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首页> 美国卫生研究院文献>The Journal of Biophysical and Biochemical Cytology >Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits
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Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits

机译：小鸡肌源性抗原。二。由大的二硫键连接的亚基组成的新型细胞外糖蛋白复合物

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This report describes the biochemical characterization of a novel extracellular matrix component, " myotendinous antigen," which appears early in chick limb morphogenesis at sites connecting developing muscle fibers, tendons, and bone ( Chiquet , M., and D. Fambrough , 1984; J. Cell Biol., 98:1926-1936). This extracellular matrix antigen is a major component of the secretory proteins released into the medium by fibroblast and muscle cultures; the soluble form is characterized here. This form of myotendinous antigen is a large glycoprotein complex consisting of several disulfide linked subunits (Mr approximately 150,000-240,000). The differently sized antigen subunits are related, since they yielded very similar proteolytic cleavage patterns. M1 antibody can bind to the denatured subunits. The antigen subunits, as well as a Mr approximately 80,000 pepsin-resistant antigenic domain derived from them, are resistant to bacterial collagenase. Despite possessing subunits similar in size to fibronectin, myotendinous antigen appears to be both structurally and antigenically unrelated to fibronectin or to other known extracellular matrix components. About seven times more M1 antigen per cell nucleus was released into the medium in fibroblast as compared to muscle cultures. In muscle conditioned medium, myotendinous antigen is noncovalently complexed to very high molecular weight material that could be heavily labeled by [3H]glucosamine and [35S]sulfate. This material is sensitive to chondroitinase ABC and hence appears to contain sulfated glycosaminoglycans. We speculate that myotendinous antigen might interact with proteoglycans on the surface of muscle fibers, thereby acting as a link to tendons.
机译：这份报告描述了一种新型的细胞外基质成分“肌源性抗原”的生化特性，这种成分在鸡肢形态发生的早期出现在连接发育中的肌肉纤维，肌腱和骨骼的部位（Chiquet，M。和D. Fambrough，1984； J （Cell Biol。，98：1926-1936）。这种细胞外基质抗原是成纤维细胞和肌肉培养物释放到培养基中的分泌蛋白的主要成分。可溶形式在此表征。肌腱抗原的这种形式是一种大型的糖蛋白复合物，由几个二硫键连接的亚基组成（Mr约为150,000-240,000）。不同大小的抗原亚基是相关的，因为它们产生非常相似的蛋白水解切割模式。 M1抗体可以结合变性的亚基。抗原亚基以及衍生自它们的大约80,000胃蛋白酶抗性的抗原结构域对细菌胶原酶具有抗性。尽管拥有大小与纤连蛋白相似的亚基，但肌腱抗原似乎在结构和抗原上均与纤连蛋白或其他已知的细胞外基质成分无关。与肌肉培养相比，成纤维细胞释放到培养基中的每个细胞核的M1抗原多约7倍。在肌肉条件培养基中，肌腱抗原非共价复合至非常高分子量的物质，该物质可能会被[3H]氨基葡萄糖和[35S]硫酸盐严重标记。该物质对软骨素酶ABC敏感，因此似乎含有硫酸化的糖胺聚糖。我们推测肌腱抗原可能与肌纤维表面的蛋白聚糖相互作用，从而充当与肌腱的链接。

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