 43) in the TCGA Nature 2014 cohort. b Kaplan-Meier plots of cumulative overall survival (OS) were calculated for patients with low and high levels of galectin-3 expression in TCGA Nature 2014 cohort ( n  = 129, left panel) and TCGA provisional cohort ( n  = 405, right panel). Lower quartile was determined as the cut-point. c Knockdown of galectin-3 by two different siRNAs (siGal3-1 and siGal3-2), using nontarget siRNA as a negative control (siNC). d Galectin-3 knockdown impaired the viability of UBC cells. e – g Galectin-3 knockdown induced G 2 /M cell cycle arrest in UBC cells. Quantification of cell cycle distribution ( e ), a representative cell cycle distribution pattern ( f ) and expression levels of G 2 /M phase transition regulators ( g ) were shown for the T24 cells with galectin-3 siRNA treatment. h Galectin-3 knockdown triggered Caspase-3 activities in UBC cells. i Effects of galectin-3 knockdown on apoptotic proteins and Akt signalings by Western blotting assay. j Galectin-3 knockdown partially rescued the inhibitory effect of MCP on cell viability in T24 cells. 48 h after siGal3-1 or siNC transfection, 1% MCP was applied to T24 cells for additional 48 h. Cell viability was assessed using the SRB assay. Bars represented mean ± SD. * P  

    Article Snippet: Moreover, galectin-3 gene knockdown activated Caspase-3 (Fig. ) and increased the accumulation of cleaved Caspase-3 and cleaved PARP (Fig. ).

    Techniques: Expressing, Negative Control, Sublimation, Western Blot, Transfection, Sulforhodamine B Assay

    MCP inhibited the growth of UBC xenografts in vivo. Tumor volume ( a ) and body weight ( b ) of T24 xenograft-bearing mice with MCP treatment for 6 weeks. Three experimental groups, including 700 mg/kg MCP, 350 mg/kg MCP and Vehicle control, were measured. Photograph ( c ) and the average weights ( d ) of T24 xenografts harvested at the endpoint. e Representative images of IHC staining for Ki67, cleaved Caspase-3 (cv Caspase-3) and Galectin-3 on tissue sections from MCP and vehicle-treated T24 xenografts. f Proliferation index and apoptosis index were quantified by the positive IHC staining for Ki67 and cleaved Caspase-3, respectively. Bars represented the mean ± SD. n.s. , P  ≥ 0.05; * P  

    Journal: Acta Pharmacologica Sinica

    Article Title: Modified citrus pectin inhibited bladder tumor growth through downregulation of galectin-3

    doi: 10.1038/s41401-018-0004-z

    Figure Lengend Snippet: MCP inhibited the growth of UBC xenografts in vivo. Tumor volume ( a ) and body weight ( b ) of T24 xenograft-bearing mice with MCP treatment for 6 weeks. Three experimental groups, including 700 mg/kg MCP, 350 mg/kg MCP and Vehicle control, were measured. Photograph ( c ) and the average weights ( d ) of T24 xenografts harvested at the endpoint. e Representative images of IHC staining for Ki67, cleaved Caspase-3 (cv Caspase-3) and Galectin-3 on tissue sections from MCP and vehicle-treated T24 xenografts. f Proliferation index and apoptosis index were quantified by the positive IHC staining for Ki67 and cleaved Caspase-3, respectively. Bars represented the mean ± SD. n.s. , P  ≥ 0.05; * P  

    Article Snippet: Moreover, galectin-3 gene knockdown activated Caspase-3 (Fig. ) and increased the accumulation of cleaved Caspase-3 and cleaved PARP (Fig. ).

    Techniques: In Vivo, Mouse Assay, Immunohistochemistry, Staining

    MCP induced apoptosis in UBC cells. a Caspase-3 activities in T24 and J82 cells treated with MCP at indicated concentrations for 48 h. Bars represented mean ± SD vs. vehicle control. * P  

    Journal: Acta Pharmacologica Sinica

    Article Title: Modified citrus pectin inhibited bladder tumor growth through downregulation of galectin-3

    doi: 10.1038/s41401-018-0004-z

    Figure Lengend Snippet: MCP induced apoptosis in UBC cells. a Caspase-3 activities in T24 and J82 cells treated with MCP at indicated concentrations for 48 h. Bars represented mean ± SD vs. vehicle control. * P  

    Article Snippet: Moreover, galectin-3 gene knockdown activated Caspase-3 (Fig. ) and increased the accumulation of cleaved Caspase-3 and cleaved PARP (Fig. ).

