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Lysophosphatidic acid‐independent platelet activation by low‐density lipoprotein
Author(s) -
Korporaal Suzanne J.A,
Relou Ingrid A.M,
van Rijn Herman J.M,
Akkerman Jan-Willem N
Publication year - 2001
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(01)02322-5
Subject(s) - chemistry , lysophosphatidic acid , platelet , biochemistry , thrombin , protein kinase a , receptor , ligand (biochemistry) , biophysics , kinase , biology , immunology
Mildly oxidized low‐density lipoprotein activates platelets through lysophosphatidic acid (LPA). Hence, the platelet‐activating properties attributed to native low‐density lipoprotein (nLDL) might be caused by LPA contamination. We show that nLDL enhances thrombin receptor‐activating peptide (TRAP)‐induced fibrinogen binding to α IIb β 3 . The LPA receptor blocker N ‐palmitoyl‐ L ‐serine‐phosphoric acid did not affect nLDL‐enhanced fibrinogen binding induced by TRAP, but reduced TRAP‐induced binding. cAMP and inhibitors of protein kinase C and Ca 2+ rises completely blocked ligand binding by TRAP and nLDL/TRAP. Inhibitors of p38 MAPK and ADP secretion interfered only partially. Blockade of Rho‐kinase increased ligand binding 2–3‐fold. We conclude that nLDL enhances TRAP‐induced fibrinogen binding independent of LPA.