MACROPHAGE PROTEASES CAN MODIFY LOW-DENSITY LIPOPROTEINS TO INCREASE THEIR UPTAKE BY MACROPHAGES

被引：16

作者：

LEAKE, DS ^{[1
]}

RANKIN, SM ^{[1
]}

COLLARD, J ^{[1
]}

机构：

[1] UNIV LONDON,KINGS COLL LONDON,DIV BIOMED SCI,PHARMACOL GRP,LONDON WC2R 2LS,ENGLAND

来源：

FEBS LETTERS | 1990年 / 269卷 / 01期

基金：

英国惠康基金;

关键词：

Apolipoprotein B-100; Atherosclerosis; Cathepsin B; Cathepsin D; Low density lipoprotein; Macrophage; Proteolysis;

D O I：

10.1016/0014-5793(90)81156-I

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：

When low density lipoprotein (LDL) was incubated with sonicated macrophages at acidic pH, its protein moiety was partially degraded by cathepsins B and D. The reisolated LDL was taken up by intact macrophages up to about 20 times as fast as control LDL. LDL proteolysis and its enhanced uptake could be inhibited almost entirely by the selective protease inhibitors leupeptin and pepstatin. If macrophages in atherosclerotic lesions were to release acidic proteases (either by exocytosis or following cell death) and these were to modify LDL, this may help to explain why so much cholesteryl ester accumulates in these cells. © 1990.

引用

页码：209 / 212

页数：4

共 23 条

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