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  • 85
    Enzo Biochem beta β mhc
    Characterization of hiPSCs and hiPSC-derived CMs. (A) Immunofluorescent staining of hiPSC colonies with antibodies against Oct-4, SSEA-4, TRA-1-60 and TRA-1-81. (B) The hiPSC-CMs differentia4ed from above hiPSC line. (Ba) The phase-contrast light micrograph images of a V-CM cluster. (Bb and Bc) Immunofluorescent staining hiPSC-CMs with antibodies against alpha-actinin and <t>beta-MHC,</t> respectively. Nuclei were stained with DAPI. (C) Action potential traces of ventricular-, atrial- and nodal-like CMs derived from hiPSCs. (D) Response of a ventricular-like hiPSC-CM to ISO recorded with patch-clamp. Abbreviations: ISO, isoproterenol.
    Beta β Mhc, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Santa Cruz Biotechnology ß myosin heavy chain β mhc
    Characterization of hiPSCs and hiPSC-derived CMs. (A) Immunofluorescent staining of hiPSC colonies with antibodies against Oct-4, SSEA-4, TRA-1-60 and TRA-1-81. (B) The hiPSC-CMs differentia4ed from above hiPSC line. (Ba) The phase-contrast light micrograph images of a V-CM cluster. (Bb and Bc) Immunofluorescent staining hiPSC-CMs with antibodies against alpha-actinin and <t>beta-MHC,</t> respectively. Nuclei were stained with DAPI. (C) Action potential traces of ventricular-, atrial- and nodal-like CMs derived from hiPSCs. (D) Response of a ventricular-like hiPSC-CM to ISO recorded with patch-clamp. Abbreviations: ISO, isoproterenol.
    ß Myosin Heavy Chain β Mhc, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore β mhc
    Effect of VEGF-C on hypertrophic markers in cardiomyocytes. VEGF-C treatment significantly increased ANP and BNP mRNAs (panel A), as well as ANP and <t>β-MHC</t> protein levels (panel B) compared to untreated cells.
    β Mhc, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Abcam β mhc
    L-type calcium channel activity is required for mechanical stretch-induced cardiomyocyte hypertrophy. A–B, [ 3 H]Leucine incorporation in cardiomyocytes stimulated with PE or HS in presence of verapamil or nifedipine, or Gd 3+ . C, Ratios of <t>β-MHC/18S</t>
    β Mhc, supplied by Abcam, used in various techniques. Bioz Stars score: 91/100, based on 81 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology β mhc
    Inhibition of β-catenin signaling ameliorates Ang II-induced cardiac hypertrophy. ( A ) Representative micrographs showed immunohistochemical staining for cardiac <t>β-MHC</t> and α-actin proteins in various groups as indicated. Arrows indicate positive staining. Scale bar, 50 µm (top panel) and 20 µm (bottom panel). ( B – D ) Western blot analysis of β-MHC and α-actin in the heart after various treatments as indicated. Representative Western blots ( B ) and quantitative data for β-MHC ( C ) and α-actin ( D ) are presented. * P
    β Mhc, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 149 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cell Signaling Technology Inc β mhc
    Autophagy inhibition by CQ counteracts the protective effect of CRA on cardiomyocyte hypertrophy ( A ) Representative blots and quantitative results for LC3 and <t>β-MHC</t> protein expression in H9c2 cells in each group ( n = 4 per group). ( B ) ANP and β-MHC mRNA expression in H9c2 cells in each group. ( C ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( D ) Quantification of cell surface area ( n = 50 + cells per group); * P
    β Mhc, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher β mhc
    Autophagy inhibition by CQ counteracts the protective effect of CRA on cardiomyocyte hypertrophy ( A ) Representative blots and quantitative results for LC3 and <t>β-MHC</t> protein expression in H9c2 cells in each group ( n = 4 per group). ( B ) ANP and β-MHC mRNA expression in H9c2 cells in each group. ( C ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( D ) Quantification of cell surface area ( n = 50 + cells per group); * P
    β Mhc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 220 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Developmental Studies Hybridoma Bank β mhc
    Autophagy inhibition by CQ counteracts the protective effect of CRA on cardiomyocyte hypertrophy ( A ) Representative blots and quantitative results for LC3 and <t>β-MHC</t> protein expression in H9c2 cells in each group ( n = 4 per group). ( B ) ANP and β-MHC mRNA expression in H9c2 cells in each group. ( C ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( D ) Quantification of cell surface area ( n = 50 + cells per group); * P
    β Mhc, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Abcam beta myosin heavy chain β mhc
    Effects of AA and the JNK inhibitor SP600125 on the expression of cardiac hypertrophy-related genes in PE-induced hypertrophic cardiomyocytes (A) Chromatin immunoprecipitation (ChIP)-PCR results demonstrating the binding of P300 and PCAF to the MEF2A promoter. (-) negative control, amplification of DNA fragments after precipitation with normal mouse IgG; (+) positive control, amplification of DNA fragments after precipitation with anti-RNA polymerase II antibody. ( B) qRT-PCR results showing that the mRNA expression of MEF2A was higher in PE-induced hypertrophic cardiomyocytes than in control cardiomyocytes, whereas histone acetyltransferase (HAT) and JNK inhibition with AA and SP600125, respectively, prevented MEF2A overexpression in these cells. ( C) ChIP-PCR demonstrated that MEF2A could bind the promoters of atrial natriuretic peptide ( ANP ), brain natriuretic peptide ( BNP ), and <t>beta-myosin</t> heavy chain ( β-MHC ). Input: positive control, IgG: negative control. ( D, E, and F) Western blotting showing that expression of the cardiac hypertrophy-related proteins ANP, BNP, and β-MHC was higher in the PE group than in the control group, whereas the HAT inhibitor AA or the JNK inhibitor SP600125 counteracted this effect. * P
    Beta Myosin Heavy Chain β Mhc, supplied by Abcam, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Abcam myosin heavy chain β mhc β
    Effects of AA and the JNK inhibitor SP600125 on the expression of cardiac hypertrophy-related genes in PE-induced hypertrophic cardiomyocytes (A) Chromatin immunoprecipitation (ChIP)-PCR results demonstrating the binding of P300 and PCAF to the MEF2A promoter. (-) negative control, amplification of DNA fragments after precipitation with normal mouse IgG; (+) positive control, amplification of DNA fragments after precipitation with anti-RNA polymerase II antibody. ( B) qRT-PCR results showing that the mRNA expression of MEF2A was higher in PE-induced hypertrophic cardiomyocytes than in control cardiomyocytes, whereas histone acetyltransferase (HAT) and JNK inhibition with AA and SP600125, respectively, prevented MEF2A overexpression in these cells. ( C) ChIP-PCR demonstrated that MEF2A could bind the promoters of atrial natriuretic peptide ( ANP ), brain natriuretic peptide ( BNP ), and <t>beta-myosin</t> heavy chain ( β-MHC ). Input: positive control, IgG: negative control. ( D, E, and F) Western blotting showing that expression of the cardiac hypertrophy-related proteins ANP, BNP, and β-MHC was higher in the PE group than in the control group, whereas the HAT inhibitor AA or the JNK inhibitor SP600125 counteracted this effect. * P
    Myosin Heavy Chain β Mhc β, supplied by Abcam, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher mhc β m01319005 g1
    Effects of AA and the JNK inhibitor SP600125 on the expression of cardiac hypertrophy-related genes in PE-induced hypertrophic cardiomyocytes (A) Chromatin immunoprecipitation (ChIP)-PCR results demonstrating the binding of P300 and PCAF to the MEF2A promoter. (-) negative control, amplification of DNA fragments after precipitation with normal mouse IgG; (+) positive control, amplification of DNA fragments after precipitation with anti-RNA polymerase II antibody. ( B) qRT-PCR results showing that the mRNA expression of MEF2A was higher in PE-induced hypertrophic cardiomyocytes than in control cardiomyocytes, whereas histone acetyltransferase (HAT) and JNK inhibition with AA and SP600125, respectively, prevented MEF2A overexpression in these cells. ( C) ChIP-PCR demonstrated that MEF2A could bind the promoters of atrial natriuretic peptide ( ANP ), brain natriuretic peptide ( BNP ), and <t>beta-myosin</t> heavy chain ( β-MHC ). Input: positive control, IgG: negative control. ( D, E, and F) Western blotting showing that expression of the cardiac hypertrophy-related proteins ANP, BNP, and β-MHC was higher in the PE group than in the control group, whereas the HAT inhibitor AA or the JNK inhibitor SP600125 counteracted this effect. * P
    Mhc β M01319005 G1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore anti β mhc
    Analysis of sarcomeric organization in untreated (control) and GFP-FAT–infected cardiac myocytes at 24, 48, and 72 h postinfection. Paraformaldehyde-fixed, acetone-permeabilized cells were stained with antibodies against α-actinin, <t>β-MHC</t> or tensin.
    Anti β Mhc, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 50 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Sangon Biotech β mhc
    Resistin increases BNP and <t>β-MHC</t> mRNA expression that are reduced by metformin. (A) BNP mRNA and (B) β-MHC mRNA levels were examined by reverse transcription quantitative PCR. Data represent the mean ± SD. *P
    β Mhc, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 90/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Bioss β mhc
    Graphs of interested protein with ventricular proteins set as the control state. (A) SERCA2a protein synthesis, (B) <t>α-MHC</t> protein synthesis, (C) <t>β-MHC</t> protein synthesis, (D) TnT protein synthesis, and (E) α-actinin protein synthesis. N ≥ 3 and two tailed significance was set at * p
    β Mhc, supplied by Bioss, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Novocastra β myosin heavy chain β mhc
    Morphological changes induced by PE or ET-1 in cardiac myocytes after 4 h. Myocytes were either unstimulated ( Control , A ), or exposed to 40 μM PE ( B ) or 40 nM ET-1 ( C ) for 4 h and immunostained for <t>β-MHC</t> as described in Materials and Methods. Myocytes shown are representative of a typical field within a single experiment. The experiment was repeated on three further occasions with similar results. Bar, 25 μm.
    β Myosin Heavy Chain β Mhc, supplied by Novocastra, used in various techniques. Bioz Stars score: 88/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Merck KGaA β mhc
    Vezf1 is expressed in adult cardiomyocytes and regulates cardiomyocyte growth and cardiomyopathy related genes. (A) qRT-PCR analysis of the expression of endothelial nitric oxide synthase (eNOS), collagen type I alpha 1 chain (Col1a1), and α myosin heavy chain 6 <t>(α-MHC)</t> mRNAs in pools of fractionated resident mouse cardiac cells. eNOS, Col1a1 and α-MHC were used as markers for endothelial cells (Endo), fibroblasts (Fibro), and cardiomyocytes (Myo), respectively. n = 5. (B) qPCR analysis of Vezf1 mRNA levels in cardiomyocytes and fibroblasts relative to that in the endothelial cells. n = 5. (C) Adult rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or Control siRNA (100 nM) and 3 days later RNA samples were collected. Shown is qRT-PCR analysis for expression of Vezf1. Results are normalized to expression of 18S (18S ribosomal RNA). n = 6. (D and E) Adult rat ventricular cardiomyocytes were transfected with two distinct Vezf1 siRNAs (100 nM) or Control siRNA (100 nM) and 1 day later cells were stimulated with isoprenaline (Iso, 1 µM) for 48 h where indicated. (D) Shown is microscopy analysis for cardiomyocyte size. Ctrl siRNA n = 8, Vezf1 A siRNA n = 9, Vezf1 B siRNA n = 10; Ctrl siRNA + Iso n = 10, Vezf1 A siRNA + Iso n = 15, Vezf1 B siRNA + Iso n = 13. (E) Shown is microscopy analysis for sarcomere length (µm). Ctrl siRNA n = 14, Vezf1 B siRNA n = 18; Ctrl siRNA + Iso n = 22, Vezf1 B siRNA + Iso n = 25. (F) Adult rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or control siRNA and 3 days later Ca 2+ cycling and cardiomyocyte (CM) shortening were analyzed. Ctrl n = 44, Vezf1 siRNA n = 43. (G) Neonatal rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or control siRNA and 2 days later cells were treated with Iso (1 µM) for 24 h. Shown is qRT-PCR analysis for expression of Vezf1, <t>β-MHC</t> (myosin heavy chain beta-subunit), Ska (skeletal alpha actin), ANP (atrial natriuretic peptide) and β-MHC versus Ska ratio. Results are normalized to expression of 18S (18S ribosomal RNA). n = 4. (H-I) Neonatal rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or control siRNA (100 nM) and 3 days later cells were treated with either vehicle, phenylephrine (PE, 100 µM) or basic fibroblast growth factor (FGF, 20 ng/ml) for 48 h. (H) Shown is immunoblot analysis for β-MHC, ANP, GAPDH, Ska and Vinculin. (I) Shown is β-MHC versus Ska ratio from immunoblot quantification. n = 4. * P
    β Mhc, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 94/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Novocastra β mhc
    Effect of ROCK inhibition on early hypertrophy markers after MI <t>(β-MHC</t> and -SKA) . (a) Upper panel: representative western blot images for β-MHC from left ventricle in rats 1 week post-MI in the 3 experimental groups. Lower panel: comparative densitometric analysis in the 3 groups (sham, n = 5; MI, n = 7 and MI treated with fasudil, n = 4). (b) Upper panel: representative western blot images for α-SKA from left ventricle in rats 1 week post-MI in the 3 experimental groups (upper panel). Lower panel: comparative densitometric analysis in the three groups ( n = 3 per group). Quantifications are shown as relative to the sham group (in folds). All measurements were normalized by GAPDH levels. Data are expressed as mean ± standard error of the mean. # p
    β Mhc, supplied by Novocastra, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Santa Cruz Biotechnology primary β mhc antibody
    Triptolide attenuated cardiac hypertrophy in mice. Cardiac hypertrophy was induced by isoproterenol (Iso, 5 mg/kg, s.c., for 14 days) in mice ( n = 8–10 in each group). (A) Body weight; (B) heart weight (HW) index to tibia length (TL); (C) left ventricular weight (LVW) indexes to TL; (D) α-myosin heavy chain <t>(MHC)</t> mRNA expression level; (E) <t>β-MHC</t> mRNA expression level; (F) atrial natriuretic peptide (ANP) mRNA expression level. These mRNA expression levels were measured with Real-time PCR method and normalized to β-actin and control group, respectively. The data are presented as mean ± SEM, ∗∗ p
    Primary β Mhc Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Abcam anti β mhc
    Triptolide attenuated cardiac hypertrophy in mice. Cardiac hypertrophy was induced by isoproterenol (Iso, 5 mg/kg, s.c., for 14 days) in mice ( n = 8–10 in each group). (A) Body weight; (B) heart weight (HW) index to tibia length (TL); (C) left ventricular weight (LVW) indexes to TL; (D) α-myosin heavy chain <t>(MHC)</t> mRNA expression level; (E) <t>β-MHC</t> mRNA expression level; (F) atrial natriuretic peptide (ANP) mRNA expression level. These mRNA expression levels were measured with Real-time PCR method and normalized to β-actin and control group, respectively. The data are presented as mean ± SEM, ∗∗ p
    Anti β Mhc, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Cell Signaling Technology Inc anti β mhc antibody
    Ang II increases while Neb and Rap suppress the Ang II-induced increase in miR-208a effector <t>β-MHC</t> (A) Representative autoradiogram and densitometric analysis using Quantity One software (graph) after Western blotting of untreated and treated HL-1 cell lysates (treated with Ang II or Ang II+Neb) and probing with anti- β-MHC antibody. (B) Representative images from immunofluorescence analysis of untreated and treated HL-1 cells. (C) Representative autoradiogram and densitometric analysis using Quantity One software (graph) after Western blotting of HL-1 cell lysates (Untreated (Con) or treated with Ang II or Ang II+Neb) and probing with anti- β-MHC antibody. Treatments with Ang II (100nM:12hrs) Neb (1µM:12 hrs)) or Rap (10nM: 12hrs) were similar to those performed for the data shown in Fig. 1 . Treatments were performed in triplicate. Neb- and Rap-treatment suppressed Ang II-induced increase in β-MHC (A, C). Immunofluorescence staining with anti- β-MHC antibody and nuclear stain DAPI indicated that in individual cells Ang II increased and Neb suppressed β-MHC (B). *p
    Anti β Mhc Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Characterization of hiPSCs and hiPSC-derived CMs. (A) Immunofluorescent staining of hiPSC colonies with antibodies against Oct-4, SSEA-4, TRA-1-60 and TRA-1-81. (B) The hiPSC-CMs differentia4ed from above hiPSC line. (Ba) The phase-contrast light micrograph images of a V-CM cluster. (Bb and Bc) Immunofluorescent staining hiPSC-CMs with antibodies against alpha-actinin and beta-MHC, respectively. Nuclei were stained with DAPI. (C) Action potential traces of ventricular-, atrial- and nodal-like CMs derived from hiPSCs. (D) Response of a ventricular-like hiPSC-CM to ISO recorded with patch-clamp. Abbreviations: ISO, isoproterenol.

