Toutant M, Toutant J P, Montarras D, Fiszman M Y
Biochimie. 1983 Nov-Dec;65(11-12):637-42. doi: 10.1016/s0300-9084(84)80027-9.
We investigated the expression of myosin light chains and tropomyosin subunits during chick embryonic development of the anterior (ALD) and posterior (PLD) parts of the latissimus dorsi muscles. As early as day 8 in ovo, both muscles accumulate a common set of myosin light chains (LC) in similar ratios (LC1F: 55 per cent; LC2S: 25 per cent; LC2F: 12 per cent; LC1S: 8 per cent) and a common set of tropomyosin (TM) subunits (beta 2, beta 1, alpha 2F). Later during development, the slow components of the LC regularly disappear in the PLD and the fast components of the LC and the alpha 2FTM disappear in the ALD, so that the adult pattern is almost established at the time of hatching. Thus, early in development, the two muscles accumulate a common set of fast and slow myosin light chains and fast tropomyosin and some isoforms are repressed at a later stage during development. These data might suggest that during development, the regulatory mechanisms of muscle specific isoform expression differ from one contractile protein to another.
我们研究了鸡胚胎发育过程中背阔肌前部（ALD）和后部（PLD）中肌球蛋白轻链和原肌球蛋白亚基的表达情况。早在胚胎发育第8天，这两块肌肉就以相似的比例积累了一组共同的肌球蛋白轻链（LC）（LC1F：55%；LC2S：25%；LC2F：12%；LC1S：8%）和一组共同的原肌球蛋白（TM）亚基（β2、β1、α2F）。在随后的发育过程中，LC的慢成分在PLD中逐渐消失，而LC的快成分和α2F TM在ALD中消失，因此在孵化时几乎已形成成年模式。因此，在发育早期，这两块肌肉积累了一组共同的快、慢肌球蛋白轻链和快原肌球蛋白，并且一些亚型在发育后期被抑制。这些数据可能表明，在发育过程中，肌肉特异性亚型表达的调控机制因收缩蛋白的不同而有所差异。
