cleaved caspase 3 rabbit 9664s ab 10831820 cst  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cleaved caspase 3 rabbit 9664s ab 10831820 cst
    Cleaved Caspase 3 Rabbit 9664s Ab 10831820 Cst, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    primary antibodies against caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc primary antibodies against caspase 3
    Primers used for reverse transcription-quantitative PCR.
    Primary Antibodies Against Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "18‑α‑glycyrrhetinic acid induces apoptosis in gingival fibroblasts exposed to phenytoin"

    Article Title: 18‑α‑glycyrrhetinic acid induces apoptosis in gingival fibroblasts exposed to phenytoin

    Journal: Experimental and Therapeutic Medicine

    doi: 10.3892/etm.2024.12586

    Primers used for reverse transcription-quantitative PCR.
    Figure Legend Snippet: Primers used for reverse transcription-quantitative PCR.

    Techniques Used: Sequencing

    Schematic representation of apoptosis accelerated by 18α-GA in gingival fibroblasts treated with phenytoin. 18α-GA induced the upregulation of FADD and caspase-3, leading to an increase in the apoptotic Fas pathway. 18α-GA also induced the upregulation of RIPK1, CRADD, caspase-2, caspase-9 and caspase-3 in the TNF pathway, which resulted in apoptosis acceleration. Furthermore, 18α-GA decreased BCL2, which increased caspase-9. Purple (components of death-inducing signaling complex), red (antiapoptotic factors) and yellow (caspases) ellipses denote the molecules analyzed in the present study. The blue or red large arrows denote upregulation or downregulation, respectively, following 18α-GA treatment. Hyphens denote the molecules that are unaffected by 18α-GA treatment. 18α-GA, 18-α-glycyrrhetinic acid; BIRC3, baculoviral IAP repeat containing 3; CFLAR, CASP8 and FADD-like apoptosis regulator; CRADD, CASP2 and RIPK1 domain containing adaptor with death domain; FADD, Fas (TNFRSF6)-associated via death domain; RIPK1, receptor (TNFRSF)-interacting serine-threonine kinase 1; TNFRSF1A, tumor necrosis factor receptor superfamily; member 1A; TRADD, TNFRSF1A associated via death domain; TRAF2, TNF receptor-associated factor 2.
    Figure Legend Snippet: Schematic representation of apoptosis accelerated by 18α-GA in gingival fibroblasts treated with phenytoin. 18α-GA induced the upregulation of FADD and caspase-3, leading to an increase in the apoptotic Fas pathway. 18α-GA also induced the upregulation of RIPK1, CRADD, caspase-2, caspase-9 and caspase-3 in the TNF pathway, which resulted in apoptosis acceleration. Furthermore, 18α-GA decreased BCL2, which increased caspase-9. Purple (components of death-inducing signaling complex), red (antiapoptotic factors) and yellow (caspases) ellipses denote the molecules analyzed in the present study. The blue or red large arrows denote upregulation or downregulation, respectively, following 18α-GA treatment. Hyphens denote the molecules that are unaffected by 18α-GA treatment. 18α-GA, 18-α-glycyrrhetinic acid; BIRC3, baculoviral IAP repeat containing 3; CFLAR, CASP8 and FADD-like apoptosis regulator; CRADD, CASP2 and RIPK1 domain containing adaptor with death domain; FADD, Fas (TNFRSF6)-associated via death domain; RIPK1, receptor (TNFRSF)-interacting serine-threonine kinase 1; TNFRSF1A, tumor necrosis factor receptor superfamily; member 1A; TRADD, TNFRSF1A associated via death domain; TRAF2, TNF receptor-associated factor 2.

    Techniques Used:

    caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc caspase 3
    Cytoprotective effect of luteolin on H 2 O 2 -induced apoptosis. (A) MTT assay was used to assess cell viability. *P<0.05 vs. control; # P<0.05 vs. H 2 O 2 . (B) Apoptotic bodies (arrow) were revealed by Hoechst 33342 staining. (C) Sub-G 1 cells, which is indicative of apoptosis, were identified by flow cytometry. (D) Western blot analysis with antibodies against Bax, Bcl-2, active caspase-9 <t>and</t> <t>caspase-3</t> was performed. β-actin was employed as a loading control.
    Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Protective effect of luteolin against oxidative stress‑mediated cell injury via enhancing antioxidant systems"

    Article Title: Protective effect of luteolin against oxidative stress‑mediated cell injury via enhancing antioxidant systems

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2024.13244

    Cytoprotective effect of luteolin on H 2 O 2 -induced apoptosis. (A) MTT assay was used to assess cell viability. *P<0.05 vs. control; # P<0.05 vs. H 2 O 2 . (B) Apoptotic bodies (arrow) were revealed by Hoechst 33342 staining. (C) Sub-G 1 cells, which is indicative of apoptosis, were identified by flow cytometry. (D) Western blot analysis with antibodies against Bax, Bcl-2, active caspase-9 and caspase-3 was performed. β-actin was employed as a loading control.
    Figure Legend Snippet: Cytoprotective effect of luteolin on H 2 O 2 -induced apoptosis. (A) MTT assay was used to assess cell viability. *P<0.05 vs. control; # P<0.05 vs. H 2 O 2 . (B) Apoptotic bodies (arrow) were revealed by Hoechst 33342 staining. (C) Sub-G 1 cells, which is indicative of apoptosis, were identified by flow cytometry. (D) Western blot analysis with antibodies against Bax, Bcl-2, active caspase-9 and caspase-3 was performed. β-actin was employed as a loading control.

    Techniques Used: MTT Assay, Staining, Flow Cytometry, Western Blot

    caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc caspase 3
    Primers used for reverse transcription-quantitative PCR.
    Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Astragaloside IV protects against autoimmune myasthenia gravis in rats via regulation of mitophagy and apoptosis"

    Article Title: Astragaloside IV protects against autoimmune myasthenia gravis in rats via regulation of mitophagy and apoptosis

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2024.13253

    Primers used for reverse transcription-quantitative PCR.
    Figure Legend Snippet: Primers used for reverse transcription-quantitative PCR.

