ISOLATION AND CHARACTERIZATION OF A MEMBRANE-PROTEIN FROM RAT ERYTHROCYTES WHICH INHIBITS LYSIS BY THE MEMBRANE ATTACK COMPLEX OF RAT COMPLEMENT

被引:84
作者
HUGHES, TR
PIDDLESDEN, SJ
WILLIAMS, JD
HARRISON, RA
MORGAN, BP
机构
[1] UNIV WALES COLL MED,DEPT MED BIOCHEM,HEATH PK,CARDIFF CF4 4XN,S GLAM,WALES
[2] CARDIFF ROYAL INFIRM,INST NEPHROL,CARDIFF CF2 1SZ,S GLAM,WALES
[3] MRC,MIP UNIT,CAMBRIDGE CB2 2QH,ENGLAND
基金
英国惠康基金;
关键词
D O I
10.1042/bj2840169
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The membrane attack complex (MAC) of complement in humans is regulated by several membrane-bound proteins; however, no such proteins have so far been described in other species. Here we report the isolation and characterization of a rat erythrocyte membrane glycoprotein of molecular mass 21 kDa which inserts into cell membranes and is a potent inhibitor of the rat MAC. This protein, here called rat inhibitory protein (RIP), was first partially purified by column chromatography from a butanol extract of rat erythrocyte membranes. Monoclonal antibodies (Mabs) were raised against RIP and used for its affinity purification. Affinity-purified RIP was shown to inhibit in a dose-dependent manner the cobra venom factor (CVF)-mediated 'reactive' lysis of guinea pig erythrocytes by rat complement. Conversely, the anti-RIP MAbs 6D1 and TH9 were shown to markedly enhance the CVF-mediated lysis of rat erythrocytes by rat complement. RIP acted late in the assembly of the MAC (at or after the C5b-8 stage) and was releasable from the membranes of rat erythrocytes by phosphatidylinositol-specific phospholipase C. These features, together with its size, deglycosylation pattern and N-terminal amino acid sequence, lead us to conclude that RIP is the rat homologue of the human MAC-inhibitory protein CD59 antigen.
引用
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页码:169 / 176
页数:8
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