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Impact of ANKRD1 mutations associated with hypertrophic cardiomyopathy on contraction parameters of engineered heart tissue

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Impact of ANKRD1 mutations associated with hypertrophic cardiomyopathy on contraction parameters of engineered heart tissue. / Crocini, Claudia ; Arimura, Takuro; Reischmann, Silke; Eder, Alexandra; Braren, Ingke ; Hansen, Arne; Eschenhagen, Thomas; Kimura, Akinori; Carrier, Lucie.

in: BASIC RES CARDIOL, Jahrgang 108, Nr. 3, 01.01.2013, S. 349.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Crocini, C, Arimura, T, Reischmann, S, Eder, A, Braren, I, Hansen, A, Eschenhagen, T, Kimura, A & Carrier, L 2013, 'Impact of ANKRD1 mutations associated with hypertrophic cardiomyopathy on contraction parameters of engineered heart tissue', BASIC RES CARDIOL, Jg. 108, Nr. 3, S. 349. https://doi.org/10.1007/s00395-013-0349-x

APA

Crocini, C., Arimura, T., Reischmann, S., Eder, A., Braren, I., Hansen, A., Eschenhagen, T., Kimura, A., & Carrier, L. (2013). Impact of ANKRD1 mutations associated with hypertrophic cardiomyopathy on contraction parameters of engineered heart tissue. BASIC RES CARDIOL, 108(3), 349. https://doi.org/10.1007/s00395-013-0349-x

Vancouver

Crocini C, Arimura T, Reischmann S, Eder A, Braren I, Hansen A et al. Impact of ANKRD1 mutations associated with hypertrophic cardiomyopathy on contraction parameters of engineered heart tissue. BASIC RES CARDIOL. 2013 Jan 1;108(3):349. https://doi.org/10.1007/s00395-013-0349-x

Bibtex

@article{61535e1d00dc42a9862b840b5a6d02f4,
title = "Impact of ANKRD1 mutations associated with hypertrophic cardiomyopathy on contraction parameters of engineered heart tissue",
abstract = "Hypertrophic cardiomyopathy (HCM) is a myocardial disease associated with mutations in sarcomeric genes. Three mutations were found in ANKRD1, encoding ankyrin repeat domain 1 (ANKRD1), a transcriptional co-factor located in the sarcomere. In the present study, we investigated whether expression of HCM-associated ANKRD1 mutations affects contraction parameters after gene transfer in engineered heart tissues (EHTs). EHTs were generated from neonatal rat heart cells and were transduced with adeno-associated virus encoding GFP or myc-tagged wild-type (WT) or mutant (P52A, T123M, or I280V) ANKRD1. Contraction parameters were analyzed from day 8 to day 16 of culture, and evaluated in the absence or presence of the proteasome inhibitor epoxomicin for 24 h. Under standard conditions, only WT- and T123M-ANKRD1 were correctly incorporated in the sarcomere. T123M-ANKRD1-transduced EHTs exhibited higher force and velocities of contraction and relaxation than WT- P52A- and I280V-ANKRD1 were highly unstable, not incorporated into the sarcomere, and did not induce contractile alterations. After epoxomicin treatment, P52A and I280V were both stabilized and incorporated into the sarcomere. I280V-transduced EHTs showed prolonged relaxation. These data suggest different impacts of ANKRD1 mutations on cardiomyocyte function: gain-of-function for T123M mutation under all conditions and dominant-negative effect for the I280V mutation which may come into play only when the proteasome is impaired.",
keywords = "Animals, Animals, Newborn, Cardiomyopathy, Hypertrophic, Cells, Cultured, Dependovirus, Fluorescent Antibody Technique, Gene Expression Regulation, Genetic Vectors, Genotype, Green Fluorescent Proteins, Humans, Muscle Proteins, Mutation, Myocardial Contraction, Myocytes, Cardiac, Nuclear Proteins, Oligopeptides, Phenotype, Proteasome Endopeptidase Complex, Proteasome Inhibitors, Rats, Repressor Proteins, Time Factors, Tissue Engineering, Transduction, Genetic, Transfection",
author = "Claudia Crocini and Takuro Arimura and Silke Reischmann and Alexandra Eder and Ingke Braren and Arne Hansen and Thomas Eschenhagen and Akinori Kimura and Lucie Carrier",
year = "2013",
month = jan,
day = "1",
doi = "10.1007/s00395-013-0349-x",
language = "English",
volume = "108",
pages = "349",
journal = "BASIC RES CARDIOL",
issn = "0300-8428",
publisher = "D. Steinkopff-Verlag",
number = "3",