    Journal: PLoS ONE

    Article Title: Identification and Characterization of Calcium Sparks in Cardiomyocytes Derived from Human Induced Pluripotent Stem Cells

    doi: 10.1371/journal.pone.0055266

    Figure Lengend Snippet: Characterization of hiPSCs and hiPSC-derived CMs. (A) Immunofluorescent staining of hiPSC colonies with antibodies against Oct-4, SSEA-4, TRA-1-60 and TRA-1-81. (B) The hiPSC-CMs differentia4ed from above hiPSC line. (Ba) The phase-contrast light micrograph images of a V-CM cluster. (Bb and Bc) Immunofluorescent staining hiPSC-CMs with antibodies against alpha-actinin and beta-MHC, respectively. Nuclei were stained with DAPI. (C) Action potential traces of ventricular-, atrial- and nodal-like CMs derived from hiPSCs. (D) Response of a ventricular-like hiPSC-CM to ISO recorded with patch-clamp. Abbreviations: ISO, isoproterenol.

    Article Snippet: After blocking with 5% goat serum in PBS for 1 h at room temperature, cells stained with mouse anti-human cardiac sarcomeric alpha-actinin (α-actinin) (clone EA-35, Sigma) and mouse anti-human cardiac myosin heave chain, beta (β-MHC) (Alexis Biochemicals, FL, USA).

    Techniques: Derivative Assay, Staining, Patch Clamp

    Generation and characterization of cardiomyocytes differentiated from H9 hESCs. A: Light microscopy and immunocytochemistry image of H9 hESC-CMs dissociated from contracting EBs. Scale bar: 100 µm. Fluorescent images of H9 hESC-CMs stained with antibodies against α-actinin, β-MHC and Titin showed typical cardiac sarcomeres. Scale bar: 30 µm. B1∼2: Action potential trace of three subtypes of cardiomyocytes derived from H9 hESCs and corresponding specific action potential properties. APA: action potential amplitude. dV/dt max : maximal rate of depolarization or maximal upstroke velocity. APD50: action potential duration at 50%. APD90: action potential duration at 90%.

    Journal: PLoS ONE

    Article Title: Hydrogen Sulfide Suppresses Outward Rectifier Potassium Currents in Human Pluripotent Stem Cell-Derived Cardiomyocytes

    doi: 10.1371/journal.pone.0050641

    Figure Lengend Snippet: Generation and characterization of cardiomyocytes differentiated from H9 hESCs. A: Light microscopy and immunocytochemistry image of H9 hESC-CMs dissociated from contracting EBs. Scale bar: 100 µm. Fluorescent images of H9 hESC-CMs stained with antibodies against α-actinin, β-MHC and Titin showed typical cardiac sarcomeres. Scale bar: 30 µm. B1∼2: Action potential trace of three subtypes of cardiomyocytes derived from H9 hESCs and corresponding specific action potential properties. APA: action potential amplitude. dV/dt max : maximal rate of depolarization or maximal upstroke velocity. APD50: action potential duration at 50%. APD90: action potential duration at 90%.

    Article Snippet: Sigma), β-myosin heavy chain or β-MHC (Alexis Biochemicals, FL, USA) followed by Alexa Fluo® 488 goat anti-rabbit IgG (Invitrogen, CA, USA); and cardiac Titin (1∶10) (Sigma-Alrich, MO, USA) followed by Alexa Fluo® 555 donkey anti-rabbit IgG.

    Techniques: Light Microscopy, Immunocytochemistry, Staining, Derivative Assay

    Effect of VEGF-C on hypertrophic markers in cardiomyocytes. VEGF-C treatment significantly increased ANP and BNP mRNAs (panel A), as well as ANP and β-MHC protein levels (panel B) compared to untreated cells.

    Journal: American Journal of Translational Research

    Article Title: VEGF-C/VEGFR-3 pathway promotes myocyte hypertrophy and survival in the infarcted myocardium

    doi:

    Figure Lengend Snippet: Effect of VEGF-C on hypertrophic markers in cardiomyocytes. VEGF-C treatment significantly increased ANP and BNP mRNAs (panel A), as well as ANP and β-MHC protein levels (panel B) compared to untreated cells.

    Article Snippet: Membranes were blocked for nonspecific protein with 5% nonfat dry milk in TBS and then probed overnight at 4°C with primary antibodies against cleaved caspase 3, 8, 9 (Cell Signaling, Danvers, MA), Bax (R & D, Minneapolis, MN), ANP, β-MHC (Millipore, Bellerica, MA) and α-actin (Sigma, St. Louis, MO).

    Techniques: Aqueous Normal-phase Chromatography

    L-type calcium channel activity is required for mechanical stretch-induced cardiomyocyte hypertrophy. A–B, [ 3 H]Leucine incorporation in cardiomyocytes stimulated with PE or HS in presence of verapamil or nifedipine, or Gd 3+ . C, Ratios of β-MHC/18S

    Journal: Circulation

    Article Title: Polycystin-1 is a Cardiomyocyte Mechanosensor That Governs L-type Ca2+ Channel Protein Stability

    doi: 10.1161/CIRCULATIONAHA.114.013537

    Figure Lengend Snippet: L-type calcium channel activity is required for mechanical stretch-induced cardiomyocyte hypertrophy. A–B, [ 3 H]Leucine incorporation in cardiomyocytes stimulated with PE or HS in presence of verapamil or nifedipine, or Gd 3+ . C, Ratios of β-MHC/18S

    Article Snippet: Other antibodies employed include RCAN (Sigma), β-MHC and PC-1 (Abcam), and ERK (Cell Signaling).

