Journal article
Influence of myosin isoforms on contractile properties of intact muscle fibers from Rana pipiens
American Journal of Physiology: Cell Physiology, v 282(4), pp C835-C844
01 Apr 2002
PMID: 11880272
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The myosin heavy chain (MHC) and myosin light chain (MLC) isoforms in skeletal muscle of Rana pipiens have been well characterized. We measured the force-velocity (F- V) properties of single intact fast-twitch fibers from R. pipiens that contained MHC types 1 or 2 (MHC1 or MHC2) or coexpressed MHC1 and MHC2 isoforms. Velocities were measured between two surface markers that spanned most of the fiber length. MHC and MLC isoform content was quantified after mechanics analysis by SDS-PAGE. Maximal shortening velocity ( V
max
) and velocity at half-maximal tension ( V
P 50
) increased with percentage of MHC1 (%MHC1). Maximal specific tension (P
o
/CSA, where P
o
is isometric tension and CSA is fiber cross-sectional area) and maximal mechanical power ( W
max
) also increased with %MHC1. MHC concentration was not significantly correlated with %MHC1, indicating that the influence of %MHC1 on P
o
/CSA and W
max
was due to intrinsic differences between MHC isoforms and not to concentration. The MLC3-to-MLC1 ratio was not significantly correlated with V
max
, V
P 50
, P
o
/CSA, or W
max
. These data demonstrate the powerful relationship between MHC isoforms and F- V properties of the two most common R. pipiensfiber types.
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Details
- Title
- Influence of myosin isoforms on contractile properties of intact muscle fibers from Rana pipiens
- Creators
- Gordon J. Lutz - Veterans Medical Research Foundation of San DiegoShashank R. Sirsi - Veterans Medical Research Foundation of San DiegoSarah A. Shapard-Palmer - Veterans Medical Research Foundation of San DiegoShannon N. Bremner - Veterans Medical Research Foundation of San DiegoRichard L. Lieber - Veterans Medical Research Foundation of San Diego
- Publication Details
- American Journal of Physiology: Cell Physiology, v 282(4), pp C835-C844
- Publisher
- American Physiological Society (APS)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000174231300020
- Scopus ID
- 2-s2.0-0036083931
- Other Identifier
- 991021463709204721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Cell Biology
- Physiology