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J Appl Physiol 81: 2540-2546, 1996;
8750-7587/96 $5.00
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Journal of Applied Physiology
Vol. 81, No. 6, pp. 2540-2546, December 1996
EXERCISE AND MUSCLE

Distribution of myosin heavy chain isoforms in non-weight-bearing rat soleus muscle fibers

Robert J. Talmadge, Roland R. Roy, and V. Reggie Edgerton

Department of Physiological Science and Brain Research Institute, University of California, Los Angeles, California 90095-1527

Received 11 March 1996; accepted in final form 14 August 1996.

Talmadge, Robert J., Roland R. Roy, and V. Reggie Edgerton. Distribution of myosin heavy chain isoforms in non-weight-bearing rat soleus muscle fibers. J. Appl. Physiol. 81(6): 2540-2546, 1996.---The effects of 14 days of spaceflight (SF) or hindlimb suspension (HS) (Cosmos 2044) on myosin heavy chain (MHC) isoform content of the rat soleus muscle and single muscle fibers were determined. On the basis of electrophoretic analyses, there was a de novo synthesis of type IIx MHC but no change in either type I or IIa MHC isoform proportions after either SF or HS compared with controls. The percentage of fibers containing only type I MHC decreased by 26 and 23%, and the percentage of fibers with multiple MHCs increased from 6% in controls to 32% in HS and 34% in SF rats. Type IIx MHC was always found in combination with another MHC or combination of MHCs; i.e., no fibers contained type IIx MHC exclusively. These data suggest that the expression of the normal complement of MHC isoforms in the adult rat soleus muscle is dependent, in part, on normal weight bearing and that the absence of weight bearing induces a shift toward type IIx MHC protein expression in the preexisting type I and IIa fibers of the soleus.

contractile proteins; fiber type; gravity; hindlimb suspension; spaceflight


0161-7567/96 $5.00 Copyright © 1996 the American Physiological Society




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