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.
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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:
Journal of applied physiology (Bethesda, Md. : 1985)
影响因子:
--
通讯作者:
Baldwin,KM
Baldwin,KM
中科院分区:
--
文献类型:
--
作者:
Tsika,RW;Herrick,RE;Baldwin,KM

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本研究的目的是确定啮齿动物快速收缩跖肌中肌球蛋白异构体表达在代偿性生长(肥大)和随后的生长回归期间的时间变化过程,以响应功能过载(由增效剂去除引起)。足底肌肥大高峰(92%)发生在过载9周后。经过7周的负荷回归(由后肢减重模型诱导),肌肉重量恢复到控制值的30%以内。肌原纤维蛋白含量(mg/g肌肉)在过载期间保持相对稳定,但在回归7周后相对于对照组显著降低。然而,当以每块肌肉为基础(mg/肌肉)表达时,在这个时间点没有差异(t = 7周回归)。超载的足底肌肌原纤维蛋白库中天然肌球蛋白同型体的分布反映了慢速肌球蛋白(Sm)相对比例的渐进式增加(t = 9周时为23%,P < 0.001)。这种变化还伴随着中间肌球蛋白(Im)的增加以及快速肌球蛋白1 (Fm1)亚型的抑制(P < 0.001)。Sm和Fm1亚型表达的这些变化在回归期间逐渐逆转,而Im相对于控制值仍然升高。肌球蛋白三磷酸腺苷酶(ATPase)活性(在过载时降低)和肌球蛋白轻链(SLC)表达缓慢的变化进一步支持了肌球蛋白异构体在肥大和退化期间表达的适应性变化。然而,在回归过程中,肌凝蛋白异型表达和肌凝蛋白atp酶的变化并不像过载时那样同步。混合肌球蛋白重链(MHC)半衰期(t1 /2),使用假设零级合成和一级降解动力学的线性模型估计,显示过载和回归期的t1 /2值分别约为19天和10天。综上所述,这些数据表明:1)骨骼肌肌球蛋白亚型和相应的atp酶活性处于动态变化状态,尽管不是完全同步的,以响应肌肉应激的改变;2)混合MHC蛋白池的变化动力学在代偿生长期间比生长回归期间更慢。
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.
兔骨骼肌肌原纤维中肌钙蛋白、原肌球蛋白、肌动蛋白和肌球蛋白的含量。
DOI: --
发表时间: 1974
影响因子: 3.9
作者:
J. Potter
通讯作者: J. Potter
大鼠肌肉生长和再生中的肌球蛋白同工酶。
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
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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
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正常和营养不良小鼠快肌和慢肌中的肌球蛋白同工酶。
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
对雏鸡快肌和慢肌中多种形式的肌球蛋白进行电泳分析。
DOI: --
发表时间: 1976
影响因子: 4.1
作者:
J. Hoh;P. A. McGrath;R. White
通讯作者: R. White