    Techniques Used:

    Effects of AS-IV on mRNA expression related to mitochondrial apoptosis. Reverse transcription-quantitative PCR was used to analyze mRNA expression. Effect of AS-IV on the mRNA expression levels of (A) Bax, (B) Bcl-2, (C) Cyt-C, (D) caspase 3 and (E) caspase 9; n=8. **P<0.01 vs. control group; # P<0.05, ## P<0.01 vs. model group. AS-IV, astragaloside IV; Cyt-C, cytochrome c ; H-ASIV, high-dose AS-IV; L-ASIV, low-dose AS-IV.
    Figure Legend Snippet: Effects of AS-IV on mRNA expression related to mitochondrial apoptosis. Reverse transcription-quantitative PCR was used to analyze mRNA expression. Effect of AS-IV on the mRNA expression levels of (A) Bax, (B) Bcl-2, (C) Cyt-C, (D) caspase 3 and (E) caspase 9; n=8. **P<0.01 vs. control group; # P<0.05, ## P<0.01 vs. model group. AS-IV, astragaloside IV; Cyt-C, cytochrome c ; H-ASIV, high-dose AS-IV; L-ASIV, low-dose AS-IV.

    Techniques Used: Expressing, Reverse Transcription, Real-time Polymerase Chain Reaction

    Effects of AS-IV on the expression of proteins related to mitochondrial apoptosis. (A) Western blotting was used to analyze protein expression. Effect of AS-IV on the protein expression levels of (B) Bax, (C) Bcl-2, (D) Cyt-C, (E) caspase 3 and (F) caspase 9; n=8. **P<0.01 vs. control group; # P<0.05, ## P<0.01 vs. model group. AS-IV, astragaloside IV; Cyt-C, cytochrome c ; H-ASIV, high-dose AS-IV; L-ASIV, low-dose AS-IV.
    Figure Legend Snippet: Effects of AS-IV on the expression of proteins related to mitochondrial apoptosis. (A) Western blotting was used to analyze protein expression. Effect of AS-IV on the protein expression levels of (B) Bax, (C) Bcl-2, (D) Cyt-C, (E) caspase 3 and (F) caspase 9; n=8. **P<0.01 vs. control group; # P<0.05, ## P<0.01 vs. model group. AS-IV, astragaloside IV; Cyt-C, cytochrome c ; H-ASIV, high-dose AS-IV; L-ASIV, low-dose AS-IV.

    Techniques Used: Expressing, Western Blot

    3 cleaved caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc 3 cleaved caspase 3
    3 Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti caspase 3 antibodies  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti caspase 3 antibodies
    Antiapoptotic influence of insulin on ER stress‐induced cell death in INS‐1 β‐cells. INS‐1 cells were incubated in the presence of insulin (1 μM) and tunicamycin (3 μM) for 48 h (a), 36 h (b, c). (a) DNA laddering was evaluated. The results were representative of three independent experiments. (b, c) Cell lysates were analyzed by western blotting <t>with</t> <t>anti‐cleaved</t> <t>caspase‐3</t> and total caspase‐3 (b) or with anti‐cleaved caspase‐9 and total caspase‐9 (c) antibodies. Representative blots and densitometry analysis are shown. Graph is shown as mean ± SD ( n = 4). Asterisk indicates statistically significant differences ( p < 0.05, Student's t ‐test). N.D, not detected.
    Anti Caspase 3 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Insulin reduces endoplasmic reticulum stress‐induced apoptosis by decreasing mitochondrial hyperpolarization and caspase‐12 in INS ‐1 pancreatic β‐cells"

    Article Title: Insulin reduces endoplasmic reticulum stress‐induced apoptosis by decreasing mitochondrial hyperpolarization and caspase‐12 in INS ‐1 pancreatic β‐cells

    Journal: Physiological Reports

    doi: 10.14814/phy2.16106

    Antiapoptotic influence of insulin on ER stress‐induced cell death in INS‐1 β‐cells. INS‐1 cells were incubated in the presence of insulin (1 μM) and tunicamycin (3 μM) for 48 h (a), 36 h (b, c). (a) DNA laddering was evaluated. The results were representative of three independent experiments. (b, c) Cell lysates were analyzed by western blotting with anti‐cleaved caspase‐3 and total caspase‐3 (b) or with anti‐cleaved caspase‐9 and total caspase‐9 (c) antibodies. Representative blots and densitometry analysis are shown. Graph is shown as mean ± SD ( n = 4). Asterisk indicates statistically significant differences ( p < 0.05, Student's t ‐test). N.D, not detected.
    Figure Legend Snippet: Antiapoptotic influence of insulin on ER stress‐induced cell death in INS‐1 β‐cells. INS‐1 cells were incubated in the presence of insulin (1 μM) and tunicamycin (3 μM) for 48 h (a), 36 h (b, c). (a) DNA laddering was evaluated. The results were representative of three independent experiments. (b, c) Cell lysates were analyzed by western blotting with anti‐cleaved caspase‐3 and total caspase‐3 (b) or with anti‐cleaved caspase‐9 and total caspase‐9 (c) antibodies. Representative blots and densitometry analysis are shown. Graph is shown as mean ± SD ( n = 4). Asterisk indicates statistically significant differences ( p < 0.05, Student's t ‐test). N.D, not detected.

