亲环蛋白-D与腺嘌呤核苷酸转位酶之间特定相互作用的直接证明证实了它们在线粒体通透性转换中的作用。
Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition.
作者信息
Woodfield K, Rück A, Brdiczka D, Halestrap A P
机构信息
Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, U.K.
出版信息
Biochem J. 1998 Dec 1;336 ( Pt 2)(Pt 2):287-90. doi: 10.1042/bj3360287.
Abstract
A fusion protein between cyclophilin-D (CyP-D) and glutathione S-transferase (GST) was shown to bind to purified liver inner mitochondrial membranes (IMMs) in a cyclosporin A (CsA)-sensitive manner. Binding was enhanced by diamide treatment of the IMMs. Immobilized GST-CyP-D avidly bound a single 30 kDa protein present in Triton X-100-solubilized IMMs; immunoblotting showed this to be the adenine nucleotide translocase (ANT). Binding was prevented by pretreatment of the CyP-D with CsA, but not with cyclosporin H. Purified ANT also bound specifically to GST-CyP-D, but porin did not, even in the presence of ANT.
摘要
亲环蛋白-D（CyP-D）与谷胱甘肽S-转移酶（GST）之间的融合蛋白被证明以环孢菌素A（CsA）敏感的方式与纯化的肝脏线粒体内膜（IMM）结合。通过二酰胺处理IMM可增强结合。固定化的GST-CyP-D能强烈结合Triton X-100溶解的IMM中存在的一种30 kDa单一蛋白质；免疫印迹显示这是腺嘌呤核苷酸转位酶（ANT）。用CsA预处理CyP-D可阻止结合，但用环孢菌素H预处理则不能。纯化的ANT也能特异性结合GST-CyP-D，但孔蛋白即使在ANT存在的情况下也不能结合。
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