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Am J Physiol Cell Physiol (August 11, 2004). doi:10.1152/ajpcell.00255.2004
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Submitted on May 25, 2004
Accepted on August 7, 2004

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

Oleg Andruchov1, Olena Andruchova1, Yishu Wang1, and Stefan Galler1*

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

* To whom correspondence should be addressed. E-mail: Stefan.Galler{at}sbg.ac.at.

Stretch activation kinetics were investigated on skinned mouse skeletal muscle fibers of known myosin heavy chain isoform (MHC) content in order 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 the MHC isoforms (t3 given in ms for fiber types containing specified isoforms, mean±SD (n): MHCI: 680±108 (18), 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 has previously been found. The kinetics slightly decreases 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 are contributing to the different kinetics of myosin heads of various MHC isoforms.




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