    Techniques Used: Incubation, DNA Laddering, Western Blot

    Involvement of caspase‐12 in ER stress‐induced apoptosis in INS‐1 cells. (a) INS‐1 cells were incubated with tunicamycin (3 μM) for indicated time. The cell lysates were analyzed with western blotting with anti‐caspase‐12 and α‐tubulin antibodies. (b–d) INS‐1 cells that had pretreated with Z‐ATAD‐FMK (50 μM) for 1 h were incubated with 3 μM tunicamycin for 36 h. Cell viability was determined using AlamarBlue dye (b). The cell lysates were analyzed with western blotting with anti‐caspase‐9, anti‐caspase‐3, and α‐tubulin antibodies. Subsequently, band intensity was determined (c, d). Graph is shown as mean ± SD ( n = 3 or 4). Different letters indicate statistically significant differences ( p < 0.05, ANOVA, Tukey–Kramer's test). Asterisk indicates statistically significant differences ( p < 0.05, Student's t ‐test). N.D, not detected.
    Figure Legend Snippet: Involvement of caspase‐12 in ER stress‐induced apoptosis in INS‐1 cells. (a) INS‐1 cells were incubated with tunicamycin (3 μM) for indicated time. The cell lysates were analyzed with western blotting with anti‐caspase‐12 and α‐tubulin antibodies. (b–d) INS‐1 cells that had pretreated with Z‐ATAD‐FMK (50 μM) for 1 h were incubated with 3 μM tunicamycin for 36 h. Cell viability was determined using AlamarBlue dye (b). The cell lysates were analyzed with western blotting with anti‐caspase‐9, anti‐caspase‐3, and α‐tubulin antibodies. Subsequently, band intensity was determined (c, d). Graph is shown as mean ± SD ( n = 3 or 4). Different letters indicate statistically significant differences ( p < 0.05, ANOVA, Tukey–Kramer's test). Asterisk indicates statistically significant differences ( p < 0.05, Student's t ‐test). N.D, not detected.

    Techniques Used: Incubation, Western Blot

    anti caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti caspase 3
    Lig improves DOX-induced cardiac toxicity in mice by activating AMPK/SIRT1 signaling and alleviating pyroptosis mediated <t>by</t> <t>caspase-3/GSDME.</t> A Representative western blotting images and statistical results of p-AMPK, AMPK and SIRT3 in mice (n = 3). B Effects of Lig on heart levels of ATP in mice caused by DOX (n = 5). C , D The serum levels of IL-1β and IL-18 of mice measured by ELISA. E The expression of GSDME-N, cleaved-caspase-3, caspase-3, IL-1β and IL-6 (n = 3). Data are presented as the mean ± SD. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01, ### p < 0.001 compared with model group
    Anti Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Liguzinediol potentiates the metabolic remodeling by activating the AMPK/SIRT3 pathway and represses Caspase-3/GSDME-mediated pyroptosis to ameliorate cardiotoxicity"

    Article Title: Liguzinediol potentiates the metabolic remodeling by activating the AMPK/SIRT3 pathway and represses Caspase-3/GSDME-mediated pyroptosis to ameliorate cardiotoxicity

    Journal: Chinese Medicine

    doi: 10.1186/s13020-024-00955-5

    Lig improves DOX-induced cardiac toxicity in mice by activating AMPK/SIRT1 signaling and alleviating pyroptosis mediated by caspase-3/GSDME. A Representative western blotting images and statistical results of p-AMPK, AMPK and SIRT3 in mice (n = 3). B Effects of Lig on heart levels of ATP in mice caused by DOX (n = 5). C , D The serum levels of IL-1β and IL-18 of mice measured by ELISA. E The expression of GSDME-N, cleaved-caspase-3, caspase-3, IL-1β and IL-6 (n = 3). Data are presented as the mean ± SD. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01, ### p < 0.001 compared with model group
    Figure Legend Snippet: Lig improves DOX-induced cardiac toxicity in mice by activating AMPK/SIRT1 signaling and alleviating pyroptosis mediated by caspase-3/GSDME. A Representative western blotting images and statistical results of p-AMPK, AMPK and SIRT3 in mice (n = 3). B Effects of Lig on heart levels of ATP in mice caused by DOX (n = 5). C , D The serum levels of IL-1β and IL-18 of mice measured by ELISA. E The expression of GSDME-N, cleaved-caspase-3, caspase-3, IL-1β and IL-6 (n = 3). Data are presented as the mean ± SD. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01, ### p < 0.001 compared with model group

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

    Lig treatment inhibits the caspase-3/GSDME signaling pathway in DOX-treated H9C2 cells. A Representative images of PI staining (n = 6). Scale bar represents 50 µm. B Effects of Lig on intracellular LDH level in H9C2 cells treated by DOX (n = 3). C Representative scanning electron microscopy (SEM) images showed the morphological changes of cultured H9C2 under different treatments (n = 3). D H9C2 cells stained with PI were detected by flow cytometry (n = 3). E The protein expression of GSDME-N, cleaved-caspase-3, caspase-3, IL-6, IL-1β in H9C2 cells (n = 3). Data are presented as the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01 compared with model group
    Figure Legend Snippet: Lig treatment inhibits the caspase-3/GSDME signaling pathway in DOX-treated H9C2 cells. A Representative images of PI staining (n = 6). Scale bar represents 50 µm. B Effects of Lig on intracellular LDH level in H9C2 cells treated by DOX (n = 3). C Representative scanning electron microscopy (SEM) images showed the morphological changes of cultured H9C2 under different treatments (n = 3). D H9C2 cells stained with PI were detected by flow cytometry (n = 3). E The protein expression of GSDME-N, cleaved-caspase-3, caspase-3, IL-6, IL-1β in H9C2 cells (n = 3). Data are presented as the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01 compared with model group

    Techniques Used: Staining, Electron Microscopy, Cell Culture, Flow Cytometry, Expressing

