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肌腱蛋白-C的结构与功能分析

Analysis of structure and function of tenascin-C.

作者信息

Pas Jakub, Wyszko Eliza, Rolle Katarzyna, Rychlewski Leszek, Nowak Stanisław, Zukiel Ryszard, Barciszewski Jan

机构信息

Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12, 61-704 Poznan, Poland.

出版信息

Int J Biochem Cell Biol. 2006;38(9):1594-602. doi: 10.1016/j.biocel.2006.03.017. Epub 2006 Apr 18.

DOI:10.1016/j.biocel.2006.03.017
PMID:16698307
Abstract

Tenascin-C is a multidomain large extracellular matrix glycoprotein composed of six monomers. The size of tenascin-C monomers (180-250 kDa) varies as a result of an alternative splicing of the fibronectin repeats at the pre-mRNA level. For the first time we applied bioinformatic and molecular modeling procedures, for detailed analysis of the organization of tenascin-C and we performed bioinformatic analysis of tenascin-C gene. We detected the presence of heat shock protein 33 in the tenascin-C N-terminal domain that may suggest its role in the protein-protein interactions and stress response. The number of fibronectin type III-like repeats and epidermal growth factor-like repeats were corrected to 15 and 14, respectively. Using polyactylamide gel electophoresis, RT/PCR analysis and microarrays data, we showed the higher level of tenascin-C in the human tumor tissues: brain, intestine and breast. These results suggested a new role of tenascin-C as the potential tumor marker and drug target.

摘要

腱生蛋白-C是一种由六个单体组成的多结构域大型细胞外基质糖蛋白。由于在mRNA前体水平上纤连蛋白重复序列的可变剪接,腱生蛋白-C单体的大小(180 - 250 kDa)会有所不同。我们首次应用生物信息学和分子建模程序,对腱生蛋白-C的结构组织进行详细分析,并对腱生蛋白-C基因进行了生物信息学分析。我们在腱生蛋白-C的N端结构域中检测到热休克蛋白33的存在,这可能表明其在蛋白质-蛋白质相互作用和应激反应中的作用。III型纤连蛋白样重复序列和表皮生长因子样重复序列的数量分别校正为15个和14个。通过聚丙烯酰胺凝胶电泳、RT/PCR分析和微阵列数据,我们发现人类肿瘤组织(脑、肠和乳腺)中腱生蛋白-C的水平较高。这些结果表明腱生蛋白-C作为潜在肿瘤标志物和药物靶点具有新的作用。

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