    Techniques: Activity Assay

    PC-1 mediates in vitro cardiomyocyte hypertrophy. A, [ 3 H]Leucine incorporation in cardiomyocytes stimulated with PE or HS and exposed to PC-1 siRNA (siPC-1) or transfected with unrelated sequences. B, Representative Western blot of β-MHC (left)

    Journal: Circulation

    Article Title: Polycystin-1 is a Cardiomyocyte Mechanosensor That Governs L-type Ca2+ Channel Protein Stability

    doi: 10.1161/CIRCULATIONAHA.114.013537

    Figure Lengend Snippet: PC-1 mediates in vitro cardiomyocyte hypertrophy. A, [ 3 H]Leucine incorporation in cardiomyocytes stimulated with PE or HS and exposed to PC-1 siRNA (siPC-1) or transfected with unrelated sequences. B, Representative Western blot of β-MHC (left)

    Article Snippet: Other antibodies employed include RCAN (Sigma), β-MHC and PC-1 (Abcam), and ERK (Cell Signaling).

    Techniques: In Vitro, Transfection, Western Blot

    Inhibition of β-catenin signaling ameliorates Ang II-induced cardiac hypertrophy. ( A ) Representative micrographs showed immunohistochemical staining for cardiac β-MHC and α-actin proteins in various groups as indicated. Arrows indicate positive staining. Scale bar, 50 µm (top panel) and 20 µm (bottom panel). ( B – D ) Western blot analysis of β-MHC and α-actin in the heart after various treatments as indicated. Representative Western blots ( B ) and quantitative data for β-MHC ( C ) and α-actin ( D ) are presented. * P

    Journal: Scientific Reports

    Article Title: An essential role for Wnt/β-catenin signaling in mediating hypertensive heart disease

    doi: 10.1038/s41598-018-27064-2

    Figure Lengend Snippet: Inhibition of β-catenin signaling ameliorates Ang II-induced cardiac hypertrophy. ( A ) Representative micrographs showed immunohistochemical staining for cardiac β-MHC and α-actin proteins in various groups as indicated. Arrows indicate positive staining. Scale bar, 50 µm (top panel) and 20 µm (bottom panel). ( B – D ) Western blot analysis of β-MHC and α-actin in the heart after various treatments as indicated. Representative Western blots ( B ) and quantitative data for β-MHC ( C ) and α-actin ( D ) are presented. * P

    Article Snippet: The primary antibodies were as follows: rabbit polyclonal anti-β-catenin antibody (ab15180; Abcam), Wnt3a (SAB2108434; Sigma, Darmstadt, Germany), β-MHC (sc-53089; Santa Cruz, CA), α-actin (KM9006; Sungene, Tianjin, China), fibronectin (F3648; Sigma, Darmstadt, Germany).

    Techniques: Inhibition, Immunohistochemistry, Staining, Western Blot

    Chronic Ang II infusion induces cardiac hypertrophy and activates Wnt/β-catenin signaling. ( A ) Histological staining (H.E.) revealed overt cardiac hypertrophy in SD rats after 4 weeks of Ang II infusion. Scale bar, 50 µm. ( B ) Western blot analysis showed an increased expression of hypertrophic markers such as β-MHC and α-actin in the heart after Ang II infusion. Whole cardiac lysates were immunoblotted with antibodies against β-MHC, α-actin and α-tubulin, respectively. ( C and D ) Quantitative data on β-MHC and α-actin levels in different groups as indicated. * P

    Journal: Scientific Reports

    Article Title: An essential role for Wnt/β-catenin signaling in mediating hypertensive heart disease

    doi: 10.1038/s41598-018-27064-2

    Figure Lengend Snippet: Chronic Ang II infusion induces cardiac hypertrophy and activates Wnt/β-catenin signaling. ( A ) Histological staining (H.E.) revealed overt cardiac hypertrophy in SD rats after 4 weeks of Ang II infusion. Scale bar, 50 µm. ( B ) Western blot analysis showed an increased expression of hypertrophic markers such as β-MHC and α-actin in the heart after Ang II infusion. Whole cardiac lysates were immunoblotted with antibodies against β-MHC, α-actin and α-tubulin, respectively. ( C and D ) Quantitative data on β-MHC and α-actin levels in different groups as indicated. * P

    Article Snippet: The primary antibodies were as follows: rabbit polyclonal anti-β-catenin antibody (ab15180; Abcam), Wnt3a (SAB2108434; Sigma, Darmstadt, Germany), β-MHC (sc-53089; Santa Cruz, CA), α-actin (KM9006; Sungene, Tianjin, China), fibronectin (F3648; Sigma, Darmstadt, Germany).

    Techniques: Staining, Western Blot, Expressing

    Autophagy inhibition by CQ counteracts the protective effect of CRA on cardiomyocyte hypertrophy ( A ) Representative blots and quantitative results for LC3 and β-MHC protein expression in H9c2 cells in each group ( n = 4 per group). ( B ) ANP and β-MHC mRNA expression in H9c2 cells in each group. ( C ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( D ) Quantification of cell surface area ( n = 50 + cells per group); * P

    Journal: Bioscience Reports

    Article Title: Corosolic acid ameliorates cardiac hypertrophy via regulating autophagy

    doi: 10.1042/BSR20191860

    Figure Lengend Snippet: Autophagy inhibition by CQ counteracts the protective effect of CRA on cardiomyocyte hypertrophy ( A ) Representative blots and quantitative results for LC3 and β-MHC protein expression in H9c2 cells in each group ( n = 4 per group). ( B ) ANP and β-MHC mRNA expression in H9c2 cells in each group. ( C ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( D ) Quantification of cell surface area ( n = 50 + cells per group); * P

    Article Snippet: Protein expression levels of AMP-activated protein kinase (AMPK), phosphorylated AMPK (P-AMPK), 4EBP1, P-4EBP1, LC3, and β-MHC (Cell Signaling Technology) were normalized to the GAPDH (Santa Cruz).

    Techniques: Inhibition, Expressing, Aqueous Normal-phase Chromatography, Imaging, Immunostaining

    AMPK knockdown with AMPKα2 siRNA counteracted LC3 II expression increase and the hypertrophic response inhibition caused by CRA in PE-treated H9c2 cells ( A ) Representative blots and quantitative results for LC3 protein expression in H9c2 cells in each group ( n = 4 per group). ( B ) ANP and β-MHC mRNA expression in H9c2 cells in each group. ( C ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( D ) Quantification of cell surface area ( n = 50 + cells per group); * P

    Journal: Bioscience Reports

    Article Title: Corosolic acid ameliorates cardiac hypertrophy via regulating autophagy

    doi: 10.1042/BSR20191860

    Figure Lengend Snippet: AMPK knockdown with AMPKα2 siRNA counteracted LC3 II expression increase and the hypertrophic response inhibition caused by CRA in PE-treated H9c2 cells ( A ) Representative blots and quantitative results for LC3 protein expression in H9c2 cells in each group ( n = 4 per group). ( B ) ANP and β-MHC mRNA expression in H9c2 cells in each group. ( C ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( D ) Quantification of cell surface area ( n = 50 + cells per group); * P

    Article Snippet: Protein expression levels of AMP-activated protein kinase (AMPK), phosphorylated AMPK (P-AMPK), 4EBP1, P-4EBP1, LC3, and β-MHC (Cell Signaling Technology) were normalized to the GAPDH (Santa Cruz).

    Techniques: Expressing, Inhibition, Aqueous Normal-phase Chromatography, Imaging, Immunostaining

    CRA blunts cardiomyocyte hypertrophy in PE-treated H9c2 cells ( A ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( B ) Quantification of cell surface area ( n = 50 + cells per group), ANP, and β-MHC mRNA levels in H9c2 cells in each group. * P

    Journal: Bioscience Reports

    Article Title: Corosolic acid ameliorates cardiac hypertrophy via regulating autophagy

    doi: 10.1042/BSR20191860

    Figure Lengend Snippet: CRA blunts cardiomyocyte hypertrophy in PE-treated H9c2 cells ( A ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( B ) Quantification of cell surface area ( n = 50 + cells per group), ANP, and β-MHC mRNA levels in H9c2 cells in each group. * P

    Article Snippet: Protein expression levels of AMP-activated protein kinase (AMPK), phosphorylated AMPK (P-AMPK), 4EBP1, P-4EBP1, LC3, and β-MHC (Cell Signaling Technology) were normalized to the GAPDH (Santa Cruz).

    Techniques: Imaging, Immunostaining, Aqueous Normal-phase Chromatography

    Autophagy inhibition by 3-MA counteracts the protective effect of CRA on cardiomyocyte hypertrophy ( A ) Representative blots and quantitative results for LC3 and β-MHC protein expression in H9c2 cells in each group ( n = 4 per group). ( B ) ANP and β-MHC mRNA expression in H9c2 cells in each group. ( C ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( D ) Quantification of cell surface area ( n = 50 + cells per group); * P

    Journal: Bioscience Reports

    Article Title: Corosolic acid ameliorates cardiac hypertrophy via regulating autophagy

    doi: 10.1042/BSR20191860

    Figure Lengend Snippet: Autophagy inhibition by 3-MA counteracts the protective effect of CRA on cardiomyocyte hypertrophy ( A ) Representative blots and quantitative results for LC3 and β-MHC protein expression in H9c2 cells in each group ( n = 4 per group). ( B ) ANP and β-MHC mRNA expression in H9c2 cells in each group. ( C ) Representative imaging of immunostaining H9c2 cells for α-actinin (green) in each group. ( D ) Quantification of cell surface area ( n = 50 + cells per group); * P

    Article Snippet: Protein expression levels of AMP-activated protein kinase (AMPK), phosphorylated AMPK (P-AMPK), 4EBP1, P-4EBP1, LC3, and β-MHC (Cell Signaling Technology) were normalized to the GAPDH (Santa Cruz).

    Techniques: Inhibition, Expressing, Aqueous Normal-phase Chromatography, Imaging, Immunostaining

    CRA ameliorates pressure overload-induced cardiac hypertrophy ( A ) Representative gross heart, HE-stained heart sections of mice in the indicated groups ( n = 5–8 mice per experimental group). ( B ) Quantification of CSA in each group ( n = 100–200 cells per experimental group), and HW/BW, HW/TL, LW/BW ratios of mice in each group ( n = 11–17 mice per experimental group). ( C ) Levels of cardiac hypertrophy-related transcripts (ANP, BNP, β-MHC, α-MHC) quantified by RT-PCR ( n = 6 mice per experimental group). ( D ) PSR staining for detecting fibrosis ( n = 5–7 mice per group). ( E ) mRNA expression levels of CTGF, Collagen Iα, IL-6 and Fibronectin in each group ( n = 6 per group). Data are presented as mean ± SEM. * P

    Journal: Bioscience Reports

    Article Title: Corosolic acid ameliorates cardiac hypertrophy via regulating autophagy

    doi: 10.1042/BSR20191860

    Figure Lengend Snippet: CRA ameliorates pressure overload-induced cardiac hypertrophy ( A ) Representative gross heart, HE-stained heart sections of mice in the indicated groups ( n = 5–8 mice per experimental group). ( B ) Quantification of CSA in each group ( n = 100–200 cells per experimental group), and HW/BW, HW/TL, LW/BW ratios of mice in each group ( n = 11–17 mice per experimental group). ( C ) Levels of cardiac hypertrophy-related transcripts (ANP, BNP, β-MHC, α-MHC) quantified by RT-PCR ( n = 6 mice per experimental group). ( D ) PSR staining for detecting fibrosis ( n = 5–7 mice per group). ( E ) mRNA expression levels of CTGF, Collagen Iα, IL-6 and Fibronectin in each group ( n = 6 per group). Data are presented as mean ± SEM. * P

    Article Snippet: Protein expression levels of AMP-activated protein kinase (AMPK), phosphorylated AMPK (P-AMPK), 4EBP1, P-4EBP1, LC3, and β-MHC (Cell Signaling Technology) were normalized to the GAPDH (Santa Cruz).