    Activation of AMPK/SIRT3 signaling is required for Lig to reduce the mitochondrial respiration and pyroptosis in cardiomyocytes. A Morphology in H9C2 cells. Scale bar represents 100 µm (n = 6). B Intracellular ROS level in H9C2 cells (n = 4). Scale bar represents 50 µm. C MMP level was measured by JC-1 assay kit. Scale bar represents 25 µm (n = 6). D Effects of Lig and CC on intracellular ATP level in H9C2 cells (n = 3). E Representative images of Hochest and PI staining (n = 6). Scale bar represents 50 µm. F The expression of SIRT3, Bax and Bcl-2 in H9C2 cells treated by DOX (n = 3). G H9C2 cells stained with PI were detected by flow cytometry (n = 3). H The protein level of GSDME-N, cleaved-caspase-3, caspase-3, IL-6, IL-1β in H9C2 cells. (n = 3) I Intracellular LDH level in H9C2 cells treated by DOX (n = 3). Data are presented as the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01 compared with model group. ns indicates no significance
    Figure Legend Snippet: Activation of AMPK/SIRT3 signaling is required for Lig to reduce the mitochondrial respiration and pyroptosis in cardiomyocytes. A Morphology in H9C2 cells. Scale bar represents 100 µm (n = 6). B Intracellular ROS level in H9C2 cells (n = 4). Scale bar represents 50 µm. C MMP level was measured by JC-1 assay kit. Scale bar represents 25 µm (n = 6). D Effects of Lig and CC on intracellular ATP level in H9C2 cells (n = 3). E Representative images of Hochest and PI staining (n = 6). Scale bar represents 50 µm. F The expression of SIRT3, Bax and Bcl-2 in H9C2 cells treated by DOX (n = 3). G H9C2 cells stained with PI were detected by flow cytometry (n = 3). H The protein level of GSDME-N, cleaved-caspase-3, caspase-3, IL-6, IL-1β in H9C2 cells. (n = 3) I Intracellular LDH level in H9C2 cells treated by DOX (n = 3). Data are presented as the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01 compared with model group. ns indicates no significance

    Techniques Used: Activation Assay, Staining, Expressing, Flow Cytometry

    Graphical abstract of how Lig ameliorates DOX-induced cardiotoxicity and potentiates the metabolic remodeling by activating the AMPK/SIRT3 pathway and represses Caspase-3/GSDME-mediated pyroptosis
    Figure Legend Snippet: Graphical abstract of how Lig ameliorates DOX-induced cardiotoxicity and potentiates the metabolic remodeling by activating the AMPK/SIRT3 pathway and represses Caspase-3/GSDME-mediated pyroptosis

    Techniques Used:

    caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc caspase 3
    Liraglutide suppresses the expression of GLP-1R and multiple signaling pathways in vivo. ( a , b ) Liraglutide suppresses the expression of GLP-1R in KKU-213A xenografted tumors in vivo. It also inhibits the phosphorylation of Akt and STAT3 consistently with the in vitro experiments. The expressions of downstream targeted proteins of Akt and STAT3, for instance, apoptotic <t>protein-</t> <t>caspase-3</t> is increased, and cell cycle regulatory protein- cyclin D1 is decreased, corresponding with the reduced tumor volumes and tumor weights in mice receiving liraglutide. Each lane of Western blot is from a xenografted tumor in one mouse, where M is the lane loaded with molecular weight marker. (* P < 0.05, *** P < 0.001, Student’s t -test).
    Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Liraglutide exhibits potential anti-tumor effects on the progression of intrahepatic cholangiocarcinoma, in vitro and in vivo"

    Article Title: Liraglutide exhibits potential anti-tumor effects on the progression of intrahepatic cholangiocarcinoma, in vitro and in vivo

    Journal: Scientific Reports

    doi: 10.1038/s41598-024-64774-2

    Liraglutide suppresses the expression of GLP-1R and multiple signaling pathways in vivo. ( a , b ) Liraglutide suppresses the expression of GLP-1R in KKU-213A xenografted tumors in vivo. It also inhibits the phosphorylation of Akt and STAT3 consistently with the in vitro experiments. The expressions of downstream targeted proteins of Akt and STAT3, for instance, apoptotic protein- caspase-3 is increased, and cell cycle regulatory protein- cyclin D1 is decreased, corresponding with the reduced tumor volumes and tumor weights in mice receiving liraglutide. Each lane of Western blot is from a xenografted tumor in one mouse, where M is the lane loaded with molecular weight marker. (* P < 0.05, *** P < 0.001, Student’s t -test).
    Figure Legend Snippet: Liraglutide suppresses the expression of GLP-1R and multiple signaling pathways in vivo. ( a , b ) Liraglutide suppresses the expression of GLP-1R in KKU-213A xenografted tumors in vivo. It also inhibits the phosphorylation of Akt and STAT3 consistently with the in vitro experiments. The expressions of downstream targeted proteins of Akt and STAT3, for instance, apoptotic protein- caspase-3 is increased, and cell cycle regulatory protein- cyclin D1 is decreased, corresponding with the reduced tumor volumes and tumor weights in mice receiving liraglutide. Each lane of Western blot is from a xenografted tumor in one mouse, where M is the lane loaded with molecular weight marker. (* P < 0.05, *** P < 0.001, Student’s t -test).

