Abstract
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 αIIbβ3. 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 Ca2+ rises completely blocked ligand binding by TRAP and nLDL/TRAP. Inhibitors of p38MAPK 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. © 2001 Federation of European Biochemical Societies.
Original language | English |
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Pages (from-to) | 121-124 |
Number of pages | 4 |
Journal | FEBS letters |
Volume | 494 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 2001 |
Keywords
- αβ
- Low-density lipoprotein
- Lysophosphatidic acid
- N-Palmitoyl-L-serine-phosphoric acid