Journal
JOURNAL OF CLINICAL INVESTIGATION
Volume 108, Issue 6, Pages 785-791Publisher
AMER SOC CLINICAL INVESTIGATION INC
DOI: 10.1172/JCI200114006
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- NEI NIH HHS [EY-10967] Funding Source: Medline
- NHLBI NIH HHS [HL-58559, HL-42540, P0HL-56987] Funding Source: Medline
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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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