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Cited by 380Cardiomyopathy and Myosin StudiesMuscle Physiology and DisordersMeat and Animal Product Quality

The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.

Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition.

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Reiser, P J, Moss, R L, Giulian, G G, Greaser, M L·1985·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(17)39330-4
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Abstract

Extensive variations exist in the heavy and light chain components of myosin in vertebrate striated muscles. In the present study, we have characterized a specific contractile property, velocity of shortening, and protein subunit composition of single fibers from adult rabbit soleus muscles. Maximum velocity of shortening (Vmax) was measured using the slack test method, and the myosin composition of these same fibers was determined using an ultrasensitive sodium dodecyl sulfate-polyacrylamide gel electrophoresis system. While most fibers were found to have velocities between 0.5 and 1.0 muscle length/s, several had velocities distributed between 1.33 and 2.99 muscle length/s. The fibers in the slower group had myosin subunits that were solely of the slow type; however, those in the faster group contained both fast and slow heavy chains and light chains. The velocity of shortening measured in fibers having both myosin types was highly correlated with the myosin heavy chain composition, with velocity increasing as the proportion of fast-type heavy chain increased. Variations in light chain composition, particularly fast and slow myosin light chain 1, appeared to occur independently of the variations in heavy chain composition, suggesting that some myosin molecules consist of mixtures of slow- and fast-type subunits.

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Crossref · 10.1016/s0021-9258(17)39330-4

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Research works printed but not linked: 3

  1. Fabiato, 1979, J. Physiol (Paris), 75, 463
  2. Greaser, 1985, Biophys. J., 47, 23a
  3. Martell, 1974, Vol. 1, xi

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Metadata

Authors
Reiser, P. J., Moss, R. L., Giulian, G. G., & Greaser, M. L.
Affiliations
University of Wisconsin–Madison (US)
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1985-08
Volume
260
Issue
16
Pages
9077-9080
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(17)39330-4
OpenAlex
W2137128469
Cited by
380
References
26
Citations by year
2026: 2 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 8 · 2020: 2 · 2019: 2 · 2018: 3 · 2017: 2 · 2016: 4 · 2015: 7 · 2014: 7 · 2013: 7 · 2012: 6
FWCI
8.67
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01am031806-03)
  • National Heart, Lung, and Blood Institute (HL-25861)
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
  • Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
Keywords
myosin heavy chain, myosin light chain, myosin light chain 1, soleus muscle, rabbit skeletal muscle, muscle fiber heterogeneity
MeSH terms
Animals, Electrophoresis, Polyacrylamide Gel, Kinetics, Molecular Weight, Muscle Contraction, Muscles, Myosins, Rabbits

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