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Human platelets exclusively bind oxidized low density lipoprotein showing no specificity for acetylated low density lipoprotein
Author(s) -
Volf I,
Moeslinger T,
Cooper J,
Schmid W,
Koller E
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00437-8
Subject(s) - scavenger receptor , cd36 , low density lipoprotein , lipoprotein , receptor , chemistry , biochemistry , low density lipoprotein receptor related protein 8 , scavenger , acetylation , high density lipoprotein , ldl receptor , biophysics , biology , cholesterol , very low density lipoprotein , gene , radical
The widely studied macrophage scavenger receptor system is known to bind both acetylated low density lipoprotein and oxidized low density lipoprotein. Although only the latter ligand has been shown to occur in vivo, acetylated low density lipoprotein is often used to evaluate the contribution of scavenger receptors to different (patho)physiologic processes, assuming that all existing subtypes of scavenger receptors recognise both lipoproteins. In the present work, we identify human platelets as the first natural cell type to bind oxidized low density lipoprotein without showing specificity for acetylated low density lipoprotein. Consequently, platelets possess exclusive receptor(s) for oxidized low density lipoprotein distinct from the ‘classical’ scavenger receptor AI/AII. From the data presented in this work, we conclude that the class B scavenger receptor CD36 (GPIV) is responsible for this exclusive oxidized low density lipoprotein binding.