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.

doi:10.1023/a:1018613907574

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

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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

DOI 10.1023/a:1018613907574

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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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Molecular studies indicate reduced actomyosin motility, which would impose an energetic drag on normal myosin during contraction.
“Such an increased energetic cost of contraction with the Arg403Gln mutation in the intact mouse heart3 is thought to be consistent with several molecular studies suggesting a decrease in actomyosin motility20,21 that effectively puts an energetic “drag” on the wild-type myosin during shortening3,19,22.”
From iRhythm ZIO: The Diagnostic Yield of a 14-day Continuous Ambulatory ECG Monitor (Turakhia et al., diagnostic yield of extended ambulatory ECG monitoring) (2013) · cites this paper as [20]

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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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Authors: CUDA, G., FANANAPAZIR, L., EPSTEIN, N. D., & SELLERS, J. R.
Affiliations: National Institutes of Health (US)
ORCID: CUDA, GIOVANNI
SELLERS, JAMES R.
Venue: Journal of Muscle Research & Cell Motility
Publisher: Springer Science and Business Media LLC
Published: 1997-05
Volume: 18
Issue: 3
Pages: 275-283
ISSN: 0142-4319 (ISSN-L)
1573-2657
DOI: 10.1023/a:1018613907574
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
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
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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The in vitro motility activity of β-cardiac myosin depends on the nature of the β-myosin heavy chain gene mutation in hypertrophic cardiomyopathy

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