    Techniques Used: Expressing, In Vivo, In Vitro, Western Blot, Molecular Weight, Marker

    caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc caspase 3
    Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    polyclonal antibodies against caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc polyclonal antibodies against caspase 3
    Polyclonal Antibodies Against Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, 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 rabbit 9664s ab 10831820 cst
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    Primers used for reverse transcription-quantitative PCR.
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    Cell Signaling Technology Inc caspase 3
    Cytoprotective effect of luteolin on H 2 O 2 -induced apoptosis. (A) MTT assay was used to assess cell viability. *P<0.05 vs. control; # P<0.05 vs. H 2 O 2 . (B) Apoptotic bodies (arrow) were revealed by Hoechst 33342 staining. (C) Sub-G 1 cells, which is indicative of apoptosis, were identified by flow cytometry. (D) Western blot analysis with antibodies against Bax, Bcl-2, active caspase-9 <t>and</t> <t>caspase-3</t> was performed. β-actin was employed as a loading control.
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    Cytoprotective effect of luteolin on H 2 O 2 -induced apoptosis. (A) MTT assay was used to assess cell viability. *P<0.05 vs. control; # P<0.05 vs. H 2 O 2 . (B) Apoptotic bodies (arrow) were revealed by Hoechst 33342 staining. (C) Sub-G 1 cells, which is indicative of apoptosis, were identified by flow cytometry. (D) Western blot analysis with antibodies against Bax, Bcl-2, active caspase-9 <t>and</t> <t>caspase-3</t> was performed. β-actin was employed as a loading control.
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    Lig improves DOX-induced cardiac toxicity in mice by activating AMPK/SIRT1 signaling and alleviating pyroptosis mediated <t>by</t> <t>caspase-3/GSDME.</t> A Representative western blotting images and statistical results of p-AMPK, AMPK and SIRT3 in mice (n = 3). B Effects of Lig on heart levels of ATP in mice caused by DOX (n = 5). C , D The serum levels of IL-1β and IL-18 of mice measured by ELISA. E The expression of GSDME-N, cleaved-caspase-3, caspase-3, IL-1β and IL-6 (n = 3). Data are presented as the mean ± SD. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01, ### p < 0.001 compared with model group
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    Primers used for reverse transcription-quantitative PCR.

    Journal: Experimental and Therapeutic Medicine

    Article Title: 18‑α‑glycyrrhetinic acid induces apoptosis in gingival fibroblasts exposed to phenytoin

    doi: 10.3892/etm.2024.12586

    Figure Lengend Snippet: Primers used for reverse transcription-quantitative PCR.

    Article Snippet: Primary antibodies against Caspase-3 (cat. no. #9662), Caspase-9 (cat. no. #9502) and β-Actin (cat. no. #4967), as well as anti-rabbit HRP-conjugated IgG were purchased from Cell Signaling Technology, Inc. (Danvers, MA, USA).

    Techniques: Sequencing

    Schematic representation of apoptosis accelerated by 18α-GA in gingival fibroblasts treated with phenytoin. 18α-GA induced the upregulation of FADD and caspase-3, leading to an increase in the apoptotic Fas pathway. 18α-GA also induced the upregulation of RIPK1, CRADD, caspase-2, caspase-9 and caspase-3 in the TNF pathway, which resulted in apoptosis acceleration. Furthermore, 18α-GA decreased BCL2, which increased caspase-9. Purple (components of death-inducing signaling complex), red (antiapoptotic factors) and yellow (caspases) ellipses denote the molecules analyzed in the present study. The blue or red large arrows denote upregulation or downregulation, respectively, following 18α-GA treatment. Hyphens denote the molecules that are unaffected by 18α-GA treatment. 18α-GA, 18-α-glycyrrhetinic acid; BIRC3, baculoviral IAP repeat containing 3; CFLAR, CASP8 and FADD-like apoptosis regulator; CRADD, CASP2 and RIPK1 domain containing adaptor with death domain; FADD, Fas (TNFRSF6)-associated via death domain; RIPK1, receptor (TNFRSF)-interacting serine-threonine kinase 1; TNFRSF1A, tumor necrosis factor receptor superfamily; member 1A; TRADD, TNFRSF1A associated via death domain; TRAF2, TNF receptor-associated factor 2.

    Journal: Experimental and Therapeutic Medicine

    Article Title: 18‑α‑glycyrrhetinic acid induces apoptosis in gingival fibroblasts exposed to phenytoin

    doi: 10.3892/etm.2024.12586

    Figure Lengend Snippet: Schematic representation of apoptosis accelerated by 18α-GA in gingival fibroblasts treated with phenytoin. 18α-GA induced the upregulation of FADD and caspase-3, leading to an increase in the apoptotic Fas pathway. 18α-GA also induced the upregulation of RIPK1, CRADD, caspase-2, caspase-9 and caspase-3 in the TNF pathway, which resulted in apoptosis acceleration. Furthermore, 18α-GA decreased BCL2, which increased caspase-9. Purple (components of death-inducing signaling complex), red (antiapoptotic factors) and yellow (caspases) ellipses denote the molecules analyzed in the present study. The blue or red large arrows denote upregulation or downregulation, respectively, following 18α-GA treatment. Hyphens denote the molecules that are unaffected by 18α-GA treatment. 18α-GA, 18-α-glycyrrhetinic acid; BIRC3, baculoviral IAP repeat containing 3; CFLAR, CASP8 and FADD-like apoptosis regulator; CRADD, CASP2 and RIPK1 domain containing adaptor with death domain; FADD, Fas (TNFRSF6)-associated via death domain; RIPK1, receptor (TNFRSF)-interacting serine-threonine kinase 1; TNFRSF1A, tumor necrosis factor receptor superfamily; member 1A; TRADD, TNFRSF1A associated via death domain; TRAF2, TNF receptor-associated factor 2.

    Article Snippet: Primary antibodies against Caspase-3 (cat. no. #9662), Caspase-9 (cat. no. #9502) and β-Actin (cat. no. #4967), as well as anti-rabbit HRP-conjugated IgG were purchased from Cell Signaling Technology, Inc. (Danvers, MA, USA).

    Techniques:

    Cytoprotective effect of luteolin on H 2 O 2 -induced apoptosis. (A) MTT assay was used to assess cell viability. *P<0.05 vs. control; # P<0.05 vs. H 2 O 2 . (B) Apoptotic bodies (arrow) were revealed by Hoechst 33342 staining. (C) Sub-G 1 cells, which is indicative of apoptosis, were identified by flow cytometry. (D) Western blot analysis with antibodies against Bax, Bcl-2, active caspase-9 and caspase-3 was performed. β-actin was employed as a loading control.

