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象大多数解整连蛋白-金属蛋白酶(a disintegrin and metalloprotease,ADAMS),肿瘤坏死因子α转换酶(tumor necrosis factor-α converting enzyme,TACE)是一种多结构域的Ⅰ型跨膜蛋白,具有显著的金属蛋白酶水解活性。其主要功能是将膜结合型肿瘤坏死因子α(mTNF-α)前体水解,产生具有生物活性的可溶性TNF-α(sTNF-α),而对TACE这一在胞外脱落机制还不十分清楚,其在生物体内调节方式及各结构域的相互作用还有待进一步研究。而TACEC末端区域能否结合信号分子及其位点如何,对研究其结构和与其结合的蛋白质的信号转导以及转换的机制将有着重要的意义。找出其在胞膜外脱落的原因,是否与C末端结合的膜蛋白或蛋白水解酶有关,这已成为研究的热点。C末端尾部(694～824)为胞浆内段,包含一个潜在的磷酸化位点和一个结合同源物3区(Srchomology3do-main,SH3)的位点,有趣的是TACE胞内区很可能具有信号转导的功能。本文就近年来TACE在其生物学结构、特性和与疾病关系方面的研究进行综述。
Like most disintegrin and metalloprotease (ADAMS), tumor necrosis factor-α converting enzyme (TACE) is a multidomain type I transmembrane protein with Significant metalloprotease hydrolysis activity. Its main function is to hydrolyze the membrane-bound precursor of tumor necrosis factor alpha (mTNF-α) to produce bioactive soluble TNF-α (sTNF-α), yet it is unclear how TACE is involved in extracellular shedding , Its in vivo regulation of the way and the interaction of each domain remains to be further studied. Whether TACEC end-region can bind signal molecules and their loci will be of great significance for studying the signal transduction and translation mechanism of its structure and the proteins it binds to. To find out the reasons for its shedding in the extracellular membrane, whether the C-terminal membrane protein or proteolytic enzymes, which has become a research hot spot. The C-terminal tail (694-824) is an intracytoplasmic segment that contains a potential phosphorylation site and a site that binds to Srchomology3do-main (SH3). Interestingly, the intracellular region of TACE is likely With signal transduction function. In this paper, recent reviews of TACE in its biological structure, properties and relationship to disease are reviewed.