Lysophosphatidic acid-independent platelet activation by low-density lipoprotein

S. J A Korporaal, I. A M Relou, H. J M Van Rijn, J. W N Akkerman

    Research output: Contribution to journalArticleAcademicpeer-review

    8 Citations (Scopus)

    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 languageEnglish
    Pages (from-to)121-124
    Number of pages4
    JournalFEBS letters
    Volume494
    Issue number1-2
    DOIs
    Publication statusPublished - 2001

    Keywords

    • αβ
    • Low-density lipoprotein
    • Lysophosphatidic acid
    • N-Palmitoyl-L-serine-phosphoric acid

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