外域
去整合素
金属蛋白酶
肿瘤坏死因子α
细胞生物学
蛋白质水解
生物
转化生长因子
受体
表型
细胞粘附
蛋白酶
细胞
基质金属蛋白酶
免疫学
酶
生物化学
基因
作者
Jacques J. Peschon,Jennifer L. Slack,P. Madhusudhana Reddy,Kim L. Stocking,Susan W. Sunnarborg,Dong Hoon Lee,William E. Russell,Beverly J. Castner,Richard S. Johnson,Jeffrey N. Fitzner,Rogely Waite Boyce,Nicole Nelson,Carl J. Kozlosky,Martin F. Wolfson,Charles T. Rauch,Douglas Pat Cerretti,Raymond J. Paxton,Carl J. March,Roy A. Black
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1998-11-13
卷期号:282 (5392): 1281-1284
被引量:1542
标识
DOI:10.1126/science.282.5392.1281
摘要
The ectodomains of numerous proteins are released from cells by proteolysis to yield soluble intercellular regulators. The responsible protease, tumor necrosis factor-α converting enzyme (TACE), has been identified only in the case when tumor necrosis factor-α (TNFα) is released. Analyses of cells lacking this metalloproteinase-disintegrin revealed an expanded role for TACE in the processing of other cell surface proteins, including a TNF receptor, the l -selectin adhesion molecule, and transforming growth factor-α (TGFα). The phenotype of mice lacking TACE suggests an essential role for soluble TGFα in normal development and emphasizes the importance of protein ectodomain shedding in vivo.
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