    Techniques:

    The gene knockdown of laminin-α5 chain of laminin-511 decreases keratinocytes proliferation and increases their apoptosis. (A) Successful laminin-α5 gene knockdown was assessed by laminin-α5 immunofluorescence. (B, C) Laminin-α5 gene knockdown significantly decreased HaCaT cell proliferation (evaluated by Ki-67 immunofluorescence), whereas it increased apoptosis (evaluated by cleaved caspase-3 immunofluorescence). (D, E) The decreased proliferation of HaCaT cells by laminin-α5 gene knockdown was recovered by laminin-511 treatment (at 1 μg/ml), whereas the significantly increased apoptosis by laminin-α5 gene knockdown was partially diminished by the co-administration of laminin-511. (* p

    Journal: Journal of Histochemistry and Cytochemistry

    Article Title: Re-investigating the Basement Membrane Zone of Psoriatic Epidermal Lesions: Is Laminin-511 a New Player in Psoriasis Pathogenesis?

    doi: 10.1369/0022155418782693

    Figure Lengend Snippet: The gene knockdown of laminin-α5 chain of laminin-511 decreases keratinocytes proliferation and increases their apoptosis. (A) Successful laminin-α5 gene knockdown was assessed by laminin-α5 immunofluorescence. (B, C) Laminin-α5 gene knockdown significantly decreased HaCaT cell proliferation (evaluated by Ki-67 immunofluorescence), whereas it increased apoptosis (evaluated by cleaved caspase-3 immunofluorescence). (D, E) The decreased proliferation of HaCaT cells by laminin-α5 gene knockdown was recovered by laminin-511 treatment (at 1 μg/ml), whereas the significantly increased apoptosis by laminin-α5 gene knockdown was partially diminished by the co-administration of laminin-511. (* p

    Article Snippet: For HaCaT cells, a mouse monoclonal antibody against human laminin-α5 (Merk, Millipore), a mouse monoclonal antibody against Ki-67 (MIB-1, M7240; Dako; Santa Clara, CA), and a rabbit polyclonal antibody against cleaved caspase-3 (D175; Cell Signaling Technology; Danvers, CO) were used.

    Techniques: Immunofluorescence

    Laminin-511 stimulates keratinocytes proliferation and inhibits their apoptosis. (A) (Upper images) Representative images of Ki-67 immunofluorescence. Green indicates Ki-67 positive immunoreactivity. (Lower graph) Laminin-511 at 1 μg/ml significantly increased HaCaT cells proliferation compared with the control evaluated by Ki-67 immunofluorescence. (B) (Upper images) Representative images of cleaved caspase-3 immunofluorescence. Green indicates cleaved caspase-3 positive immunoreactivity. (Lower graph) Laminin-511 at 0.1 μg/ml and 10 μg/ml significantly decreased apoptosis assessed by cleaved caspase-3 immunofluorescence. (** p

    Journal: Journal of Histochemistry and Cytochemistry

    Article Title: Re-investigating the Basement Membrane Zone of Psoriatic Epidermal Lesions: Is Laminin-511 a New Player in Psoriasis Pathogenesis?

    doi: 10.1369/0022155418782693

    Figure Lengend Snippet: Laminin-511 stimulates keratinocytes proliferation and inhibits their apoptosis. (A) (Upper images) Representative images of Ki-67 immunofluorescence. Green indicates Ki-67 positive immunoreactivity. (Lower graph) Laminin-511 at 1 μg/ml significantly increased HaCaT cells proliferation compared with the control evaluated by Ki-67 immunofluorescence. (B) (Upper images) Representative images of cleaved caspase-3 immunofluorescence. Green indicates cleaved caspase-3 positive immunoreactivity. (Lower graph) Laminin-511 at 0.1 μg/ml and 10 μg/ml significantly decreased apoptosis assessed by cleaved caspase-3 immunofluorescence. (** p

    Article Snippet: For HaCaT cells, a mouse monoclonal antibody against human laminin-α5 (Merk, Millipore), a mouse monoclonal antibody against Ki-67 (MIB-1, M7240; Dako; Santa Clara, CA), and a rabbit polyclonal antibody against cleaved caspase-3 (D175; Cell Signaling Technology; Danvers, CO) were used.

    Techniques: Immunofluorescence

    Caspase-3 protein expression was significantly elevated in all extrinsic muscles of old rats compared to young adult rats (genioglossus, A; styloglossus, B; hyoglossus, C). (* signifies p

    Journal: Muscle & nerve

    Article Title: “Age-related effect of cell death on fiber morphology and number in tongue muscle” 1

    doi: 10.1002/mus.25671

    Figure Lengend Snippet: Caspase-3 protein expression was significantly elevated in all extrinsic muscles of old rats compared to young adult rats (genioglossus, A; styloglossus, B; hyoglossus, C). (* signifies p

    Article Snippet: An age-related increase in the full length caspase-3 protein may suggest that extrinsic tongue muscles are more susceptible to apoptosis., , , The absence of the activated, cleaved form of caspase-3, may mean that few muscles fibers are actively undergoing apoptosis at the 32 month time-point or may, in fact, be indicative of a caspase-independent pathway of age-related myonuclear loss., , , , Misregulation of these apoptotic processes may have deleterious consequences in the affected tissue., In aging tongue muscle, alterations in the apoptotic regulator proteins, Bcl-2 and caspase-3, resulting in increased activation of apoptotic processes, may have led to the removal of individual myonuclei, the associated sarcoplasm, , and contributed to the eventual atrophy and loss of muscle fibers we observed in the genioglossus and styloglossus muscles of old rats.

    Techniques: Expressing