CD36: a class B scavenger receptor involved in angiogenesis, atherosclerosis, inflammation, and lipid metabolism

被引:551
作者
Febbraio, M
Hajjar, DP
Silverstein, RL
机构
[1] Cornell Univ, Weill Med Coll, Dept Med, Div Hematol Med Oncol, New York, NY 10021 USA
[2] Cornell Univ, Weill Med Coll, Ctr Vasc Biol, New York, NY 10021 USA
[3] Cornell Univ, Weill Med Coll, Dept Pathol, New York, NY 10021 USA
[4] Cornell Univ, Weill Med Coll, Dept Biochem, New York, NY 10021 USA
关键词
D O I
10.1172/JCI14006
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
CD36, identified more than a quarter of a century ago as a platelet integral membrane glycoprotein (glycoprotein IV), was until recently best known as a receptor for thrombospondin-1 (TSP-1). TSP-1 is found in ECMs and platelet a granules, and it participates in cell attachment, motility and proliferation, as well as in modulation of protease activity, TGF-beta activation, neurite outgrowth, and angiogenesis (1). Initially, this receptor-ligand pair was shown to mediate interactions between platelets and monocytes, tumor cells, and matrix. Since then, CD36 has been implicated in multiple biological processes that define it as a multiligand scavenger receptor (see ref. 2 for review). These ligands appear remarkably diverse: In addition to TSP-1, they include long-chain fatty acids, modified LDL, retinal photoreceptor outer segments, Plasmodium falciparum malaria-parasitized erythrocytes, sickle erythrocytes, anionic phospholipids, apoptotic cells, and collagens I and IV. The biology of CD36 can be broadly divided in terms of functions that it mediates with or without TSP-1, but it is probable that it acts in concert with other proteins, such as fatty acid-binding proteins, caveola-associated proteins, integrins, cytoskeletal proteins, and signaling molecules, to effect its diverse functions.
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页码:785 / 791
页数:7
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