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Am J Physiol Heart Circ Physiol 281: H266-H274, 2001;
0363-6135/01 $5.00
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Vol. 281, Issue 1, H266-H274, July 2001

Regulation of tyrosine phosphorylation of PYK2 in vascular endothelial cells by lysophosphatidylcholine

Yoshiyuki Rikitake1, Seinosuke Kawashima1, Tomosaburo Takahashi1, Tomomi Ueyama1, Satoshi Ishido2, Nobutaka Inoue1, Ken-Ichi Hirata1, and Mitsuhiro Yokoyama1

1 First Department of Internal Medicine and 2 Department of Microbiology, Kobe University School of Medicine, Kobe 650-0017, Japan

Lysophosphatidylcholine (LPC), a component of oxidized low-density lipoprotein, exerts various biological effects on vascular endothelial cells. However, the intracellular signaling of LPC is poorly understood. In this study, we investigated the involvement of proline-rich tyrosine kinase (PYK2) in LPC signaling in cultured bovine aortic endothelial cells by immunoprecipitation and Western blotting assays. Treatment of cells with LPC promoted a rapid increase in tyrosine phosphorylation of PYK2. LPC-stimulated PYK2 phosphorylation was inhibited by calcium chelators, 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid-acetoxymethyl ester, EGTA, protein kinase C (PKC) inhibitor, GF-109203X, or PKC depletion by phorbol esters. PYK2 phosphorylation was inhibited by treatment with cytochalasin D but with neither botulinum C3 transferase nor overexpression of a dominant negative mutant of Rho A. LPC stimulated the association of Shc with PYK2, Shc tyrosine phosphorylation, and Grb2 binding to Shc and induced Ras activation. These results provide evidence that 1) LPC tyrosine phosphorylates PYK2 by calcium- and PKC-dependent mechanisms, 2) the intact cytoskeleton is required for LPC-stimulated PYK2 phosphorylation, and 3) LPC-activated Ras via the PYK2/Shc/Grb2 signaling.

tyrosine kinase; calcium; protein kinase C; Ras; proline-rich tyrosine kinase


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