Tyrosine phosphorylation of platelet endothelial cell adhesion molecule-1 induced by lysophosphatidylcholine in cultured endothelial cells

Lysophosphatidylcholine (lyse-PC), a biologically active phospholipid, appears to modulate various endothelial cell functions through tyrosine kinase-dependent signaling pathways. In cultured bovine aortic endothelial cells (BAEC), we have found that a 130 kDa protein (p130) was rapidly tyrosine phosphorylated within 2 min and sustained for, at least, 1 hr in response to 10 mu mol/L of lyse-PC but not to phorbol myristate acetate (PMA). Prolonged preexposure to PMA did not affect lyse-PC-induced p130 tyrosine phosphorylation, suggesting that mechanisms independent of protein kinase C may be involved, Fractionation of the cell lysates revealed that p130 was detectable in the membrane fraction but not in the cytosolic fraction. Immunoprecipitation followed by immunoblot ting of lyse-PC-treated BAEC identified p130 as bovine PECAM-1. Tyrosine phosphorylation of PECAM-1 appears to be one of the earliest events elicited by lyso-PC, and may play a role in lyse-PC-induced modulation of endothelial functions. (C) 1998 Academic Press.