    Journal: Molecular Medicine Reports

    Article Title: Protective effect of luteolin against oxidative stress‑mediated cell injury via enhancing antioxidant systems

    doi: 10.3892/mmr.2024.13244

    Figure Lengend Snippet: Cytoprotective effect of luteolin on H 2 O 2 -induced apoptosis. (A) MTT assay was used to assess cell viability. *P<0.05 vs. control; # P<0.05 vs. H 2 O 2 . (B) Apoptotic bodies (arrow) were revealed by Hoechst 33342 staining. (C) Sub-G 1 cells, which is indicative of apoptosis, were identified by flow cytometry. (D) Western blot analysis with antibodies against Bax, Bcl-2, active caspase-9 and caspase-3 was performed. β-actin was employed as a loading control.

    Article Snippet: Additionally, 7-amino-4-chloromethylcoumarin (CMAC) and diphenyl-1-pyrenylphosphine (DPPP) were purchased from Molecular Probes (Thermo Fisher Scientific, Inc.) The primary Bax, Bcl-2, GPx, CAT and HO-1 antibodies were obtained from Santa Cruz Biotechnology, Inc.; primary β-actin, phosphorylated (phospho)-H2A histone family member X (H2A.X), H2A.X, caspase-3 and caspase-9 antibodies were obtained from Cell Signaling Technology, Inc.; primary γ-glutamylcysteine ligase (γ-GCL) antibody was obtained from Thermo Fisher Scientific, Inc.; primary Cu/Zn SOD was obtained from Enzo Life Science.

    Techniques: MTT Assay, Staining, Flow Cytometry, Western Blot

    Antiapoptotic influence of insulin on ER stress‐induced cell death in INS‐1 β‐cells. INS‐1 cells were incubated in the presence of insulin (1 μM) and tunicamycin (3 μM) for 48 h (a), 36 h (b, c). (a) DNA laddering was evaluated. The results were representative of three independent experiments. (b, c) Cell lysates were analyzed by western blotting with anti‐cleaved caspase‐3 and total caspase‐3 (b) or with anti‐cleaved caspase‐9 and total caspase‐9 (c) antibodies. Representative blots and densitometry analysis are shown. Graph is shown as mean ± SD ( n = 4). Asterisk indicates statistically significant differences ( p < 0.05, Student's t ‐test). N.D, not detected.

    Journal: Physiological Reports

    Article Title: Insulin reduces endoplasmic reticulum stress‐induced apoptosis by decreasing mitochondrial hyperpolarization and caspase‐12 in INS ‐1 pancreatic β‐cells

    doi: 10.14814/phy2.16106

    Figure Lengend Snippet: Antiapoptotic influence of insulin on ER stress‐induced cell death in INS‐1 β‐cells. INS‐1 cells were incubated in the presence of insulin (1 μM) and tunicamycin (3 μM) for 48 h (a), 36 h (b, c). (a) DNA laddering was evaluated. The results were representative of three independent experiments. (b, c) Cell lysates were analyzed by western blotting with anti‐cleaved caspase‐3 and total caspase‐3 (b) or with anti‐cleaved caspase‐9 and total caspase‐9 (c) antibodies. Representative blots and densitometry analysis are shown. Graph is shown as mean ± SD ( n = 4). Asterisk indicates statistically significant differences ( p < 0.05, Student's t ‐test). N.D, not detected.

    Article Snippet: Western blotting was performed using polyclonal rabbit anti‐caspase‐12 (1/1000, 3282–100, Biovision, Waltham, MA, USA; RRID:AB_2243910), polyclonal rabbit anti‐caspase‐9 (1/3000, #9502, Cell Signaling Technology; RRID:AB_2068621), polyclonal rabbit anti‐cleaved caspase‐3 (Asp175) and polyclonal rabbit anti‐caspase‐3 antibodies (1/3000 for both #9661 and #9662, Cell Signaling Technology, Danvers, MA, USA; RRID:AB_2341188 and RRID:AB_331439), monoclonal mouse anti‐Cox IV antibody (1/5000, 4D11‐B3‐E8, Cell Signaling Technology; RRID:AB_2797784), polyclonal rabbit anti‐triosephosphate isomerase antibody (Yamaji et al., ), monoclonal mouse anti‐cytochrome c (1/1000, 7H8, Santa Cruz Biotechnology, Santa Cruz, CA, USA; RRID:AB_627383), monoclonal mouse anti‐α‐tubulin (1/5000, DM1A, Santa Cruz Biotechnology; RRID:AB_628412), and monoclonal mouse anti‐FLAG antibody (1/5000, M2, Sigma‐Aldrich; RRID:AB_259529).

    Techniques: Incubation, DNA Laddering, Western Blot

    Involvement of caspase‐12 in ER stress‐induced apoptosis in INS‐1 cells. (a) INS‐1 cells were incubated with tunicamycin (3 μM) for indicated time. The cell lysates were analyzed with western blotting with anti‐caspase‐12 and α‐tubulin antibodies. (b–d) INS‐1 cells that had pretreated with Z‐ATAD‐FMK (50 μM) for 1 h were incubated with 3 μM tunicamycin for 36 h. Cell viability was determined using AlamarBlue dye (b). The cell lysates were analyzed with western blotting with anti‐caspase‐9, anti‐caspase‐3, and α‐tubulin antibodies. Subsequently, band intensity was determined (c, d). Graph is shown as mean ± SD ( n = 3 or 4). Different letters indicate statistically significant differences ( p < 0.05, ANOVA, Tukey–Kramer's test). Asterisk indicates statistically significant differences ( p < 0.05, Student's t ‐test). N.D, not detected.

