Cited by 538Cardiomyopathy and Myosin StudiesCardiac Fibrosis and RemodelingCardiovascular Function and Risk Factors

Myosin heavy chain isoform expression in the failing and nonfailing human heart

Miyata, Setsuya, Minobe, Wayne, Bristow, Michael R., Leinwand, Leslie A.·2000·Circulation Research

Abstract

Abstract —In the heart, the relative proportions of the 2 forms of the motor protein myosin heavy chain (MyHC) have been shown to be affected by a wide variety of pathological and physiological stimuli. Hearts that express the faster MyHC motor protein, α, produce more power than those expressing the slower MyHC motor protein, β, leading to the hypothesis that MyHC isoforms play a major role in the determination of cardiac contractility. We showed previously that a significant amount of αMyHC mRNA is expressed in nonfailing human ventricular myocardium and that αMyHC mRNA expression is decreased 15-fold in end-stage failing left ventricles. In the present study, we determined the MyHC protein isoform content of human heart samples of known MyHC mRNA composition. We demonstrate that αMyHC protein was easily detectable in 12 nonfailing hearts. αMyHC protein represented 7.2±3.2% of total MyHC protein (compared with ≈35% of the MyHC mRNA), suggesting that translational regulation may be operative; in contrast, there was effectively no detectable αMyHC protein in the left ventricles of 10 end-stage failing human hearts.

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Crossref · 10.1161/01.res.86.4.386

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  • Rabbit ventricles predominantly express beta-MHC (88% to >95%), similar to human ventricles (>90-95%).

    “Rabbit ventricles predominately express β-MHC (88% to >95%) (Hamilton & Ianuzzo, 1991; James, et al., 2005; Suzuki, et al., 2009) similar to humans (>90–95%) (Miyata, et al., 2000; Reiser, et al., 2001).”
  • Canine ventricular myocardium predominantly expresses slow beta-MHC (>80-100%), similar to humans (>90-95%).

    “The canine ventricular myocardium predominately expresses slow β-MHC (>80–100%) similar to humans (>90–95%) (Fuller, Bicer, Hamlin, Yamaguchi, & Reiser, 2007; Hamilton & Ianuzzo, 1991; Miyata, et al., 2000; Reiser, et al., 2001).”
  • Swine ventricles predominantly express beta-MHC (~100%, 87% sub-epicardium, 97% sub-endocardium), similar to humans (>90-95%).

    “Swine ventricles predominately express β-MHC (~100%, 87% sub-epicardium, 97% sub-endocardium) similar to humans’ (>90–95%) (Hamilton & Ianuzzo, 1991; Locher, et al., 2011; Miyata, et al., 2000; Reiser, et al., 2001; Stelzer, et al., 2008).”
  • The predominant myosin heavy chain isoform in sheep is slow beta-MHC (~100%), similar to humans (>90-95%).

    “The predominate myosin heavy chain isoform is the slow β-MHC in sheep (~100%) similar to humans (>90–95%) (Hamilton & Ianuzzo, 1991; Miyata, et al., 2000; Reiser, et al., 2001).”

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Cites

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Research works printed but not linked: 6

  1. Alpert NR, Mulieri LA. Increased myothermal economy of isometric force generation in compensated cardiac hypertrophy induced by pulmonary artery constriction in the rabbit. Circ Res. 1982;50: 491-500.
  2. Holubarsch CH, Goulette RP, Litten RZ, Martin BJ, Mulieri LA, Alpert NR. The economy force development, myosin isozyme pattern and myofibrillar ATPase activity in normal and hyperthyroid rat myocardium. Circ Res. 1985;56:78 -86.
  3. Lompre AM, Schwartz K, d'Albis A, Lacombe G, Thiem NV, Swynghedauw B. Myosin isozyme re-distribution in chronic heart over-load. Nature. 1979;282:105-107.
  4. Mercadier JJ, Bouveret P, Gorza L, Schiaffino S, Clark WA, Zak R, Swynghedauw B, Schwartz K. Myosin isozymes in normal and hyper- trophied human ventricle myocardium. Circ Res. 1983;53:52-62.
  5. Bouvagnet P, Leger J, Pons F, Dechesne C, Leger J. Fiber types and myosin types in human atrial and ventricular myocardium. Circ Res. 1984;55:794 -804.
  6. Sata M, Ikebe M. Functional analysis of the mutations in the human ␤-cardiac myosin that are responsible for familial hypertrophic car- diomyopathy. J Clin Invest. 1996;98:2866 -2873.

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Authors
Miyata, S., Minobe, W., Bristow, M. R., & Leinwand, L. A.
Affiliations
  • From the Department of Molecular, Cellular and Developmental Biology (S.M., L.A.L.), University of Colorado (Boulder); and Division of Cardiology (W.M., M.B.), University of Colorado Health Science Center (Denver).
  • University of Colorado Boulder (US)
Venue
Circulation Research
Published
2000-03-03
Volume
86
Issue
4
Pages
386-390
ISSN
  • 0009-7330 (ISSN-L)
  • 1524-4571
OpenAlex
W2119706727
Cited by
538
References
38
Citations by year
2026: 8 · 2025: 28 · 2024: 9 · 2023: 24 · 2022: 23 · 2021: 19 · 2020: 23 · 2019: 16 · 2018: 24 · 2017: 22 · 2016: 35 · 2015: 22 · 2014: 25 · 2013: 25 · 2012: 22
FWCI
12.49
Type
journal article
Language
en
Open access
closed
Locations
  • Circulation Research (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • American Heart Association
  • National Institutes of Health
  • National Heart, Lung, and Blood Institute (HL-50560)
Topics
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Fibrosis and Remodeling
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiovascular Function and Risk Factors
Keywords
myosin heavy chain, alpha-myosin heavy chain, beta-myosin heavy chain, heart failure, translational regulation, cardiac contractility, left ventricle, ventricular myocardium, mRNA-protein correlation
MeSH terms
Adolescent, Adult, Cardiac Output, Low, Female, Humans, Male, Middle Aged, Reference Values, RNA, Messenger, Tissue Distribution, Myosin Heavy Chains, Protein Isoforms

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