Peitsch M C, Tschopp J, Kress A, Isliker H
Institute of Biochemistry, University of Lausanne, Switzerland.
Biochem J. 1988 Jan 15;249(2):495-500. doi: 10.1042/bj2490495.
Non-immune activation of the first component of complement (C1) by the heart mitochondrial inner membrane has been investigated. Cardiolipin, the only strong activator of C1 among phospholipids, is present in large amounts in the heart mitochondrial inner membrane. We therefore studied its contribution to C1 activation by mitochondria. The proteins of the mitochondrial inner membrane were found to activate C1 only weakly, in contrast with the phospholipid fraction which induces strong C1 activation. Furthermore, the digestion of mitochondrial inner membranes with proteolytic enzymes did not affect C1 activation. Additional support in favour of cardiolipin being the responsible activator came from competition experiments with mitochondrial creatine kinase (mt-CPK) and adriamycin, known to bind to cardiolipin. Both mt-CPK and adriamycin displaced C1q from the mitochondrial inner membrane. In addition, C1q displaced mt-CPK bound to mitoplasts.
已对心脏线粒体内膜对补体第一成分（C1）的非免疫激活进行了研究。心磷脂是磷脂中唯一能强烈激活C1的物质，大量存在于心脏线粒体内膜中。因此，我们研究了它对线粒体激活C1的作用。与能强烈激活C1的磷脂部分相比，线粒体内膜蛋白仅能微弱激活C1。此外，用蛋白水解酶消化线粒体内膜并不影响C1的激活。支持心磷脂是激活因子的其他证据来自与线粒体肌酸激酶（mt-CPK）和阿霉素的竞争实验，已知这两种物质能与心磷脂结合。mt-CPK和阿霉素都能使C1q从线粒体内膜上解离下来。此外，C1q能使结合在有丝分裂体上的mt-CPK解离下来。
