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Originally published In Press as doi:10.1074/jbc.M104726200 on December 5, 2001

J. Biol. Chem., Vol. 277, Issue 9, 7298-7307, March 1, 2002
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Signal Transduction of Physiological Concentrations of Vasopressin in A7r5 Vascular Smooth Muscle Cells
A ROLE FOR PYK2 AND TYROSINE PHOSPHORYLATION OF K+ CHANNELS IN THE STIMULATION OF Ca2+ SPIKING*

Kenneth L. ByronDagger § and Pamela A. Lucchesi

From the Dagger  Loyola University Chicago, Department of Medicine, Cardiovascular Institute, Maywood, Illinois 60153 and  Department of Physiology and Biophysics, University of Alabama at Birmingham, Birmingham, Alabama 35294

The signal transduction pathway linking physiological concentrations of [Arg8]vasopressin (AVP) to an increase in frequency of Ca2+ spiking was examined in confluent cultures of A7r5 vascular smooth muscle cells. Immunoprecipitation/Western blot studies revealed a robust increase in tyrosine phosphorylation of the non-receptor tyrosine kinase, PYK2, in A7r5 cells treated with 4beta -phorbol 12-myristate 13-acetate or ionomycin. 100 pM AVP also induced PYK2 tyrosine phosphorylation, and this effect was inhibited by protein kinase C inhibitors Ro-31-8220 (1-10 µM) or chelerythrine chloride (1-20 µM). In fura-2-loaded A7r5 cells, the stimulation of Ca2+ spiking by 100 pM AVP or 1 nM 4beta -phorbol 12-myristate 13-acetate was completely blocked by PP2 (10 µM, a Src family kinase inhibitor). Salicylate (20 mM, recently identified as a PYK2 inhibitor) and the tyrosine kinase inhibitor, tyrphostin A47 (50 µM), but not its inactive analog, tyrphostin A63, also blocked AVP-stimulated Ca2+ spiking. PYK2 phosphorylation was inhibited by both PP2 and salicylate, whereas tyrphostin A47 failed to inhibit PYK2 tyrosine phosphorylation. ERK1/2 kinases did not appear to be involved because 1) 100 pM AVP did not appreciably increase ERK1/2 phosphorylation and U-0126 (2.5 µM) did not inhibit AVP-stimulated Ca2+ spiking; and 2) epidermal growth factor (10 nM) robustly stimulated ERK1/2 phosphorylation but did not induce Ca2+ spiking. Delayed rectifier K+ channels may mediate the PYK2 activity because Kv1.2 channel protein co-immunoprecipitated with PYK2 and tyrosine phosphorylation of Kv1.2 was stimulated by AVP and inhibited by Ro-31-8220, PP2, and salicylate but not tyrphostin A47. Our findings are consistent with a role for PYK2 and phosphorylation of K+ channels in the stimulation of Ca2+ spiking by physiological concentrations of AVP.

* This work was supported by the Eugene J. and Elsie E. Weyler Endowment for Clinical Cardiology Research, the John and Marian Falk Trust for Medical Research, and NHLBI Grants R01HL60164 (to K. L. B.) and R29HL56046 (to P. A. L.) from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Loyola University Medical Center, Cardiovascular Institute, 2160 South First Ave., Maywood, IL 60153. Tel.: 708-327-2819; Fax.: 708-327-2849; E-mail: kbyron@lumc.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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