Hilber K, Galler S, Gohlsch B, Pette D
Institute of Zoology, University of Salzburg, Austria.
FEBS Lett. 1999 Jul 23;455(3):267-70. doi: 10.1016/s0014-5793(99)00903-5.
The head portion of the myosin heavy chain is essential in force generation. As previously shown, Ca2+-activated muscle fibers from rat and rabbit display a strong correlation between their myosin heavy chain isoform composition and the kinetics of stretch activation, corresponding to an order of velocity: myosin heavy chain Ib > myosin heavy chain IId(x) > myosin heavy chain IIa >> myosin heavy chain I. Here, we show a similar correlation for human muscle fibers (myosin heavy chain IIb > myosin heavy chain IIa >> myosin heavy chain I), suggesting isoform-specific differences between the kinetics of force-generating power strokes. The kinetics of myosin heavy chain I are similar in human and rodents. This holds also true for myosin heavy chain IIa, but human myosin heavy chain IIb is slower than rodent myosin heavy chain IIb. It is similar to rodent myosin heavy chain IId(x).
肌球蛋白重链的头部对于产生力量至关重要。如先前所示,大鼠和兔子的钙激活肌肉纤维在其肌球蛋白重链异构体组成与拉伸激活动力学之间显示出强烈的相关性,对应于速度顺序:肌球蛋白重链Ib > 肌球蛋白重链IId(x) > 肌球蛋白重链IIa >> 肌球蛋白重链I。在此,我们展示了人类肌肉纤维的类似相关性(肌球蛋白重链IIb > 肌球蛋白重链IIa >> 肌球蛋白重链I),这表明在产生力量的动力冲程动力学方面存在异构体特异性差异。人类和啮齿动物的肌球蛋白重链I的动力学相似。肌球蛋白重链IIa也是如此,但人类的肌球蛋白重链IIb比啮齿动物的肌球蛋白重链IIb慢。它与啮齿动物的肌球蛋白重链IId(x)相似。