HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: 287/6/C1725    most recent 00255.2004v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (9) Citing Articles via Google Scholar Google Scholar Articles by Andruchov, O. Articles by Galler, S. Search for Related Content PubMed PubMed Citation Articles by Andruchov, O. Articles by Galler, S.

MUSCLE CELL BIOLOGY AND CELL MOTILITY

Kinetic properties of myosin heavy chain isoforms in mouse skeletal muscle: comparison with rat, rabbit, and human and correlation with amino acid sequence

Department of Cell Biology, University of Salzburg, A-5020 Salzburg, Austria

Submitted 25 May 2004 ; accepted in final form 7 August 2004

Stretch activation kinetics were investigated in skinned mouse skeletal muscle fibers of known myosin heavy chain (MHC) isoform content to assess kinetic properties of different myosin heads while generating force. The time to peak of stretch-induced delayed force increase (t₃) was strongly correlated with MHC isoforms [t₃ given in ms for fiber types containing specified isoforms; means ± SD with n in parentheses: MHCI 680 ± 108 (13), MHCIIa 110.5 ± 10.7 (23), MHCIIx(d) 46.2 ± 5.2 (20), MHCIIb 23.5 ± 3.3 (76)]. This strong correlation suggests different kinetics of force generation of different MHC isoforms in the following order:MHCIIb > MHCIIx(d) > MHCIIa >> MHCI. For rat, rabbit, and human skeletal muscles the same type of correlation was found previously. The kinetics decreases slightly with increasing body mass. Available amino acid sequences were aligned to quantify the structural variability of MHC isoforms of different animal species. The variation in t₃ showed a correlation with the structural variability of specific actin-binding loops (so-called loop 2 and loop 3) of myosin heads (r = 0.74). This suggests that alterations of amino acids in these loops contribute to the different kinetics of myosin heads of various MHC isoforms.

isoform structure-function relationship; stretch activation; muscle mechanics

This article has been cited by other articles:

				W. Herzog, E. J. Lee, and D. E. Rassier Residual force enhancement in skeletal muscle J. Physiol., August 1, 2006; 574(3): 635 - 642. [Abstract] [Full Text] [PDF]

				O. Andruchova, G. M. M. Stephenson, O. Andruchov, D. G. Stephenson, and S. Galler Myosin heavy chain isoform composition and stretch activation kinetics in single fibres of Xenopus laevis iliofibularis muscle J. Physiol., July 1, 2006; 574(1): 307 - 317. [Abstract] [Full Text] [PDF]

				O. Andruchov, O. Andruchova, Y. Wang, and S. Galler Dependence of cross-bridge kinetics on myosin light chain isoforms in rabbit and rat skeletal muscle fibres J. Physiol., February 15, 2006; 571(1): 231 - 242. [Abstract] [Full Text] [PDF]