    Techniques: Staining, Mouse Assay, Aqueous Normal-phase Chromatography, Reverse Transcription Polymerase Chain Reaction, Expressing

    Effects of AA and the JNK inhibitor SP600125 on the expression of cardiac hypertrophy-related genes in PE-induced hypertrophic cardiomyocytes (A) Chromatin immunoprecipitation (ChIP)-PCR results demonstrating the binding of P300 and PCAF to the MEF2A promoter. (-) negative control, amplification of DNA fragments after precipitation with normal mouse IgG; (+) positive control, amplification of DNA fragments after precipitation with anti-RNA polymerase II antibody. ( B) qRT-PCR results showing that the mRNA expression of MEF2A was higher in PE-induced hypertrophic cardiomyocytes than in control cardiomyocytes, whereas histone acetyltransferase (HAT) and JNK inhibition with AA and SP600125, respectively, prevented MEF2A overexpression in these cells. ( C) ChIP-PCR demonstrated that MEF2A could bind the promoters of atrial natriuretic peptide ( ANP ), brain natriuretic peptide ( BNP ), and beta-myosin heavy chain ( β-MHC ). Input: positive control, IgG: negative control. ( D, E, and F) Western blotting showing that expression of the cardiac hypertrophy-related proteins ANP, BNP, and β-MHC was higher in the PE group than in the control group, whereas the HAT inhibitor AA or the JNK inhibitor SP600125 counteracted this effect. * P

    Journal: bioRxiv

    Article Title: Anacardic acid protects against phenylephrine-induced mouse cardiac hypertrophy through JNK signaling-dependent regulation of histone acetylation

    doi: 10.1101/2020.02.06.937672

    Figure Lengend Snippet: Effects of AA and the JNK inhibitor SP600125 on the expression of cardiac hypertrophy-related genes in PE-induced hypertrophic cardiomyocytes (A) Chromatin immunoprecipitation (ChIP)-PCR results demonstrating the binding of P300 and PCAF to the MEF2A promoter. (-) negative control, amplification of DNA fragments after precipitation with normal mouse IgG; (+) positive control, amplification of DNA fragments after precipitation with anti-RNA polymerase II antibody. ( B) qRT-PCR results showing that the mRNA expression of MEF2A was higher in PE-induced hypertrophic cardiomyocytes than in control cardiomyocytes, whereas histone acetyltransferase (HAT) and JNK inhibition with AA and SP600125, respectively, prevented MEF2A overexpression in these cells. ( C) ChIP-PCR demonstrated that MEF2A could bind the promoters of atrial natriuretic peptide ( ANP ), brain natriuretic peptide ( BNP ), and beta-myosin heavy chain ( β-MHC ). Input: positive control, IgG: negative control. ( D, E, and F) Western blotting showing that expression of the cardiac hypertrophy-related proteins ANP, BNP, and β-MHC was higher in the PE group than in the control group, whereas the HAT inhibitor AA or the JNK inhibitor SP600125 counteracted this effect. * P

    Article Snippet: After blocking for 1 h with 5% bovine serum albumin, these PVDF blots were probed with rabbit polyclonal antibodies against brain natriuretic peptide (BNP) (Abcam, 1:1000 dilution), atrial natriuretic peptide (ANP) (Abcam,1:5000 dilution), lysine 9-acetylated histone H3 (H3K9ac) (Abcam, 1:5000 dilution), beta-myosin heavy chain (β-MHC) (Abcam, 1:5000 dilution), PCAF (Abcam, 1:500 dilution), and P300 (Abcam, 1:2000 dilution), rabbit polyclonal antibodies against JNK and phospho-JNK (Cell Signaling, 1:1000 dilution), or rabbit polyclonal antibodies against β-actin and histone H3 (Beyotime, 1:5000 dilution).

    Techniques: Expressing, Chromatin Immunoprecipitation, Polymerase Chain Reaction, Binding Assay, Negative Control, Amplification, Positive Control, Quantitative RT-PCR, HAT Assay, Inhibition, Over Expression, Aqueous Normal-phase Chromatography, Western Blot

    Analysis of sarcomeric organization in untreated (control) and GFP-FAT–infected cardiac myocytes at 24, 48, and 72 h postinfection. Paraformaldehyde-fixed, acetone-permeabilized cells were stained with antibodies against α-actinin, β-MHC or tensin.

    Journal: Molecular Biology of the Cell

    Article Title: Focal Adhesion Kinase and p130Cas Mediate Both Sarcomeric Organization and Activation of Genes Associated with Cardiac Myocyte Hypertrophy

    doi:

    Figure Lengend Snippet: Analysis of sarcomeric organization in untreated (control) and GFP-FAT–infected cardiac myocytes at 24, 48, and 72 h postinfection. Paraformaldehyde-fixed, acetone-permeabilized cells were stained with antibodies against α-actinin, β-MHC or tensin.

    Article Snippet: Monoclonal anti-HA (HA.11) antibody was purchased from BAbCo (Richmond, CA), anti-paxillin was purchased from Zymed, anti-tensin was purchased from Transduction Laboratories, anti-sarcomeric α-actinin was purchased from Sigma (St. Louis, MO), anti-phosphotyrosine (4G10) was purchased from UBI (Lake Placid, NY), and anti–β-MHC was purchased from Chemicon International ( Temecula, CA).

    Techniques: Infection, Staining

    Cas is colocalized with FAK and paxillin at Z-lines in cardiac myocytes. (A) Cas is localized at Z-lines in cardiac myocytes. Cells were grown for 24 or 48 h on fibronectin-coated glass coverslips, fixed with ethanol at −20°C for 30 min, and exposed to acetone at room temperature for 1 min. Cells were double stained with monoclonal antibodies against Cas (detected by fluorescein isothiocyanate) and α-actinin or β-MHC (detected by rhodamine). The merged image shows that Cas staining localizes between sarcomeric A-bands in a pattern that overlies the Z-lines of the sarcomere. Arrowheads identify Cas at intercalated disks. (B) Subcellular localization of FAK in cardiac myocytes. Cells were grown on fibronectin-coated glass coverslips and then fixed for 10 min in cold acetone. Left, FAK was stained with rabbit polyclonal JF1 antibody. Asterisks (*) indicate neighboring nonmyocyte cell. Arrows indicate focal adhesions on both fibroblasts and cardiomyocytes. Right, FAK in intercalated disks (arrowheads) was demonstrated with a combination of rabbit and goat polyclonal A-17 and C-20 antibodies (Santa Cruz Biotechnology). (C) Expression of GFP-paxillin in cardiac myocytes. Freshly isolated cells transiently transfected with a GFP-paxillin expression vector were plated on fibronectin-coated glass coverslips for immunofluorescence. At 48 h posttransfection cells were fixed with paraformaldehyde, permeabilized with acetone, and stained with anti–β-MHC antibodies (detected with rhodamine, middle). GFP-paxillin–expressing cells were visualized by fluorescence microscopy (left). The merged image (right) shows that paxillin localizes between sarcomeric A-bands in a pattern corresponding to the Z-lines of the sarcomere.

    Journal: Molecular Biology of the Cell

    Article Title: Focal Adhesion Kinase and p130Cas Mediate Both Sarcomeric Organization and Activation of Genes Associated with Cardiac Myocyte Hypertrophy

    doi:

    Figure Lengend Snippet: Cas is colocalized with FAK and paxillin at Z-lines in cardiac myocytes. (A) Cas is localized at Z-lines in cardiac myocytes. Cells were grown for 24 or 48 h on fibronectin-coated glass coverslips, fixed with ethanol at −20°C for 30 min, and exposed to acetone at room temperature for 1 min. Cells were double stained with monoclonal antibodies against Cas (detected by fluorescein isothiocyanate) and α-actinin or β-MHC (detected by rhodamine). The merged image shows that Cas staining localizes between sarcomeric A-bands in a pattern that overlies the Z-lines of the sarcomere. Arrowheads identify Cas at intercalated disks. (B) Subcellular localization of FAK in cardiac myocytes. Cells were grown on fibronectin-coated glass coverslips and then fixed for 10 min in cold acetone. Left, FAK was stained with rabbit polyclonal JF1 antibody. Asterisks (*) indicate neighboring nonmyocyte cell. Arrows indicate focal adhesions on both fibroblasts and cardiomyocytes. Right, FAK in intercalated disks (arrowheads) was demonstrated with a combination of rabbit and goat polyclonal A-17 and C-20 antibodies (Santa Cruz Biotechnology). (C) Expression of GFP-paxillin in cardiac myocytes. Freshly isolated cells transiently transfected with a GFP-paxillin expression vector were plated on fibronectin-coated glass coverslips for immunofluorescence. At 48 h posttransfection cells were fixed with paraformaldehyde, permeabilized with acetone, and stained with anti–β-MHC antibodies (detected with rhodamine, middle). GFP-paxillin–expressing cells were visualized by fluorescence microscopy (left). The merged image (right) shows that paxillin localizes between sarcomeric A-bands in a pattern corresponding to the Z-lines of the sarcomere.

    Article Snippet: Monoclonal anti-HA (HA.11) antibody was purchased from BAbCo (Richmond, CA), anti-paxillin was purchased from Zymed, anti-tensin was purchased from Transduction Laboratories, anti-sarcomeric α-actinin was purchased from Sigma (St. Louis, MO), anti-phosphotyrosine (4G10) was purchased from UBI (Lake Placid, NY), and anti–β-MHC was purchased from Chemicon International ( Temecula, CA).

