Rj. Talmadge et al., MHC AND SARCOPLASMIC-RETICULUM PROTEIN ISOFORMS IN FUNCTIONALLY OVERLOADED CAT PLANTARIS MUSCLE-FIBERS, Journal of applied physiology, 80(4), 1996, pp. 1296-1303
To determine whether the adaptations in myosin heavy chain (MHC) isofo
rm expression after functional overload (FO) are accompanied by commen
surate adaptations in protein isoforms responsible for relaxation [sar
co(endo)plasmic reticulum (SR) Ca2+-adenosinetriphosphatase (SERCA) an
d phospholamban (PHL)] in single muscle fibers, the isoforms of MHC an
d SERCA and the presence or absence of PHL were determined for eat pla
ntaris fibers 3 mo after FO. In control plantaris the relative MHC iso
form composition was 23% type I, 21% type IIa, and 56% type IIb. FO re
sulted in a shift toward slower isoforms (33% type I, 44% type IIa, an
d 23% type IIb). In the deep region of the plantaris the proportions o
f type I MHC and hybrid MHC fibers (containing type I and II MHCs) wer
e 40 and 200% greater in FO cats, respectively. FO resulted in a 47% i
ncrease in the proportion of fibers containing only the slow SERCA iso
form (SERCA2) and a 41% increase in the proportion of fibers containin
g PHL. The proportions of fibers containing type I MHC, SERCA2, and PH
L in control and FO plantaris were linearly correlated. These data sho
w that adaptations in MHC isoform expression are accompanied by commen
surate adaptations in sarcoplasmic reticulum protein isoforms in singl
e muscle fibers after FO.