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首页> 外文期刊>Journal of cell biology >Tenascin-Y: a protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue.
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Tenascin-Y: a protein of novel domain structure is secreted by differentiated fibroblasts of muscle connective tissue.

机译：Tenascin-Y：一种新的结构域结构蛋白是由肌肉结缔组织的分化成纤维细胞分泌的。

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Tenascin-Y was identified in chicken as a novel member of the tenascin (TN) family of ECM proteins. Like TN-C, TN-R, and TN-X, TN-Y is a multidomain protein consisting of heptad repeats, epidermal growth factor-like repeats, fibronectin type III-like (FNIII) domains and a domain homologous to fibrinogen. In contrast to all other known TNs, the series of FNIII domains is interrupted by a novel domain, rich in serines (S) and prolines (P) that occur as repeated S-P-X-motifs, where X stands for any amino acid. Interestingly, the TN-Y-type FNIII domains are 70-100% identical with respect to their DNA sequence. Different TN-Y variants are created by alternative splicing of FNIII domains. Although, based on sequence comparisons TN-Y is most similar to mammalian TN-X, these molecules are not species homologues. TN-Y is predominantly expressed in embryonic and adult chicken heart and skeletal muscle and, to a lower extent, also in several non-muscular tissues. Two major transcripts of approximately 6.5 and 9.5 kb are differentially expressed during heart and skeletal muscle development and are also present in the adult. Anti-TN-Y antibodies recognize a approximately 400-kD double band and a approximately 300-kD form of TN-Y on immunoblots of chicken heart extracts. In situ hybridization and immunofluorescence analysis of aortic smooth muscle, heart, and skeletal muscle revealed that TN-Y is mainly expressed and secreted by cells within muscle-associated connective tissue. Cultured primary muscle fibroblasts released a approximately 220-kD doublet and a approximately 170-kD single TN-Y variant only when cultured in 10% horse serum but not in medium containing 10% fetal calf serum. All TN-Y variants isolated bind to heparin under physiologically relevant conditions that may indicate an important function retained in all tenascins.
机译：Tenascin-Y在鸡中被鉴定为ECM蛋白Tenascin（TN）家族的新成员。像TN-C，TN-R和TN-X一样，TN-Y是一种多域蛋白，由七肽重复序列，表皮生长因子样重复序列，纤连蛋白III型（FNIII）域和与纤维蛋白原同源的域组成。与所有其他已知的TN相比，这一系列的FNIII结构域被一个富含丝氨酸（S）和脯氨酸（P）的新颖结构域中断，这些结构域以重复的S-P-X-基序出现，其中X代表任何氨基酸。有趣的是，TN-Y型FNIII结构域的DNA序列具有70-100％的同一性。通过TNIII域的可变剪接产生不同的TN-Y变体。尽管基于序列比较，TN-Y与哺乳动物TN-X最相似，但这些分子不是物种同源物。 TN-Y主要在胚胎和成年鸡的心脏和骨骼肌中表达，并在较低的程度上在几种非肌肉组织中表达。在心脏和骨骼肌发育过程中，约有6.5和9.5 kb的两个主要转录本差异表达，它们也存在于成年人中。抗TN-Y抗体在鸡心提取物的免疫印迹上识别大约400 kD的双条带和大约300 kD的TN-Y形式。对主动脉平滑肌，心脏和骨骼肌的原位杂交和免疫荧光分析表明，TN-Y主要由与肌肉相关的结缔组织内的细胞表达和分泌。仅当在10％的马血清中培养而不在含有10％胎牛血清的培养基中培养时，培养的原代肌成纤维细胞才会释放出约220 kD的双态和约170 kD的单个TN-Y变体。在生理相关条件下，分离出的所有TN-Y变体均与肝素结合，这可能表明所有腱糖蛋白均具有重要功能。

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