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(Arteriosclerosis, Thrombosis, and Vascular Biology. 2007;27:2491.)
© 2007 American Heart Association, Inc.

Editorials

Scavenger Receptor A and CD36 Are Implicated in Mediating Platelet Activation Induced by Oxidized Low- Density Lipoproteins

Sophie Collot-Teixeira; Ferrucio Delorenzo; John L. McGregor

From the Cardiovascular Division (S.C.-T., J.L.M.), King’s College London, UK; Chelsea and Westminster Hospital Trust NHS Foundation (F.D.), London, UK; and INSERM unit 689 (J.L.M.), Hôpital Lariboissiere, Paris, France.

Correspondence to John L. McGregor, the Cardiovascular Division, King’s College London, UK. Email john.mcgregor@kcl.ae.uk

An extract of the first 250 words of the full text is provided, because this article has no abstract.

See ATVB 2007;2476–2483.

CD36, previously known as GPIIIb or GPIV, is an 88-kDa membrane glycoprotein that was isolated from blood platelets soon after being identified on monocytes by monoclonal antibody OKM5. Cloning the CD36 gene showed this cell adhesion molecule to be a member of the scavenger receptor class B family. Moreover, it was observed that CD36 has the capacity to bind oxidized low-density lipoproteins (oxLDL) but not acetylated lipoproteins. Scavenger receptor class A (SRA),¹ also expressed on platelets and monocytes/macrophages, is a trimer of 77 kDa, that binds to acetylated and oxidized lipoproteins. SRA is closely associated to macrophage CD36 in initiating atherosclerotic lesions, in some studies but not all.^2,3,4 Very little was known, up to now, on the role played by oxLDL in activating platelets via CD36 and SRA and promoting a prothrombotic phenotype.

The study, in this issue of Arteriosclerosis, Thrombosis, and Vascular Biology, by Suzanne Korporaal and coworkers,⁵ shows very elegantly that oxLDL, in tandem with CD36 and SRA, is activating platelets and potentially increasing the risk of thrombosis. This investigation brings some exciting data on a novel platelet-activating pathway triggered by partially oxidized (30% to 60%) LDL and mediated by the combined activity of CD36 and SRA. The authors observed a 2-fold increase, with no change in transient kinetics, in the phosphorylation of platelet p38^MAPK induced by oxLDL compared with native LDL (nLDL). Such an increase was not attributable to stronger activation of the LDL receptor family member apolipoprotein E receptor-2 (apoER2'), also known . . . [Full Text of this Article]