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

Abstract：

:Lysophosphatidylcholine (lyso-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 mumol/L of lyso-PC but not to phorbol myristate acetate (PMA). Prolonged preexposure to PMA did not affect lyso-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 immunoblotting of lyso-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 lyso-PC-induced modulation of endothelial functions.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Ochi H,Kume N,Nishi E,Moriwaki H,Masuda M,Fujiwara K,Kita T

doi

10.1006/bbrc.1998.8198

subject

Has Abstract

pub_date

1998-02-24 00:00:00

pages

862-8

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(98)98198-0

journal_volume

243

pub_type

杂志文章

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