Time course adaptations in rat skeletal muscle isomyosins during compensatory growth and regression.
Time course adaptations in rat skeletal muscle isomyosins during compensatory growth and regression.
复制标题
大鼠骨骼肌同肌球蛋白在代偿性生长和退化过程中的时程适应。
DOI:
10.1152/jappl.1987.63.5.2111
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发表时间:
1987
期刊:
影响因子:
--
通讯作者:
Baldwin,KM
中科院分区:
文献类型:
--
作者:
Tsika,RW;Herrick,RE;Baldwin,KM
The purpose of this study was to ascertain the time course of change during both compensatory growth (hypertrophy) and subsequent growth regression on myosin isoform expression in rodent fast-twitch plantaris muscle in response to functional overload (induced by removal of synergists). Peak hypertrophy of the plantaris muscle (92%) occurred after 9 wk of overload. After 7 wk of overload regression (induced by a model of hindlimb unweighting), muscle weight returned to within 30% of control values. Myofibril protein content (mg/g muscle) remained relatively constant throughout the overload period but became significantly depressed relative to control values after 7 wk of regression. However, when expressed on a per muscle basis (mg/muscle) no differences existed at this time point (t = 7 wk regression). The distribution of native myosin isoforms in the myofibril protein pool of the overloaded plantaris muscle reflected a progressive increase (23% at t = 9 wk; P less than 0.001) in the relative proportion of slow myosin (Sm). This change was also accompanied by increases in intermediate myosin (Im) as well as the repression of the fast myosin one (Fm1) isoform (P less than 0.001). These shifts in Sm and Fm1 isoform expression were gradually reversed during the regression period, whereas Im remained elevated relative to control values. These adaptive changes in myosin isoform expression during both hypertrophy and regression were further supported by concomitant shifts in both myosin adenosinetriphosphatase (ATPase) activity (decreased during overload) and slow myosin light chain (SLC) expression. However, during regression the changes in myosin isoform expression and myosin ATPase were not as synchronous as they were during overload. Estimation of the mixed myosin heavy chain (MHC) half-life (t 1/2), using a linear model that assumes zero-order synthesis and first-order degradation kinetics, revealed t 1/2 values of approximately 19 and 10 days for the overload and regression periods, respectively. Collectively these data suggest that 1) skeletal muscle myosin isoforms and corresponding ATPase activity are in a dynamic state of change, although not completely synchronous, in response to altered muscle stress, and 2) the kinetics of change in the mixed MHC protein pool are slower during compensatory growth compared with regression of growth.
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影响因子:
3.9
作者:
J. Potter
通讯作者:
J. Potter
DOI:
--
发表时间:
1984
期刊:
European Journal of Biochemistry
影响因子:
--
作者:
G. Maréchal;K. Schwartz;G. Beckers;E. Ghins
通讯作者:
E. Ghins
DOI:
10.1152/jappl.1985.59.2.639
发表时间:
1985
期刊:
Journal of applied physiology (Bethesda, Md. : 1985)
影响因子:
--
作者:
Roy,RR;Baldwin,KM;Martin,TP;Chimarusti,SP;Edgerton,VR
通讯作者:
Edgerton,VR
DOI:
--
发表时间:
1983
期刊:
Journal of Physiology
影响因子:
--
作者:
R. Fitzsimons;J. Hoh
通讯作者:
J. Hoh
影响因子:
4.1
作者:
J. Hoh;P. A. McGrath;R. White
通讯作者:
R. White