Rosser B W, Wick M, Waldbillig D M, Bandman E
University of Saskatchewan, College of Medicine, Department of Anatomy and Cell Biology, Saskatoon, Canada.
Biochem Cell Biol. 1996;74(5):715-28. doi: 10.1139/o96-078.
The aims of this study are to investigate the diversity of myosin heavy-chain (MyHC) expression among avian fast-twitch fibers, and to test the hypothesis that dissimilar MyHC isoforms are found in each of the principal avian fast-twitch fiber types. MyHCs within the muscle fibers of the pectoralis of 31 species of bird are characterized using immunocytochemical methods. A library of 11 monoclonal antibodies previously produced against chicken MyHCs is used. The specificity of these antibodies for MyHCs in each of the muscles studied is confirmed by Western blots. The results show that avian fast-twitch glycolytic fibers and fast-twitch oxidative-glycolytic fibers can contain different MyHCs. Among the species studied, there is also a conspicuous variety of MyHC isoforms expressed. In addition, the results suggest that two epitopes are restricted to chickens and closely allied gallinaceous birds. There are no apparent correlations between between MyHC epitope and presupposed contractile properties. However, the presence of different isoforms in different fast-twitch fiber types suggests a correlation between isoform and contractile function.
本研究的目的是调查鸟类快肌纤维中肌球蛋白重链（MyHC）表达的多样性，并检验在鸟类主要快肌纤维类型中均存在不同MyHC亚型的假设。运用免疫细胞化学方法对31种鸟类胸肌纤维中的MyHC进行表征。使用了一个先前针对鸡MyHC产生的11种单克隆抗体文库。通过蛋白质免疫印迹法证实了这些抗体对所研究的每块肌肉中MyHC的特异性。结果表明，鸟类快肌糖酵解纤维和快肌氧化糖酵解纤维可能含有不同的MyHC。在所研究的物种中，表达的MyHC亚型也存在显著差异。此外，结果表明有两个表位仅限于鸡和与之亲缘关系密切的雉科鸟类。MyHC表位与预先假定的收缩特性之间没有明显的相关性。然而，不同快肌纤维类型中存在不同的亚型表明亚型与收缩功能之间存在相关性。
