Stål P, Eriksson P O, Schiaffino S, Butler-Browne G S, Thornell L E
Department of Anatomy, Umeå University, Sweden.
J Muscle Res Cell Motil. 1994 Oct;15(5):517-34. doi: 10.1007/BF00121158.
Immunohistochemistry was used to determine the myosin composition of defined fibre types of three embryologically different adult muscles, the oro-facial, masseter and limb muscles. In addition, the myosin composition in whole muscle specimens was analysed with biochemical methods. Both similarities and differences between muscles in the content of myosin heavy chains and myosin light chains were found. Nevertheless, each muscle had its own distinct identity. Our results indicated the presence of a previously undetected fast myosin heavy chain isoform in the oro-facial type II fibre population, tentatively termed 'fast F'. The masseter contained aberrant myosin isoforms, such as foetal myosin heavy chain and alpha-cardiac myosin heavy chain and unique combinations of myosin heavy chain isoforms which were not found in the limb or oro-facial muscles. The type IM and IIC fibres coexpressed slow and fast A myosin heavy chains in the oro-facial and limb muscles but slow and a fast B like myosin heavy chain in the masseter. While single oro-facial and limb muscle fibres contained one or two myosin heavy chain types, single masseter fibres coexpressed up to four different myosin heavy chain isoforms. Describing the fibres according to their expression of myosin heavy chain isozymes, up to five fibre types could be distinguished in the oro-facial and limb muscles and eight in the masseter. Oro-facial and limb muscles expressed five myosin light chains, MLC1S, MLC2S, MLC1F, MLC2F and MLC3F, and the masseter four, MLC1S, MLC2S, MLC1F, and, in addition, an embryonic myosin light chain, MLC1emb, which is usually not present in normal adult skeletal muscle. These results probably reflect the way the muscles have evolved to meet the specialized functional requirements imposed upon them and are in agreement with the previously proposed concept that jaw and limb muscles belong to two distinct allotypes.
免疫组织化学法用于确定三种胚胎发育不同的成年肌肉(口面部肌肉、咬肌和肢体肌肉)特定纤维类型的肌球蛋白组成。此外,采用生化方法分析了整块肌肉标本中的肌球蛋白组成。发现这些肌肉在肌球蛋白重链和肌球蛋白轻链含量上既有相似之处也有差异。然而,每块肌肉都有其独特的特征。我们的结果表明,在口面部II型纤维群体中存在一种先前未检测到的快速肌球蛋白重链异构体,暂称为“快速F”。咬肌含有异常的肌球蛋白异构体,如胎儿肌球蛋白重链和α-心肌肌球蛋白重链,以及肢体或口面部肌肉中未发现的独特肌球蛋白重链异构体组合。IM型和IIC型纤维在口面部和肢体肌肉中共同表达慢速和快速A肌球蛋白重链,但在咬肌中共同表达慢速和一种类似快速B的肌球蛋白重链。虽然单个口面部和肢体肌肉纤维含有一种或两种肌球蛋白重链类型,但单个咬肌纤维可共同表达多达四种不同的肌球蛋白重链异构体。根据肌球蛋白重链同工酶的表达来描述纤维,在口面部和肢体肌肉中可区分出多达五种纤维类型,在咬肌中可区分出八种。口面部和肢体肌肉表达五种肌球蛋白轻链,即MLC1S、MLC2S、MLC1F、MLC2F和MLC3F,而咬肌表达四种,即MLC1S、MLC2S、MLC1F,此外还表达一种胚胎肌球蛋白轻链MLC1emb,正常成年骨骼肌中通常不存在这种轻链。这些结果可能反映了肌肉为满足其特定功能需求而进化的方式,并且与先前提出的颌部和肢体肌肉属于两种不同异型的概念一致。