    Techniques: Staining, Expressing, Isolation, Transfection, Plasmid Preparation, Immunofluorescence, Fluorescence, Microscopy

    Effects of EPC-MVs on Ang II-induced CM hypertrophy and β-MHC protein expression. (A) Representative immunohistochemistry images of β-MHC expression in H9c2 CMs in each group. H9c2 CMs were labeled with β-MHC antibody (red), and DAPI (blue, for nucleus). Scale bar, 100 µm. (B) Summarized data of surface areas of CMs in each group. (C) Western blot bands and graphs showing the β-MHC expression in H9c2 CMs in different treatment groups. The molecular weights are 223 kDa for β-MHC and 43 kDa for β-actin. * P

    Journal: PLoS ONE

    Article Title: EPC-Derived Microvesicles Protect Cardiomyocytes from Ang II-Induced Hypertrophy and Apoptosis

    doi: 10.1371/journal.pone.0085396

    Figure Lengend Snippet: Effects of EPC-MVs on Ang II-induced CM hypertrophy and β-MHC protein expression. (A) Representative immunohistochemistry images of β-MHC expression in H9c2 CMs in each group. H9c2 CMs were labeled with β-MHC antibody (red), and DAPI (blue, for nucleus). Scale bar, 100 µm. (B) Summarized data of surface areas of CMs in each group. (C) Western blot bands and graphs showing the β-MHC expression in H9c2 CMs in different treatment groups. The molecular weights are 223 kDa for β-MHC and 43 kDa for β-actin. * P

    Article Snippet: Immunohistochemistry of β-myosin Heavy Chain (β-MHC) H9c2 CMs were fixed with 2% paraformaldehyde at RT for 30 min and then permeated with 0.1% TX-100 at RT for 15 min. After being blocked with 1% BSA and 2% donkey serum for 1 h, the cells were incubated with β-MHC antibody (1∶50; Millipore, MA) overnight at 4°C, and followed by incubation with Cy3-conjugated donkey anti-mouse antibody (1∶250; Jackson, PA) at RT in the dark for 1 h. DAPI was used for nuclear stain.

    Techniques: Expressing, Immunohistochemistry, Labeling, Western Blot

    Successfully established cardiac hypertrophy models in vivo and in vitro. The echocardiographic parameters were measured throughout the experiment. (A) Representative M‐mode images of the indicated groups. (B) LVPW s: left ventricular posterior wall depth. (C) LVAW s: left ventricular anterior wall thickness. (D) LVEF : left ventricular ejection fraction. (E) LVFS : left ventricular fractional shortening. (F) Quantitative data of heart‐to‐bodyweight ratio. (G) Histological sections were stained with haematoxylin and eosin ( HE ) to detect cardiomyocyte hypertrophy (×200 and ×400). (H) Cardiomyocyte surface areas were detected (×200) with α‐ SMA antibody (green signal). (I and J) The expressions of BNP protein were measured in vivo and in vitro. (K and L) The expressions of β‐ MHC protein were measured in vivo and in vitro. Data were represented by mean ± SEM (n = 3‐6). * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: MiR‐103 inhibiting cardiac hypertrophy through inactivation of myocardial cell autophagy via targeting TRPV3 channel in rat hearts, et al. MiR‐103 inhibiting cardiac hypertrophy through inactivation of myocardial cell autophagy via targeting TRPV3 channel in rat hearts

    doi: 10.1111/jcmm.14095

    Figure Lengend Snippet: Successfully established cardiac hypertrophy models in vivo and in vitro. The echocardiographic parameters were measured throughout the experiment. (A) Representative M‐mode images of the indicated groups. (B) LVPW s: left ventricular posterior wall depth. (C) LVAW s: left ventricular anterior wall thickness. (D) LVEF : left ventricular ejection fraction. (E) LVFS : left ventricular fractional shortening. (F) Quantitative data of heart‐to‐bodyweight ratio. (G) Histological sections were stained with haematoxylin and eosin ( HE ) to detect cardiomyocyte hypertrophy (×200 and ×400). (H) Cardiomyocyte surface areas were detected (×200) with α‐ SMA antibody (green signal). (I and J) The expressions of BNP protein were measured in vivo and in vitro. (K and L) The expressions of β‐ MHC protein were measured in vivo and in vitro. Data were represented by mean ± SEM (n = 3‐6). * P

    Article Snippet: Then, the membranes were blocked and incubated with the following primary antibodies: anti‐BNP antibody (1:1000, Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti‐β‐MHC antibody (1:2000, Sigma, St Louis, MO, USA), anti‐TRPV3 antibody (1:200, Abcam, Cambridge, MA, USA), anti‐Beclin‐1 antibody (1:500, Abcam), anti‐LC3‐II antibody (1:500, Abcam)and anti‐β‐actin (1:2000, Santa Cruz Biotechnology). β‐actin was used as a loading control.

    Techniques: In Vivo, In Vitro, Staining

    The effect of miR‐103 on cardiac hypertrophy. (A and B) The expressions of miR‐103 in cardiac hypertrophy models in vivo and in vitro were assayed by quantitative real‐time PCR analysis. U6 was used as an internal control. (C) Expression level of miR‐103 in cardiomyocytes transfected with scramble or miR‐103 mimics. (D) Representative photographs of immunofluorescence staining (×200) and statistical histogram of cardiomyocyte area. (E and F) The expressions of BNP and β‐ MHC proteins were measured in cultured cardiomyocytes. (G) Forcing overexpression of miR‐103 repressed relative fluorescence intensity of Ca 2+ signal in cultured cardiomyocytes challenged by Ang II . Data were represented by mean ± SEM (n = 3). * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: MiR‐103 inhibiting cardiac hypertrophy through inactivation of myocardial cell autophagy via targeting TRPV3 channel in rat hearts, et al. MiR‐103 inhibiting cardiac hypertrophy through inactivation of myocardial cell autophagy via targeting TRPV3 channel in rat hearts

    doi: 10.1111/jcmm.14095

    Figure Lengend Snippet: The effect of miR‐103 on cardiac hypertrophy. (A and B) The expressions of miR‐103 in cardiac hypertrophy models in vivo and in vitro were assayed by quantitative real‐time PCR analysis. U6 was used as an internal control. (C) Expression level of miR‐103 in cardiomyocytes transfected with scramble or miR‐103 mimics. (D) Representative photographs of immunofluorescence staining (×200) and statistical histogram of cardiomyocyte area. (E and F) The expressions of BNP and β‐ MHC proteins were measured in cultured cardiomyocytes. (G) Forcing overexpression of miR‐103 repressed relative fluorescence intensity of Ca 2+ signal in cultured cardiomyocytes challenged by Ang II . Data were represented by mean ± SEM (n = 3). * P

    Article Snippet: Then, the membranes were blocked and incubated with the following primary antibodies: anti‐BNP antibody (1:1000, Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti‐β‐MHC antibody (1:2000, Sigma, St Louis, MO, USA), anti‐TRPV3 antibody (1:200, Abcam, Cambridge, MA, USA), anti‐Beclin‐1 antibody (1:500, Abcam), anti‐LC3‐II antibody (1:500, Abcam)and anti‐β‐actin (1:2000, Santa Cruz Biotechnology). β‐actin was used as a loading control.

    Techniques: In Vivo, In Vitro, Real-time Polymerase Chain Reaction, Expressing, Transfection, Immunofluorescence, Staining, Cell Culture, Over Expression, Fluorescence

    TRPV 3 activation promoted cardiac hypertrophy. (A and B) The expressions of TRPV 3 protein were measured in vivo and in vitro. (C and D) Successfully silencing TRPV 3 by transfecting TRPV 3‐si RNA sequence into cultured cardiomyocytes. (E) Silencing TRPV 3 reduced the surface area of cardiomyocytes (×200) treated with Ang II . (F and G) Silencing TRPV 3 suppressed the expressions of BNP and β‐ MHC protein in cardiomyocytes treated with Ang II . (H) Relative fluorescence intensity of Ca 2+ signal was recorded by laser scanning confocal microscope. Data were represented by mean ± SEM . (n = 3) * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: MiR‐103 inhibiting cardiac hypertrophy through inactivation of myocardial cell autophagy via targeting TRPV3 channel in rat hearts, et al. MiR‐103 inhibiting cardiac hypertrophy through inactivation of myocardial cell autophagy via targeting TRPV3 channel in rat hearts

    doi: 10.1111/jcmm.14095

    Figure Lengend Snippet: TRPV 3 activation promoted cardiac hypertrophy. (A and B) The expressions of TRPV 3 protein were measured in vivo and in vitro. (C and D) Successfully silencing TRPV 3 by transfecting TRPV 3‐si RNA sequence into cultured cardiomyocytes. (E) Silencing TRPV 3 reduced the surface area of cardiomyocytes (×200) treated with Ang II . (F and G) Silencing TRPV 3 suppressed the expressions of BNP and β‐ MHC protein in cardiomyocytes treated with Ang II . (H) Relative fluorescence intensity of Ca 2+ signal was recorded by laser scanning confocal microscope. Data were represented by mean ± SEM . (n = 3) * P

    Article Snippet: Then, the membranes were blocked and incubated with the following primary antibodies: anti‐BNP antibody (1:1000, Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti‐β‐MHC antibody (1:2000, Sigma, St Louis, MO, USA), anti‐TRPV3 antibody (1:200, Abcam, Cambridge, MA, USA), anti‐Beclin‐1 antibody (1:500, Abcam), anti‐LC3‐II antibody (1:500, Abcam)and anti‐β‐actin (1:2000, Santa Cruz Biotechnology). β‐actin was used as a loading control.

    Techniques: Activation Assay, In Vivo, In Vitro, Sequencing, Cell Culture, Fluorescence, Microscopy

    Resistin increases BNP and β-MHC mRNA expression that are reduced by metformin. (A) BNP mRNA and (B) β-MHC mRNA levels were examined by reverse transcription quantitative PCR. Data represent the mean ± SD. *P

    Journal: Biomedical Reports

    Article Title: LKB1/AMPK pathway mediates resistin-induced cardiomyocyte hypertrophy in H9c2 embryonic rat cardiomyocytes

    doi: 10.3892/br.2016.593

    Figure Lengend Snippet: Resistin increases BNP and β-MHC mRNA expression that are reduced by metformin. (A) BNP mRNA and (B) β-MHC mRNA levels were examined by reverse transcription quantitative PCR. Data represent the mean ± SD. *P

    Article Snippet: The BNP, β-MHC and 18s primers were designed and synthesized by Sangon Biotech Co., Ltd.

    Techniques: Expressing, Real-time Polymerase Chain Reaction

    Graphs of interested protein with ventricular proteins set as the control state. (A) SERCA2a protein synthesis, (B) α-MHC protein synthesis, (C) β-MHC protein synthesis, (D) TnT protein synthesis, and (E) α-actinin protein synthesis. N ≥ 3 and two tailed significance was set at * p

    Journal: Analytical Chemistry

    Article Title: Effects of Physiologic Mechanical Stimulation on Embryonic Chick Cardiomyocytes Using a Microfluidic Cardiac Cell Culture Model

    doi: 10.1021/ac503716z

    Figure Lengend Snippet: Graphs of interested protein with ventricular proteins set as the control state. (A) SERCA2a protein synthesis, (B) α-MHC protein synthesis, (C) β-MHC protein synthesis, (D) TnT protein synthesis, and (E) α-actinin protein synthesis. N ≥ 3 and two tailed significance was set at * p

    Article Snippet: After blocked with 5% nonfat milk, the membrane was probed with different primary antibodies including anti-SERCA2a (1:500) (LSBio, Seattle, WA), anti α-MHC (1:150) (Santa Cruz, Dallas, TX) and β-MHC (1:500) (Bioss, Woburn, MA), anti-Actinin (1:500) (Abcam, Cambridge, MA), anti TnT (1:1000) (Sigma-Aldrich, St. Louis, MO), and anti β-actin (1:1000) (Cell Signaling, Beverly, MA).

