Platelet sensitization by LDL

Stable Identifier
Homo sapiens
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Physiological concentrations (1g/L) of Low density lipoprotein (LDL) enhance platelet aggregation responses initiated by thrombin, collagen, and ADP. This enhancement involves the rapid phosphorylation of p38 mitogen-activated protein kinase (p38MAPK) at Thr180 and Tyr182. The receptor for LDL is ApoER2, a splice variant of the classical ApoE receptor. ApoER2 stimulation leads to association of the Src family kinase Fgr which is probably responsible for subsequent phosphorylation of p38MAPK. This stimulation is transient because LDL also increases the activity of PECAM-1, which stimulates phosphatases that dephosphorylate p38MAPK.

Literature References
PubMed ID Title Journal Year
12775720 Platelet endothelial cell adhesion molecule-1 (PECAM-1) inhibits low density lipoprotein-induced signaling in platelets

Akkerman, JW, Gorter, G, Ferreira, IA, Relou, IA, van Rijn, HJ

J Biol Chem 2003
15459198 Binding of low density lipoprotein to platelet apolipoprotein E receptor 2' results in phosphorylation of p38MAPK

Akkerman, JW, Gorter, G, Korporaal, SJ, Strasser, V, Lenting, PJ, Bezemer, M, Nimpf, J, van Eck, M, Relou, IA, van Berkel, TJ

J Biol Chem 2004
12038793 Platelet activation by the apoB/E receptor-binding domain of LDL

Akkerman, JW, Gorter, G, van Rijn, HJ, Relou, AM

Thromb Haemost 2002
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