Jf. Watchko et al., MYOSIN HEAVY-CHAIN TRANSITIONS DURING DEVELOPMENT FUNCTIONAL IMPLICATIONS FOR THE RESPIRATORY MUSCULATURE, Comparative biochemistry and physiology. B. Comparative biochemistry, 119(3), 1998, pp. 459-470
The myosin heavy chain (MHC) exists as multiple isoforms that are enco
ded for by a family of genes. The respiratory musculature demonstrates
muscle-specific and temporally-dependent changes in MHC isoform expre
ssion during maturation. Developmental expression of MHC isoforms corr
elate well with postnatal changes in actomyosin ATPase activity, speci
fic force generation (P(0/)CSA), maximum unloaded velocity of shorteni
ng (V-0), and fatigue resistance. More specifically, as the expression
of MHCneonatal declines and MHC2A, MHC2X, and MHC2B increase, actomyo
sin ATPase activity, P-0/CSA, V-0, and muscle fatigability increase. T
he increase in actomyosin ATPase activity with maturation is partially
offset by a postnatal increase in oxidative capacity; however, as fat
igue resistance declines with development it is apparent that the ener
gy costs of contraction are not fully matched by an increase in energy
production. Developmental transitions in smooth muscle MHC phenotype
also occur although their functional importance remains unclear. (C) 1
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