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.
Open accessAbstract
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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“Functionally, MyHC isoform expression directly affects muscle fiber-type contractile velocity via myosin ATPase activity (74), with relative velocities of I < IIA < IIX < IIB (73, 74).”
From Sex-Based Differences in Skeletal Muscle Kinetics and Fiber-Type Composition (2015) · cites this paper as [73]
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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)
- 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
- hybrid
- doi.org
- 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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