Parmar J S, Lomas D A
Cambridge Institute for Medical Research.
J R Coll Physicians Lond. 2000 May-Jun;34(3):295-300.
Alpha-1-antitrypsin deficiency results from point mutations that distort the structure of the protein to allow a unique protein-protein interaction that we have termed loopsheet polymerisation. Polymers of Z alpha 1-antitrypsin accumulate within hepatocytes to form inclusion bodies that are associated with juvenile cirrhosis and hepatocellular carcinoma. The lack of circulating protein predisposes the Z alpha 1-antitrypsin homozygote to emphysema. This process also occurs in other members of the serine proteinase inhibitor (serpin) superfamily, antithrombin, C1-inhibitor and alpha 1-antichymotrypsin, in association with thrombosis, angioedema and chronic obstructive pulmonary disease, respectively, and we have recently shown that it underlies a novel inclusion body dementia. The interaction provides a useful paradigm for other 'conformational diseases' such as Huntington's disease, Creutzfeldt-Jakob disease and the amyloidoses.
α-1-抗胰蛋白酶缺乏症是由点突变引起的,这些突变会扭曲蛋白质的结构,从而产生一种独特的蛋白质-蛋白质相互作用,我们将其称为环片聚合。Z型α-1-抗胰蛋白酶的聚合物在肝细胞内积累,形成与青少年肝硬化和肝细胞癌相关的包涵体。循环蛋白的缺乏使Z型α-1-抗胰蛋白酶纯合子易患肺气肿。这个过程也发生在丝氨酸蛋白酶抑制剂(serpin)超家族的其他成员中,抗凝血酶、C1抑制剂和α-1-抗糜蛋白酶,分别与血栓形成、血管性水肿和慢性阻塞性肺疾病有关,并且我们最近发现它是一种新型包涵体痴呆的基础。这种相互作用为其他“构象性疾病”,如亨廷顿舞蹈症、克雅氏病和淀粉样变性病,提供了一个有用的范例。