    Techniques: Two Tailed Test

    (A) Picture of the experimental setup of the CCCM system. Schematic of experimental design for chick ventricle embryonic cells. The day on the schematic was based on the 21-day chick embryo gestation. Abbreviation, ISO, isoproterenol. (B) SERCA 2a gene expressions, (C) α-MHC gene expressions, (D) β-MHC, and (E) PLB gene expressions. All samples were collected on day 16 (out of 21 days of gestation). Fold change for each gene of interest was determined by ΔΔC t using chick ED16 ventricles as the calibrating sample for comparison to the native in vivo level of expression. N ≥ 3 and p > 0.05. Abbreviations: ECT, engineered cardiac tissue; PLB, phospholamban.

    Journal: Analytical Chemistry

    Article Title: Effects of Physiologic Mechanical Stimulation on Embryonic Chick Cardiomyocytes Using a Microfluidic Cardiac Cell Culture Model

    doi: 10.1021/ac503716z

    Figure Lengend Snippet: (A) Picture of the experimental setup of the CCCM system. Schematic of experimental design for chick ventricle embryonic cells. The day on the schematic was based on the 21-day chick embryo gestation. Abbreviation, ISO, isoproterenol. (B) SERCA 2a gene expressions, (C) α-MHC gene expressions, (D) β-MHC, and (E) PLB gene expressions. All samples were collected on day 16 (out of 21 days of gestation). Fold change for each gene of interest was determined by ΔΔC t using chick ED16 ventricles as the calibrating sample for comparison to the native in vivo level of expression. N ≥ 3 and p > 0.05. Abbreviations: ECT, engineered cardiac tissue; PLB, phospholamban.

    Article Snippet: After blocked with 5% nonfat milk, the membrane was probed with different primary antibodies including anti-SERCA2a (1:500) (LSBio, Seattle, WA), anti α-MHC (1:150) (Santa Cruz, Dallas, TX) and β-MHC (1:500) (Bioss, Woburn, MA), anti-Actinin (1:500) (Abcam, Cambridge, MA), anti TnT (1:1000) (Sigma-Aldrich, St. Louis, MO), and anti β-actin (1:1000) (Cell Signaling, Beverly, MA).

    Techniques: In Vivo, Expressing

    Morphological changes induced by PE or ET-1 in cardiac myocytes after 4 h. Myocytes were either unstimulated ( Control , A ), or exposed to 40 μM PE ( B ) or 40 nM ET-1 ( C ) for 4 h and immunostained for β-MHC as described in Materials and Methods. Myocytes shown are representative of a typical field within a single experiment. The experiment was repeated on three further occasions with similar results. Bar, 25 μm.

    Journal: The Journal of Cell Biology

    Article Title: Stimulation of the p38 Mitogen-activated Protein Kinase Pathway in Neonatal Rat Ventricular Myocytes by the G Protein-coupled Receptor Agonists, Endothelin-1 and Phenylephrine: A Role in Cardiac Myocyte Hypertrophy?

    doi:

    Figure Lengend Snippet: Morphological changes induced by PE or ET-1 in cardiac myocytes after 4 h. Myocytes were either unstimulated ( Control , A ), or exposed to 40 μM PE ( B ) or 40 nM ET-1 ( C ) for 4 h and immunostained for β-MHC as described in Materials and Methods. Myocytes shown are representative of a typical field within a single experiment. The experiment was repeated on three further occasions with similar results. Bar, 25 μm.

    Article Snippet: A mouse monoclonal antibody to β-myosin heavy chain (β-MHC) was from Novocastra (Newcastle-upon-Tyne, Tyne and Wear, UK).

    Techniques:

    Effects of PD98059 or SB203580 on the morphological changes induced by PE in cardiac myocytes after 48 h. ( A–C ) Myocytes were unstimulated ( Control , A ), or exposed to 40 μM PE ( B and C ) for 48 h in the absence of inhibitors. ( D and E ) Myocytes were pretreated with 50 μM PD98059 ( D ) or 10 μM SB203580 ( E ) for 15 min and exposed to PE in the presence of inhibitors for 48 h. Myocytes were subsequently immunostained for β-MHC as described in Materials and Methods. Myocytes shown are representative of a typical field within a single experiment. The experiment was repeated on two further occasions with similar results. Bar, 25 μm.

    Journal: The Journal of Cell Biology

    Article Title: Stimulation of the p38 Mitogen-activated Protein Kinase Pathway in Neonatal Rat Ventricular Myocytes by the G Protein-coupled Receptor Agonists, Endothelin-1 and Phenylephrine: A Role in Cardiac Myocyte Hypertrophy?

    doi:

    Figure Lengend Snippet: Effects of PD98059 or SB203580 on the morphological changes induced by PE in cardiac myocytes after 48 h. ( A–C ) Myocytes were unstimulated ( Control , A ), or exposed to 40 μM PE ( B and C ) for 48 h in the absence of inhibitors. ( D and E ) Myocytes were pretreated with 50 μM PD98059 ( D ) or 10 μM SB203580 ( E ) for 15 min and exposed to PE in the presence of inhibitors for 48 h. Myocytes were subsequently immunostained for β-MHC as described in Materials and Methods. Myocytes shown are representative of a typical field within a single experiment. The experiment was repeated on two further occasions with similar results. Bar, 25 μm.

    Article Snippet: A mouse monoclonal antibody to β-myosin heavy chain (β-MHC) was from Novocastra (Newcastle-upon-Tyne, Tyne and Wear, UK).

    Techniques:

    Effects of PD98059 or SB203580 on the morphological changes induced by PE or ET-1 in cardiac myocytes after 8 h. ( A–C ) Myocytes were either unstimulated ( Control , A ), or exposed to 40 μM PE ( B ) or 40 nM ET-1 ( C ) for 8 h in the absence of inhibitors. ( D–F ) Myocytes were pretreated with 50 μM PD98059 for 15 min and exposed to 50 μM PD98059 alone ( D ), to PE in the presence of PD98059 ( E ), or to ET-1 in the presence of PD98059 ( F ) for 8 h. ( G–I ) Myocytes were pretreated with 10 μM SB203580 for 15 min and exposed to 10 μM SB203580 alone ( G ), to PE in the presence of SB203580 ( H ), or to ET-1 in the presence of SB203580 ( I ) for 8 h. Myocytes were subsequently immunostained for β-MHC as described in Materials and Methods. Myocytes shown are representative of a typical field within a single experiment. The experiment was repeated on five further occasions with similar results. Bar, 25 μm.

    Journal: The Journal of Cell Biology

    Article Title: Stimulation of the p38 Mitogen-activated Protein Kinase Pathway in Neonatal Rat Ventricular Myocytes by the G Protein-coupled Receptor Agonists, Endothelin-1 and Phenylephrine: A Role in Cardiac Myocyte Hypertrophy?

    doi:

    Figure Lengend Snippet: Effects of PD98059 or SB203580 on the morphological changes induced by PE or ET-1 in cardiac myocytes after 8 h. ( A–C ) Myocytes were either unstimulated ( Control , A ), or exposed to 40 μM PE ( B ) or 40 nM ET-1 ( C ) for 8 h in the absence of inhibitors. ( D–F ) Myocytes were pretreated with 50 μM PD98059 for 15 min and exposed to 50 μM PD98059 alone ( D ), to PE in the presence of PD98059 ( E ), or to ET-1 in the presence of PD98059 ( F ) for 8 h. ( G–I ) Myocytes were pretreated with 10 μM SB203580 for 15 min and exposed to 10 μM SB203580 alone ( G ), to PE in the presence of SB203580 ( H ), or to ET-1 in the presence of SB203580 ( I ) for 8 h. Myocytes were subsequently immunostained for β-MHC as described in Materials and Methods. Myocytes shown are representative of a typical field within a single experiment. The experiment was repeated on five further occasions with similar results. Bar, 25 μm.

    Article Snippet: A mouse monoclonal antibody to β-myosin heavy chain (β-MHC) was from Novocastra (Newcastle-upon-Tyne, Tyne and Wear, UK).

    Techniques:

    Effects of PD98059 or SB203580 on the morphological changes induced by PE or ET-1 in cardiac myocytes after 24 h. ( A–C ) Myocytes were either unstimulated ( Control , A ), or exposed to 40 μM PE ( B ) or 40 nM ET-1 ( C ) for 24 h in the absence of inhibitors. ( D–F ) Myocytes were pretreated with 50 μM PD98059 for 15 min and exposed to 50 μM PD98059 alone ( D ), to PE in the presence of PD98059 ( E ), or to ET-1 in the presence of PD98059 ( F ) for 24 h. ( G–I ) Myocytes were pretreated with 10 μM SB203580 for 15 min and exposed to 10 μM SB203580 alone ( G ), to PE in the presence of SB203580 ( H ), or to ET-1 in the presence of SB203580 ( I ) for 24 h. Myocytes were subsequently immunostained for β-MHC as described in Materials and Methods. Myocytes shown are representative of a typical field within a single experiment. The experiment was repeated on three further occasions with similar results. Bar, 25 μm.

    Journal: The Journal of Cell Biology

    Article Title: Stimulation of the p38 Mitogen-activated Protein Kinase Pathway in Neonatal Rat Ventricular Myocytes by the G Protein-coupled Receptor Agonists, Endothelin-1 and Phenylephrine: A Role in Cardiac Myocyte Hypertrophy?

    doi:

    Figure Lengend Snippet: Effects of PD98059 or SB203580 on the morphological changes induced by PE or ET-1 in cardiac myocytes after 24 h. ( A–C ) Myocytes were either unstimulated ( Control , A ), or exposed to 40 μM PE ( B ) or 40 nM ET-1 ( C ) for 24 h in the absence of inhibitors. ( D–F ) Myocytes were pretreated with 50 μM PD98059 for 15 min and exposed to 50 μM PD98059 alone ( D ), to PE in the presence of PD98059 ( E ), or to ET-1 in the presence of PD98059 ( F ) for 24 h. ( G–I ) Myocytes were pretreated with 10 μM SB203580 for 15 min and exposed to 10 μM SB203580 alone ( G ), to PE in the presence of SB203580 ( H ), or to ET-1 in the presence of SB203580 ( I ) for 24 h. Myocytes were subsequently immunostained for β-MHC as described in Materials and Methods. Myocytes shown are representative of a typical field within a single experiment. The experiment was repeated on three further occasions with similar results. Bar, 25 μm.

    Article Snippet: A mouse monoclonal antibody to β-myosin heavy chain (β-MHC) was from Novocastra (Newcastle-upon-Tyne, Tyne and Wear, UK).

