期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 269, 期 1, 页码 143-148出版社
ACADEMIC PRESS INC
DOI: 10.1006/bbrc.2000.2271
关键词
aminopeptidase N/CD13; microdomains; raft; cyclodextrin; GM1 ganglioside
Ectopeptidases play important roles in cell activation, proliferation, and communication. Human monocytic cells express considerable amounts of aminopeptidase N/CD13, a transmembrane protein previously proposed to play a role in the regulation of neuropeptides and chemotactic mediators as well as in adhesion and cell-cell interactions. Here, we report for the first time that aminopeptidase N/CD13 in monocytes is partially localized in detergent-insoluble membrane microdomains enriched in cholesterol, glycolipids, and glycosylphosphoinositol-anchored proteins, referred to as rafts. Raft fractions of monocytes were characterized by the presence of GM1 ganglioside as raft marker molecule and by the high level of tyrosine-phosphorylated proteins. Furthermore, similar to polarized cells, rafts in monocytic cells lack Na+, K+-ATPase. Cholesterol depletion of monocytes by methyl-beta-cyclodextrin greatly reduces raft localization of aminopeptidase N/CD13 without affecting ala-p-nitroanilide cleaving activity of cells. (C) 2000 Academic Press.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据