| Autor: |
Korporaal SJ; Department of Haematology, Laboratory Thrombosis and Haemostasis, Institute for Biomembranes, University Medical Center Utrecht, The Netherlands. j.a.korporaal@lab.azu.nl, Relou IA, van Rijn HJ, Akkerman JW |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 2001 Apr 06; Vol. 494 (1-2), pp. 121-4. |
| DOI: |
10.1016/s0014-5793(01)02322-5 |
| Abstrakt: |
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 alpha(IIb)beta(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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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