    Techniques:

    Vezf1 is expressed in adult cardiomyocytes and regulates cardiomyocyte growth and cardiomyopathy related genes. (A) qRT-PCR analysis of the expression of endothelial nitric oxide synthase (eNOS), collagen type I alpha 1 chain (Col1a1), and α myosin heavy chain 6 (α-MHC) mRNAs in pools of fractionated resident mouse cardiac cells. eNOS, Col1a1 and α-MHC were used as markers for endothelial cells (Endo), fibroblasts (Fibro), and cardiomyocytes (Myo), respectively. n = 5. (B) qPCR analysis of Vezf1 mRNA levels in cardiomyocytes and fibroblasts relative to that in the endothelial cells. n = 5. (C) Adult rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or Control siRNA (100 nM) and 3 days later RNA samples were collected. Shown is qRT-PCR analysis for expression of Vezf1. Results are normalized to expression of 18S (18S ribosomal RNA). n = 6. (D and E) Adult rat ventricular cardiomyocytes were transfected with two distinct Vezf1 siRNAs (100 nM) or Control siRNA (100 nM) and 1 day later cells were stimulated with isoprenaline (Iso, 1 µM) for 48 h where indicated. (D) Shown is microscopy analysis for cardiomyocyte size. Ctrl siRNA n = 8, Vezf1 A siRNA n = 9, Vezf1 B siRNA n = 10; Ctrl siRNA + Iso n = 10, Vezf1 A siRNA + Iso n = 15, Vezf1 B siRNA + Iso n = 13. (E) Shown is microscopy analysis for sarcomere length (µm). Ctrl siRNA n = 14, Vezf1 B siRNA n = 18; Ctrl siRNA + Iso n = 22, Vezf1 B siRNA + Iso n = 25. (F) Adult rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or control siRNA and 3 days later Ca 2+ cycling and cardiomyocyte (CM) shortening were analyzed. Ctrl n = 44, Vezf1 siRNA n = 43. (G) Neonatal rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or control siRNA and 2 days later cells were treated with Iso (1 µM) for 24 h. Shown is qRT-PCR analysis for expression of Vezf1, β-MHC (myosin heavy chain beta-subunit), Ska (skeletal alpha actin), ANP (atrial natriuretic peptide) and β-MHC versus Ska ratio. Results are normalized to expression of 18S (18S ribosomal RNA). n = 4. (H-I) Neonatal rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or control siRNA (100 nM) and 3 days later cells were treated with either vehicle, phenylephrine (PE, 100 µM) or basic fibroblast growth factor (FGF, 20 ng/ml) for 48 h. (H) Shown is immunoblot analysis for β-MHC, ANP, GAPDH, Ska and Vinculin. (I) Shown is β-MHC versus Ska ratio from immunoblot quantification. n = 4. * P

    Journal: EBioMedicine

    Article Title: Vezf1 regulates cardiac structure and contractile function

    doi: 10.1016/j.ebiom.2019.102608

    Figure Lengend Snippet: Vezf1 is expressed in adult cardiomyocytes and regulates cardiomyocyte growth and cardiomyopathy related genes. (A) qRT-PCR analysis of the expression of endothelial nitric oxide synthase (eNOS), collagen type I alpha 1 chain (Col1a1), and α myosin heavy chain 6 (α-MHC) mRNAs in pools of fractionated resident mouse cardiac cells. eNOS, Col1a1 and α-MHC were used as markers for endothelial cells (Endo), fibroblasts (Fibro), and cardiomyocytes (Myo), respectively. n = 5. (B) qPCR analysis of Vezf1 mRNA levels in cardiomyocytes and fibroblasts relative to that in the endothelial cells. n = 5. (C) Adult rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or Control siRNA (100 nM) and 3 days later RNA samples were collected. Shown is qRT-PCR analysis for expression of Vezf1. Results are normalized to expression of 18S (18S ribosomal RNA). n = 6. (D and E) Adult rat ventricular cardiomyocytes were transfected with two distinct Vezf1 siRNAs (100 nM) or Control siRNA (100 nM) and 1 day later cells were stimulated with isoprenaline (Iso, 1 µM) for 48 h where indicated. (D) Shown is microscopy analysis for cardiomyocyte size. Ctrl siRNA n = 8, Vezf1 A siRNA n = 9, Vezf1 B siRNA n = 10; Ctrl siRNA + Iso n = 10, Vezf1 A siRNA + Iso n = 15, Vezf1 B siRNA + Iso n = 13. (E) Shown is microscopy analysis for sarcomere length (µm). Ctrl siRNA n = 14, Vezf1 B siRNA n = 18; Ctrl siRNA + Iso n = 22, Vezf1 B siRNA + Iso n = 25. (F) Adult rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or control siRNA and 3 days later Ca 2+ cycling and cardiomyocyte (CM) shortening were analyzed. Ctrl n = 44, Vezf1 siRNA n = 43. (G) Neonatal rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or control siRNA and 2 days later cells were treated with Iso (1 µM) for 24 h. Shown is qRT-PCR analysis for expression of Vezf1, β-MHC (myosin heavy chain beta-subunit), Ska (skeletal alpha actin), ANP (atrial natriuretic peptide) and β-MHC versus Ska ratio. Results are normalized to expression of 18S (18S ribosomal RNA). n = 4. (H-I) Neonatal rat ventricular cardiomyocytes were transfected with Vezf1 siRNA (100 nM) or control siRNA (100 nM) and 3 days later cells were treated with either vehicle, phenylephrine (PE, 100 µM) or basic fibroblast growth factor (FGF, 20 ng/ml) for 48 h. (H) Shown is immunoblot analysis for β-MHC, ANP, GAPDH, Ska and Vinculin. (I) Shown is β-MHC versus Ska ratio from immunoblot quantification. n = 4. * P

    Article Snippet: Primary antibodies used were 1:1000 β-MHC (MAB1628, RRID: AB_2,282,287, Merck, Darmstadt, Germany), 1:1000 skeletal alpha actin (Ska, ab28052, RRID: AB_867,491, Abcam, Cambridge, United Kingdom), 1:1000 atrial natriuretic peptide (ANP, custom made), 1:2000 Vinculin (ab18058, RRID: AB_444,215, Abcam), 1:500 TEAD-1 (610,922, RRID: AB_398,237, BD) and 1:1,000,000 glyceraldehyde 3‐phosphate dehydrogenase (GAPDH, MAB374, RRID: AB_2,107,445, Millipore).

    Techniques: Quantitative RT-PCR, Expressing, Real-time Polymerase Chain Reaction, Transfection, Microscopy, Aqueous Normal-phase Chromatography

    Vezf1 targets an MCAT binding site within β-MHC promoter and interacts with TEAD-1. (A) Neonatal rat ventricular cardiomyocytes (NRVMs) were transfected with β-MHC promoter (−171 to −3500 bp) luciferase reporter constructs together with Vezf1 siRNA (100 nM) or control siRNA (100 nM). 3 days later, relative luciferase activities were analyzed. Firefly luciferase activities were normalized to renilla luciferase activity and expressed as relative to the activity of respective β-MHC promoter luciferase construct treated with control siRNA. n = 4. (B–D) NRVMs were transfected with an intact −408 β-MHC promoter construct or with −408 β-MHC promoter construct containing either Δβe1, Δβe2 or Δβe3 mutation together with (B) control siRNA (100 nM) ( n = 6–8) or (C) Vezf1 siRNA (100 nM) ( n = 3–7). 3 days later, relative luciferase activities of the different lengths of β-MHC promoter constructs were analyzed. Firefly luciferase activities were normalized to renilla luciferase and the data are expressed as relative to that of the wild-type −408 β-MHC promoter construct activity. (D) Comparison of relative change in luciferase activity of −408 β-MHC Δβe1, Δβe2 or Δβe3 promoter construct to that of wild-type −408 β-MHC promoter luciferase construct in control siRNA and Vezf1 siRNA treated cells. n = 3–8. (E) Adult rat left ventricular (LV) tissue samples were immunoprecipitated with Vezf1 antibody or control IgG. Shown is immunoblot analysis for Transcription enhancer factor-1 (TEAD-1) in immunoprecipitates and LV lysates. (F) NRVMs were transfected with two distinct TEAD-1 siRNAs (100 nM) or control siRNA (100 nM) and 3 days later protein samples were collected. Shown is immunoblot analysis for TEAD-1 in rat LV lysates and in NRVMs. * P

    Journal: EBioMedicine

    Article Title: Vezf1 regulates cardiac structure and contractile function

    doi: 10.1016/j.ebiom.2019.102608

    Figure Lengend Snippet: Vezf1 targets an MCAT binding site within β-MHC promoter and interacts with TEAD-1. (A) Neonatal rat ventricular cardiomyocytes (NRVMs) were transfected with β-MHC promoter (−171 to −3500 bp) luciferase reporter constructs together with Vezf1 siRNA (100 nM) or control siRNA (100 nM). 3 days later, relative luciferase activities were analyzed. Firefly luciferase activities were normalized to renilla luciferase activity and expressed as relative to the activity of respective β-MHC promoter luciferase construct treated with control siRNA. n = 4. (B–D) NRVMs were transfected with an intact −408 β-MHC promoter construct or with −408 β-MHC promoter construct containing either Δβe1, Δβe2 or Δβe3 mutation together with (B) control siRNA (100 nM) ( n = 6–8) or (C) Vezf1 siRNA (100 nM) ( n = 3–7). 3 days later, relative luciferase activities of the different lengths of β-MHC promoter constructs were analyzed. Firefly luciferase activities were normalized to renilla luciferase and the data are expressed as relative to that of the wild-type −408 β-MHC promoter construct activity. (D) Comparison of relative change in luciferase activity of −408 β-MHC Δβe1, Δβe2 or Δβe3 promoter construct to that of wild-type −408 β-MHC promoter luciferase construct in control siRNA and Vezf1 siRNA treated cells. n = 3–8. (E) Adult rat left ventricular (LV) tissue samples were immunoprecipitated with Vezf1 antibody or control IgG. Shown is immunoblot analysis for Transcription enhancer factor-1 (TEAD-1) in immunoprecipitates and LV lysates. (F) NRVMs were transfected with two distinct TEAD-1 siRNAs (100 nM) or control siRNA (100 nM) and 3 days later protein samples were collected. Shown is immunoblot analysis for TEAD-1 in rat LV lysates and in NRVMs. * P

    Article Snippet: Primary antibodies used were 1:1000 β-MHC (MAB1628, RRID: AB_2,282,287, Merck, Darmstadt, Germany), 1:1000 skeletal alpha actin (Ska, ab28052, RRID: AB_867,491, Abcam, Cambridge, United Kingdom), 1:1000 atrial natriuretic peptide (ANP, custom made), 1:2000 Vinculin (ab18058, RRID: AB_444,215, Abcam), 1:500 TEAD-1 (610,922, RRID: AB_398,237, BD) and 1:1,000,000 glyceraldehyde 3‐phosphate dehydrogenase (GAPDH, MAB374, RRID: AB_2,107,445, Millipore).

