Cited by 138Cardiomyopathy and Myosin StudiesMuscle Physiology and DisordersCardiac electrophysiology and arrhythmias

The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.

The in vitro motility activity of β-cardiac myosin depends on the nature of the β-myosin heavy chain gene mutation in hypertrophic cardiomyopathy

CUDA, GIOVANNI, FANANAPAZIR, LAMEH, EPSTEIN, NEAL D., SELLERS, JAMES R.·1997·Journal of Muscle Research & Cell Motility

Abstract

Several mutations in the beta-myosin heavy chain gene cause hypertrophic cardiomyopathy. This study investigates (1) the in vitro velocities of translocation of fluorescently-labelled actin by beta-myosin purified from soleus muscle of 30 hypertrophic cardiomyopathy patients with seven distinct beta-myosin heavy chain gene mutations: Thr124Ile, Tyr162Cys, Gly256Glu, Arg403Gln, Val606Met, Arg870His, and Leu908Val mutations; and (2) motility activity of beta-myosin purified from cardiac and soleus muscle biopsies in the same patients. The velocity of translocation of actin by beta-myosin purified from soleus or cardiac muscle of 22 normal controls was 0.48 +/- 0.09 micron s-1. By comparison, the motility activity was reduced in all 30 patients with beta-myosin heavy chain gene mutations (range, 0.112 +/- 0.041 to 0.292 +/- 0.066 micron s-1. Notably, the Tyr162Cys and Arg403Gln mutations demonstrated significantly lower actin sliding velocities: 0.123 +/- 0.044, and 0.112 +/- 0.041 micron s-1, respectively. beta-myosin purified from soleus muscle from four patients with the Arg403Gln mutation had a similar actomyosin motility activity compared to beta-myosin purified from their cardiac biopsies (0.127 +/- 0.045 micron s-1 versus 0.119 +/- 0.068 micron s-1, respectively). Since these seven mutations lie in several distinct functional domains, it is likely that the mechanisms of their inhibitions of motility are different.

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Crossref · 10.1023/a:1018613907574

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  1. FANANAPAZIR, L., MCAREAVEY, D. & EPSTEIN, N. D. (1994) Hypertrophic cardiomyopathy. In Electrophysiology, From Cell to Bedside (edited by ZIPES, D. & JALIFE, J. ) pp. 769–79. Philadelphia: W. B. Saunders Co.

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Metadata

Authors
CUDA, G., FANANAPAZIR, L., EPSTEIN, N. D., & SELLERS, J. R.
Affiliations
National Institutes of Health (US)
Venue
Journal of Muscle Research & Cell Motility
Published
1997-05
Volume
18
Issue
3
Pages
275-283
ISSN
  • 0142-4319 (ISSN-L)
  • 1573-2657
OpenAlex
W383489959
Cited by
137
References
39
Citations by year
2025: 1 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 6 · 2020: 2 · 2019: 6 · 2018: 2 · 2017: 5 · 2016: 2 · 2015: 3 · 2014: 2 · 2013: 6 · 2012: 2
FWCI
7.04
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Muscle Research and Cell Motility (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
Keywords
hypertrophic cardiomyopathy, beta-myosin heavy chain, myosin mutations, actomyosin motility, soleus muscle, myocardium, cardiac contractility
MeSH terms
Actins, Cardiomyopathy, Hypertrophic, Humans, Models, Biological, Myocardium, Myosins, Muscle, Skeletal, Myosin Heavy Chains

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