    Journal: Physiological Reports

    Article Title: Insulin reduces endoplasmic reticulum stress‐induced apoptosis by decreasing mitochondrial hyperpolarization and caspase‐12 in INS ‐1 pancreatic β‐cells

    doi: 10.14814/phy2.16106

    Figure Lengend Snippet: Involvement of caspase‐12 in ER stress‐induced apoptosis in INS‐1 cells. (a) INS‐1 cells were incubated with tunicamycin (3 μM) for indicated time. The cell lysates were analyzed with western blotting with anti‐caspase‐12 and α‐tubulin antibodies. (b–d) INS‐1 cells that had pretreated with Z‐ATAD‐FMK (50 μM) for 1 h were incubated with 3 μM tunicamycin for 36 h. Cell viability was determined using AlamarBlue dye (b). The cell lysates were analyzed with western blotting with anti‐caspase‐9, anti‐caspase‐3, and α‐tubulin antibodies. Subsequently, band intensity was determined (c, d). Graph is shown as mean ± SD ( n = 3 or 4). Different letters indicate statistically significant differences ( p < 0.05, ANOVA, Tukey–Kramer's test). Asterisk indicates statistically significant differences ( p < 0.05, Student's t ‐test). N.D, not detected.

    Article Snippet: Western blotting was performed using polyclonal rabbit anti‐caspase‐12 (1/1000, 3282–100, Biovision, Waltham, MA, USA; RRID:AB_2243910), polyclonal rabbit anti‐caspase‐9 (1/3000, #9502, Cell Signaling Technology; RRID:AB_2068621), polyclonal rabbit anti‐cleaved caspase‐3 (Asp175) and polyclonal rabbit anti‐caspase‐3 antibodies (1/3000 for both #9661 and #9662, Cell Signaling Technology, Danvers, MA, USA; RRID:AB_2341188 and RRID:AB_331439), monoclonal mouse anti‐Cox IV antibody (1/5000, 4D11‐B3‐E8, Cell Signaling Technology; RRID:AB_2797784), polyclonal rabbit anti‐triosephosphate isomerase antibody (Yamaji et al., ), monoclonal mouse anti‐cytochrome c (1/1000, 7H8, Santa Cruz Biotechnology, Santa Cruz, CA, USA; RRID:AB_627383), monoclonal mouse anti‐α‐tubulin (1/5000, DM1A, Santa Cruz Biotechnology; RRID:AB_628412), and monoclonal mouse anti‐FLAG antibody (1/5000, M2, Sigma‐Aldrich; RRID:AB_259529).

    Techniques: Incubation, Western Blot

    Lig improves DOX-induced cardiac toxicity in mice by activating AMPK/SIRT1 signaling and alleviating pyroptosis mediated by caspase-3/GSDME. A Representative western blotting images and statistical results of p-AMPK, AMPK and SIRT3 in mice (n = 3). B Effects of Lig on heart levels of ATP in mice caused by DOX (n = 5). C , D The serum levels of IL-1β and IL-18 of mice measured by ELISA. E The expression of GSDME-N, cleaved-caspase-3, caspase-3, IL-1β and IL-6 (n = 3). Data are presented as the mean ± SD. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01, ### p < 0.001 compared with model group

    Journal: Chinese Medicine

    Article Title: Liguzinediol potentiates the metabolic remodeling by activating the AMPK/SIRT3 pathway and represses Caspase-3/GSDME-mediated pyroptosis to ameliorate cardiotoxicity

    doi: 10.1186/s13020-024-00955-5

    Figure Lengend Snippet: Lig improves DOX-induced cardiac toxicity in mice by activating AMPK/SIRT1 signaling and alleviating pyroptosis mediated by caspase-3/GSDME. A Representative western blotting images and statistical results of p-AMPK, AMPK and SIRT3 in mice (n = 3). B Effects of Lig on heart levels of ATP in mice caused by DOX (n = 5). C , D The serum levels of IL-1β and IL-18 of mice measured by ELISA. E The expression of GSDME-N, cleaved-caspase-3, caspase-3, IL-1β and IL-6 (n = 3). Data are presented as the mean ± SD. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01, ### p < 0.001 compared with model group

    Article Snippet: Antibodies utilized in this study include anti-phospho-AMPK (p-AMPK, Thr172, #2535) and anti-cleaved-caspase-3 (#9664) from Cell Signaling Technology in Beverly, USA; anti-caspase-3 (BS1518), anti-β-actin (BS6007M), anti-IL-1β (BS3506) from Bioworld in Minnesota, USA; anti-AMPK (YT0215) from Immunoway in Beijing, China; and anti-Bcl-2 (68103-1-lg), anti-Bax (60267-1-lg), anti-IL-6 (23457-1-AP), anti-SIRT3 (10099-1-AP) from Proteintech in Wuhan, China.

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

    Lig treatment inhibits the caspase-3/GSDME signaling pathway in DOX-treated H9C2 cells. A Representative images of PI staining (n = 6). Scale bar represents 50 µm. B Effects of Lig on intracellular LDH level in H9C2 cells treated by DOX (n = 3). C Representative scanning electron microscopy (SEM) images showed the morphological changes of cultured H9C2 under different treatments (n = 3). D H9C2 cells stained with PI were detected by flow cytometry (n = 3). E The protein expression of GSDME-N, cleaved-caspase-3, caspase-3, IL-6, IL-1β in H9C2 cells (n = 3). Data are presented as the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01 compared with model group