    Techniques: Binding Assay, Transfection, Luciferase, Construct, Activity Assay, Mutagenesis, Immunoprecipitation

    Effect of ROCK inhibition on early hypertrophy markers after MI (β-MHC and -SKA) . (a) Upper panel: representative western blot images for β-MHC from left ventricle in rats 1 week post-MI in the 3 experimental groups. Lower panel: comparative densitometric analysis in the 3 groups (sham, n = 5; MI, n = 7 and MI treated with fasudil, n = 4). (b) Upper panel: representative western blot images for α-SKA from left ventricle in rats 1 week post-MI in the 3 experimental groups (upper panel). Lower panel: comparative densitometric analysis in the three groups ( n = 3 per group). Quantifications are shown as relative to the sham group (in folds). All measurements were normalized by GAPDH levels. Data are expressed as mean ± standard error of the mean. # p

    Journal: Therapeutic Advances in Cardiovascular Disease

    Article Title: Mechanisms of favorable effects of Rho kinase inhibition on myocardial remodeling and systolic function after experimental myocardial infarction in the rat

    doi: 10.1177/1753944715609516

    Figure Lengend Snippet: Effect of ROCK inhibition on early hypertrophy markers after MI (β-MHC and -SKA) . (a) Upper panel: representative western blot images for β-MHC from left ventricle in rats 1 week post-MI in the 3 experimental groups. Lower panel: comparative densitometric analysis in the 3 groups (sham, n = 5; MI, n = 7 and MI treated with fasudil, n = 4). (b) Upper panel: representative western blot images for α-SKA from left ventricle in rats 1 week post-MI in the 3 experimental groups (upper panel). Lower panel: comparative densitometric analysis in the three groups ( n = 3 per group). Quantifications are shown as relative to the sham group (in folds). All measurements were normalized by GAPDH levels. Data are expressed as mean ± standard error of the mean. # p

    Article Snippet: After blocking with 7% nonfat milk (for nonphosphorylated proteins) or bovine serum albumin (BSA) 5% (for phosphorylated proteins) for 1 hour at room temperature, the blots were incubated overnight at 4°C with the following antibodies: anti-myosin phosphatase target subunit-1 (MYPT-1, mouse monoclonal, 1/1000 BD Biosciences, Cat 612164); p-MYPT-1 (phospho-MYPT1-Thr 853 rabbit polyclonal, 1/700, Cyclex Co, Cat CY-P1025), ezrin–radixin–moesin (ERM, total-ERM, rabbit polyclonal, 1/700, Cell Signaling, Cat 3142S); p-ERM (phospho-ERM, Ezrin Thr567, Radixin Thr564, Moesin Thr558, rabbit polyclonal, 1/700, Cell Signaling, Cat 3141F); β-MHC (myosin heavy chain, mouse monoclonal, 1/1000, Novocastra TM); α-SKA (α-skeletal actin, mouse monoclonal, 1/2500, US Biological Life Sciences, Cat A0760-24); p-SMAD3 (phospho-SMAD S423/425, rabbit monoclonal, 1/1000, Cell Signaling, Cat 8769S); SMAD3 (total-SMAD, rabbit monoclonal, 1/1000, Cell Signaling, Cat 9523S); ROCK-1 (mouse monoclonal, 1/1000, BD BioScience, Cat 611136); ROCK-2 (mouse monoclonal, 1/1000, BD BioScience, Cat 610623); troponin I (cTnI, total-troponin I, mouse monoclonal, 1/1000, Abcam, Cat Ab19615); p -cTnI (phospho-troponin I, phospho S22+S23, 1/1000, Rabbit polyclonal, Abcam, Cat Ab58545); ERK1/2 (total extracellular-signal-regulated kinase, rabbit polyclonal, 1/1000, Cell Signaling, Cat 9102); p -ERK1/2 (phospho-ERK 44/42 Thr202/Tyr204, 1/1000, Cell Signaling, Cat 9101); GATA-4 (total-GATA-4, rabbit polyclonal, 1/1000, Thermo Scientific, Cat PA592663); and p -GATA-4 (Phospho-GATA-4, phospho S105, 1/1000, rabbit polyclonal, Abcam, Cat 5245).

    Techniques: Inhibition, Western Blot

    Triptolide attenuated cardiac hypertrophy in mice. Cardiac hypertrophy was induced by isoproterenol (Iso, 5 mg/kg, s.c., for 14 days) in mice ( n = 8–10 in each group). (A) Body weight; (B) heart weight (HW) index to tibia length (TL); (C) left ventricular weight (LVW) indexes to TL; (D) α-myosin heavy chain (MHC) mRNA expression level; (E) β-MHC mRNA expression level; (F) atrial natriuretic peptide (ANP) mRNA expression level. These mRNA expression levels were measured with Real-time PCR method and normalized to β-actin and control group, respectively. The data are presented as mean ± SEM, ∗∗ p

    Journal: Frontiers in Pharmacology

    Article Title: Triptolide Upregulates Myocardial Forkhead Helix Transcription Factor p3 Expression and Attenuates Cardiac Hypertrophy

    doi: 10.3389/fphar.2016.00471

    Figure Lengend Snippet: Triptolide attenuated cardiac hypertrophy in mice. Cardiac hypertrophy was induced by isoproterenol (Iso, 5 mg/kg, s.c., for 14 days) in mice ( n = 8–10 in each group). (A) Body weight; (B) heart weight (HW) index to tibia length (TL); (C) left ventricular weight (LVW) indexes to TL; (D) α-myosin heavy chain (MHC) mRNA expression level; (E) β-MHC mRNA expression level; (F) atrial natriuretic peptide (ANP) mRNA expression level. These mRNA expression levels were measured with Real-time PCR method and normalized to β-actin and control group, respectively. The data are presented as mean ± SEM, ∗∗ p

    Article Snippet: The proteins were transferred onto a PVDF membrane (Millipore, Bedford, MA, USA) and incubated with a primary β-MHC antibody (1:1000; Santa Cruz Biotechnology, Santa Cruz, CA, USA) at 4°C overnight, followed by horseradish peroxidase (HRP)-conjugated secondary antibody.

    Techniques: Mouse Assay, Expressing, Aqueous Normal-phase Chromatography, Real-time Polymerase Chain Reaction

    The effects of triptolide on the myocardial expression of myosin heavy chains (MHC). Cardiac hypertrophy was induced by isoproterenol (Iso, 5 mg/kg, s.c., for 14 days) in mice ( n = 8–10 in each group). The mice were treated with normal saline, Iso, and triptolide (10, 30, 90 μg/kg), respectively, for 14 days. (A) The expression of α- and β-MHC were determined with immunohistochemistry (bar = 10 μm); (B) Expression of α-MHC; (C) Expression of β-MHC. The data are presented as mean ± SEM, ∗∗ p

    Journal: Frontiers in Pharmacology

    Article Title: Triptolide Upregulates Myocardial Forkhead Helix Transcription Factor p3 Expression and Attenuates Cardiac Hypertrophy

    doi: 10.3389/fphar.2016.00471

    Figure Lengend Snippet: The effects of triptolide on the myocardial expression of myosin heavy chains (MHC). Cardiac hypertrophy was induced by isoproterenol (Iso, 5 mg/kg, s.c., for 14 days) in mice ( n = 8–10 in each group). The mice were treated with normal saline, Iso, and triptolide (10, 30, 90 μg/kg), respectively, for 14 days. (A) The expression of α- and β-MHC were determined with immunohistochemistry (bar = 10 μm); (B) Expression of α-MHC; (C) Expression of β-MHC. The data are presented as mean ± SEM, ∗∗ p

    Article Snippet: The proteins were transferred onto a PVDF membrane (Millipore, Bedford, MA, USA) and incubated with a primary β-MHC antibody (1:1000; Santa Cruz Biotechnology, Santa Cruz, CA, USA) at 4°C overnight, followed by horseradish peroxidase (HRP)-conjugated secondary antibody.

    Techniques: Expressing, Mouse Assay, Immunohistochemistry

    Triptolide attenuated the hypertrophic response of neonatal rat ventricular myocytes. Hypertrophic response of neonatal rat ventricular myocytes (NRVM) was induced by angiotensin II (Ang II). (A) NRVM treated with Ang II (1 μmol/L) and triptolide (TP) for 24 h, stained with rhodamine-phalloidin (bar = 50 μm); (B) cell size ( n = 50 cells in each group); (C) β-MHC mRNA expression determined using Real-time PCR ( n = 4); (D) β-MHC expression level determined using Western blotting ( n = 4). The data are presented as mean ± SEM, ∗∗ p

    Journal: Frontiers in Pharmacology

    Article Title: Triptolide Upregulates Myocardial Forkhead Helix Transcription Factor p3 Expression and Attenuates Cardiac Hypertrophy

    doi: 10.3389/fphar.2016.00471

    Figure Lengend Snippet: Triptolide attenuated the hypertrophic response of neonatal rat ventricular myocytes. Hypertrophic response of neonatal rat ventricular myocytes (NRVM) was induced by angiotensin II (Ang II). (A) NRVM treated with Ang II (1 μmol/L) and triptolide (TP) for 24 h, stained with rhodamine-phalloidin (bar = 50 μm); (B) cell size ( n = 50 cells in each group); (C) β-MHC mRNA expression determined using Real-time PCR ( n = 4); (D) β-MHC expression level determined using Western blotting ( n = 4). The data are presented as mean ± SEM, ∗∗ p

    Article Snippet: The proteins were transferred onto a PVDF membrane (Millipore, Bedford, MA, USA) and incubated with a primary β-MHC antibody (1:1000; Santa Cruz Biotechnology, Santa Cruz, CA, USA) at 4°C overnight, followed by horseradish peroxidase (HRP)-conjugated secondary antibody.

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

    Ang II increases while Neb and Rap suppress the Ang II-induced increase in miR-208a effector β-MHC (A) Representative autoradiogram and densitometric analysis using Quantity One software (graph) after Western blotting of untreated and treated HL-1 cell lysates (treated with Ang II or Ang II+Neb) and probing with anti- β-MHC antibody. (B) Representative images from immunofluorescence analysis of untreated and treated HL-1 cells. (C) Representative autoradiogram and densitometric analysis using Quantity One software (graph) after Western blotting of HL-1 cell lysates (Untreated (Con) or treated with Ang II or Ang II+Neb) and probing with anti- β-MHC antibody. Treatments with Ang II (100nM:12hrs) Neb (1µM:12 hrs)) or Rap (10nM: 12hrs) were similar to those performed for the data shown in Fig. 1 . Treatments were performed in triplicate. Neb- and Rap-treatment suppressed Ang II-induced increase in β-MHC (A, C). Immunofluorescence staining with anti- β-MHC antibody and nuclear stain DAPI indicated that in individual cells Ang II increased and Neb suppressed β-MHC (B). *p

    Journal: Obesity (Silver Spring, Md.)

    Article Title: Regulation of cardiac miR-208a, an inducer of obesity, by Rapamycin and Nebivolol

    doi: 10.1002/oby.21227

    Figure Lengend Snippet: Ang II increases while Neb and Rap suppress the Ang II-induced increase in miR-208a effector β-MHC (A) Representative autoradiogram and densitometric analysis using Quantity One software (graph) after Western blotting of untreated and treated HL-1 cell lysates (treated with Ang II or Ang II+Neb) and probing with anti- β-MHC antibody. (B) Representative images from immunofluorescence analysis of untreated and treated HL-1 cells. (C) Representative autoradiogram and densitometric analysis using Quantity One software (graph) after Western blotting of HL-1 cell lysates (Untreated (Con) or treated with Ang II or Ang II+Neb) and probing with anti- β-MHC antibody. Treatments with Ang II (100nM:12hrs) Neb (1µM:12 hrs)) or Rap (10nM: 12hrs) were similar to those performed for the data shown in Fig. 1 . Treatments were performed in triplicate. Neb- and Rap-treatment suppressed Ang II-induced increase in β-MHC (A, C). Immunofluorescence staining with anti- β-MHC antibody and nuclear stain DAPI indicated that in individual cells Ang II increased and Neb suppressed β-MHC (B). *p

    Article Snippet: All antibodies except anti-β-MHC antibody were from Cell Signaling Technology Inc. (Boston, MA).

    Techniques: Software, Western Blot, Immunofluorescence, Staining