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Articles in PresS, published online ahead of print December 5, 2001
Am J Physiol Cell Physiol, 10.1152/ajpcell.00482.2001
Submitted on October 10, 2001
Accepted on November 14, 2001
1 Orthopaedics, University of California San Diego, San Diego, CA, USA; Veterans Medical Research Foundation, San Diego, CA, USA
2 Bioengineering, University of California San Diego, San Diego, CA, USA
3 Veterans Medical Research Foundation, San Diego, CA, USA
4 Veterans Affairs Medical Center, San Diego, CA, USA
5 Orthopaedics, University of California San Diego, San Diego, CA, USA; Veterans Affairs Medical Center, San Diego, CA, USA; Bioengineering, University of California San Diego, San Diego, CA, USA
* To whom correspondence should be addressed. E-mail: glutz{at}ucsd.edu.
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 MHC1, MHC2 or co-expressed both MHC1 and MHC2 isoforms. Velocities were measured between two surface markers that spanned 78% of the fiber length. MHC and MLC isoforms were measured after mechanics by SDS-PAGE. Maximal shortening velocity (Vmax), and velocity at half maximal tension (VP50) both increased with percentage of type 1 MHC (%MHC1). Maximal specific tension (Po/CSA) and maximal mechanical power (Wmax) also increased with %MHC1. MHC concentration was not significantly correlated with %MHC1, indicating that the influence of %MHC1 on Po/CSA and Wmax was due to intrinsic differences between MHC isoforms and not to concentration. MLC3/MLC1 ratio was not significantly correlated with Vmax, VP50, Po/CSA or Wmax. These data demonstrate the powerful relationship between MHC isoforms and F-V properties of the most common R. pipiens fiber types.
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