    Journal: Chinese Medicine

    Article Title: Liguzinediol potentiates the metabolic remodeling by activating the AMPK/SIRT3 pathway and represses Caspase-3/GSDME-mediated pyroptosis to ameliorate cardiotoxicity

    doi: 10.1186/s13020-024-00955-5

    Figure Lengend Snippet: Lig treatment inhibits the caspase-3/GSDME signaling pathway in DOX-treated H9C2 cells. A Representative images of PI staining (n = 6). Scale bar represents 50 µm. B Effects of Lig on intracellular LDH level in H9C2 cells treated by DOX (n = 3). C Representative scanning electron microscopy (SEM) images showed the morphological changes of cultured H9C2 under different treatments (n = 3). D H9C2 cells stained with PI were detected by flow cytometry (n = 3). E The protein expression of GSDME-N, cleaved-caspase-3, caspase-3, IL-6, IL-1β in H9C2 cells (n = 3). Data are presented as the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01 compared with model group

    Article Snippet: Antibodies utilized in this study include anti-phospho-AMPK (p-AMPK, Thr172, #2535) and anti-cleaved-caspase-3 (#9664) from Cell Signaling Technology in Beverly, USA; anti-caspase-3 (BS1518), anti-β-actin (BS6007M), anti-IL-1β (BS3506) from Bioworld in Minnesota, USA; anti-AMPK (YT0215) from Immunoway in Beijing, China; and anti-Bcl-2 (68103-1-lg), anti-Bax (60267-1-lg), anti-IL-6 (23457-1-AP), anti-SIRT3 (10099-1-AP) from Proteintech in Wuhan, China.

    Techniques: Staining, Electron Microscopy, Cell Culture, Flow Cytometry, Expressing

    Activation of AMPK/SIRT3 signaling is required for Lig to reduce the mitochondrial respiration and pyroptosis in cardiomyocytes. A Morphology in H9C2 cells. Scale bar represents 100 µm (n = 6). B Intracellular ROS level in H9C2 cells (n = 4). Scale bar represents 50 µm. C MMP level was measured by JC-1 assay kit. Scale bar represents 25 µm (n = 6). D Effects of Lig and CC on intracellular ATP level in H9C2 cells (n = 3). E Representative images of Hochest and PI staining (n = 6). Scale bar represents 50 µm. F The expression of SIRT3, Bax and Bcl-2 in H9C2 cells treated by DOX (n = 3). G H9C2 cells stained with PI were detected by flow cytometry (n = 3). H The protein level of GSDME-N, cleaved-caspase-3, caspase-3, IL-6, IL-1β in H9C2 cells. (n = 3) I Intracellular LDH level in H9C2 cells treated by DOX (n = 3). Data are presented as the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01 compared with model group. ns indicates no significance

    Journal: Chinese Medicine

    Article Title: Liguzinediol potentiates the metabolic remodeling by activating the AMPK/SIRT3 pathway and represses Caspase-3/GSDME-mediated pyroptosis to ameliorate cardiotoxicity

    doi: 10.1186/s13020-024-00955-5

    Figure Lengend Snippet: Activation of AMPK/SIRT3 signaling is required for Lig to reduce the mitochondrial respiration and pyroptosis in cardiomyocytes. A Morphology in H9C2 cells. Scale bar represents 100 µm (n = 6). B Intracellular ROS level in H9C2 cells (n = 4). Scale bar represents 50 µm. C MMP level was measured by JC-1 assay kit. Scale bar represents 25 µm (n = 6). D Effects of Lig and CC on intracellular ATP level in H9C2 cells (n = 3). E Representative images of Hochest and PI staining (n = 6). Scale bar represents 50 µm. F The expression of SIRT3, Bax and Bcl-2 in H9C2 cells treated by DOX (n = 3). G H9C2 cells stained with PI were detected by flow cytometry (n = 3). H The protein level of GSDME-N, cleaved-caspase-3, caspase-3, IL-6, IL-1β in H9C2 cells. (n = 3) I Intracellular LDH level in H9C2 cells treated by DOX (n = 3). Data are presented as the mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared with control group; # p < 0.05, ## p < 0.01 compared with model group. ns indicates no significance

    Article Snippet: Antibodies utilized in this study include anti-phospho-AMPK (p-AMPK, Thr172, #2535) and anti-cleaved-caspase-3 (#9664) from Cell Signaling Technology in Beverly, USA; anti-caspase-3 (BS1518), anti-β-actin (BS6007M), anti-IL-1β (BS3506) from Bioworld in Minnesota, USA; anti-AMPK (YT0215) from Immunoway in Beijing, China; and anti-Bcl-2 (68103-1-lg), anti-Bax (60267-1-lg), anti-IL-6 (23457-1-AP), anti-SIRT3 (10099-1-AP) from Proteintech in Wuhan, China.

    Techniques: Activation Assay, Staining, Expressing, Flow Cytometry

    Graphical abstract of how Lig ameliorates DOX-induced cardiotoxicity and potentiates the metabolic remodeling by activating the AMPK/SIRT3 pathway and represses Caspase-3/GSDME-mediated pyroptosis

    Journal: Chinese Medicine

    Article Title: Liguzinediol potentiates the metabolic remodeling by activating the AMPK/SIRT3 pathway and represses Caspase-3/GSDME-mediated pyroptosis to ameliorate cardiotoxicity

    doi: 10.1186/s13020-024-00955-5

    Figure Lengend Snippet: Graphical abstract of how Lig ameliorates DOX-induced cardiotoxicity and potentiates the metabolic remodeling by activating the AMPK/SIRT3 pathway and represses Caspase-3/GSDME-mediated pyroptosis

    Article Snippet: Antibodies utilized in this study include anti-phospho-AMPK (p-AMPK, Thr172, #2535) and anti-cleaved-caspase-3 (#9664) from Cell Signaling Technology in Beverly, USA; anti-caspase-3 (BS1518), anti-β-actin (BS6007M), anti-IL-1β (BS3506) from Bioworld in Minnesota, USA; anti-AMPK (YT0215) from Immunoway in Beijing, China; and anti-Bcl-2 (68103-1-lg), anti-Bax (60267-1-lg), anti-IL-6 (23457-1-AP), anti-SIRT3 (10099-1-AP) from Proteintech in Wuhan, China.

    Techniques: