MHC and sarcoplasmic reticulum protein isoforms in functionally overloaded cat plantaris muscle fibers.
To determine whether the adaptations in myosin heavy chain (MHC) isoform expression after functional overload (FO) are accompanied by commensurate adaptations in protein isoforms responsible for relaxation [sarco(endo)plasmic reticulum (SR) Ca(2+)-adenosinetriphosphatase (SERCA) and phospholamban (PHL)] in single muscle fibers, the isoforms of MHC and SERCA and the presence or absence of PHL were determined for cat plantaris fibers 3 mo after FO. In control plantaris the relative MHC isoform composition was 23% type I, 21% type IIa, and 56% type IIb. FO resulted in a shift toward slower isoforms (33% type I, 44% type IIa, and 23% type IIb). In the deep region of the plantaris the proportions of type I MHC and hybrid MHC fibers (containing type I and II MHCs) were 40 and 200% greater in FO cats, respectively. FO resulted in a 47% increase in the proportion of fibers containing only the slow SERCA isoform (SERCA2) and a 41% increase in the proportion of fibers containing PHL. The proportions of fibers containing type I MHC, SERCA2, and PHL in control and FO plantaris were linearly correlated. These data show that adaptations in MHC isoform expression are accompanied by commensurate adaptations in sarcoplasmic reticulum protein isoforms in single muscle fibers after FO.
Talmadge
R J
RJ
Department of Physiological Science, University of California, Los Angeles 90095-1527, USA.
Roy
R R
RR
Chalmers
G R
GR
Edgerton
V R
VR
D000818:Animals; D002415:Cats; D005260:Female; D007150:Immunohistochemistry; D018485:Muscle Fibers, Skeletal / Q000648:ultrastructure*; D018482:Muscle, Skeletal / Q000378:metabolism*; D018995:Myosin Heavy Chains / Q000378:metabolism*; D012519:Sarcoplasmic Reticulum / Q000648:ultrastructure*
D018995:Myosin Heavy Chains