}

RIS

TY - JOUR

T1 - Impact of ANKRD1 mutations associated with hypertrophic cardiomyopathy on contraction parameters of engineered heart tissue

AU - Crocini, Claudia

AU - Arimura, Takuro

AU - Reischmann, Silke

AU - Eder, Alexandra

AU - Braren, Ingke

AU - Hansen, Arne

AU - Eschenhagen, Thomas

AU - Kimura, Akinori

AU - Carrier, Lucie

PY - 2013/1/1

Y1 - 2013/1/1

N2 - Hypertrophic cardiomyopathy (HCM) is a myocardial disease associated with mutations in sarcomeric genes. Three mutations were found in ANKRD1, encoding ankyrin repeat domain 1 (ANKRD1), a transcriptional co-factor located in the sarcomere. In the present study, we investigated whether expression of HCM-associated ANKRD1 mutations affects contraction parameters after gene transfer in engineered heart tissues (EHTs). EHTs were generated from neonatal rat heart cells and were transduced with adeno-associated virus encoding GFP or myc-tagged wild-type (WT) or mutant (P52A, T123M, or I280V) ANKRD1. Contraction parameters were analyzed from day 8 to day 16 of culture, and evaluated in the absence or presence of the proteasome inhibitor epoxomicin for 24 h. Under standard conditions, only WT- and T123M-ANKRD1 were correctly incorporated in the sarcomere. T123M-ANKRD1-transduced EHTs exhibited higher force and velocities of contraction and relaxation than WT- P52A- and I280V-ANKRD1 were highly unstable, not incorporated into the sarcomere, and did not induce contractile alterations. After epoxomicin treatment, P52A and I280V were both stabilized and incorporated into the sarcomere. I280V-transduced EHTs showed prolonged relaxation. These data suggest different impacts of ANKRD1 mutations on cardiomyocyte function: gain-of-function for T123M mutation under all conditions and dominant-negative effect for the I280V mutation which may come into play only when the proteasome is impaired.

AB - Hypertrophic cardiomyopathy (HCM) is a myocardial disease associated with mutations in sarcomeric genes. Three mutations were found in ANKRD1, encoding ankyrin repeat domain 1 (ANKRD1), a transcriptional co-factor located in the sarcomere. In the present study, we investigated whether expression of HCM-associated ANKRD1 mutations affects contraction parameters after gene transfer in engineered heart tissues (EHTs). EHTs were generated from neonatal rat heart cells and were transduced with adeno-associated virus encoding GFP or myc-tagged wild-type (WT) or mutant (P52A, T123M, or I280V) ANKRD1. Contraction parameters were analyzed from day 8 to day 16 of culture, and evaluated in the absence or presence of the proteasome inhibitor epoxomicin for 24 h. Under standard conditions, only WT- and T123M-ANKRD1 were correctly incorporated in the sarcomere. T123M-ANKRD1-transduced EHTs exhibited higher force and velocities of contraction and relaxation than WT- P52A- and I280V-ANKRD1 were highly unstable, not incorporated into the sarcomere, and did not induce contractile alterations. After epoxomicin treatment, P52A and I280V were both stabilized and incorporated into the sarcomere. I280V-transduced EHTs showed prolonged relaxation. These data suggest different impacts of ANKRD1 mutations on cardiomyocyte function: gain-of-function for T123M mutation under all conditions and dominant-negative effect for the I280V mutation which may come into play only when the proteasome is impaired.

KW - Animals

KW - Animals, Newborn

KW - Cardiomyopathy, Hypertrophic

KW - Cells, Cultured

KW - Dependovirus

KW - Fluorescent Antibody Technique

KW - Gene Expression Regulation

KW - Genetic Vectors

KW - Genotype

KW - Green Fluorescent Proteins

KW - Humans

KW - Muscle Proteins

KW - Mutation

KW - Myocardial Contraction

KW - Myocytes, Cardiac

KW - Nuclear Proteins

KW - Oligopeptides

KW - Phenotype

KW - Proteasome Endopeptidase Complex

KW - Proteasome Inhibitors

KW - Rats

KW - Repressor Proteins

KW - Time Factors

KW - Tissue Engineering

KW - Transduction, Genetic

KW - Transfection

U2 - 10.1007/s00395-013-0349-x

DO - 10.1007/s00395-013-0349-x

M3 - SCORING: Journal article

C2 - 23572067

VL - 108

SP - 349

JO - BASIC RES CARDIOL

JF - BASIC RES CARDIOL

SN - 0300-8428

IS - 3

ER -