(Hypertension. 1999;33:201-206.)
© 1999 American Heart Association, Inc.
Scientific Contributions |
Involvement of PYK2 in Angiotensin II Signaling of Vascular Smooth Muscle Cells
From the 2nd Department of Internal Medicine, Tokyo Medical and Dental University (S.E., H.I., F.M., Y.H.), Tokyo 113, Japan; Department of Biochemistry, Vanderbilt University School of Medicine (SE, T.I., K.N., T.Y.), Nashville, Tenn; Department of Anatomy and Physiology, Meharry Medical College (E.D.M), Nashville, Tenn; and Institute of Molecular and Cellular Biology for Pharmaceutical Sciences, Kyoto Pharmaceutical University (K.M.O.), Kyoto 607, Japan.
Correspondence to Satoru Eguchi, MD, PhD, the 2nd Department of Internal Medicine, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-Ku, Tokyo 113-8519, Japan. E-mail seguchi.med2{at}med.tmd.ac.jp
Abstract—PYK2, a recently identified Ca2+-sensitive tyrosine kinase, has been implicated in extracellular signal-regulated kinase (ERK) activation via several G protein–coupled receptors. We have reported that angiotensin II (Ang II) induces Ca2+-dependent transactivation of the epidermal growth factor receptor (EGFR) which serves as a scaffold for preactivated c-Src and downstream adaptors (Shc/Grb2), leading to ERK activation in cultured rat vascular smooth muscle cells (VSMC). Herein we demonstrate the involvement of PYK2 in this cascade. Ang II rapidly induced tyrosine phosphorylation of PYK2, whose effect was completely inhibited by an AT1 receptor antagonist and an intracellular Ca2+ chelator. A Ca2+ ionophore also induced PYK2 tyrosine phosphorylation to a level comparable with that by Ang II, whereas phorbol ester–induced phosphorylation was less than that by Ang II. Moreover, PYK2 formed a complex coprecipitable with catalytically active c-Src after Ang II stimulation. Although a selective EGFR kinase inhibitor completely abolished Ang II–induced recruitment of Grb2 to EGFR and markedly attenuated Ang II–induced ERK activation, it had no effect on Ang II–induced PYK2 tyrosine phosphorylation or its association with c-Src and Grb2. These data suggest that the AT1 receptor uses Ca2+-dependent PYK2 to activate c-Src, thereby leading to EGFR transactivation, which preponderantly recruits Grb2 in rat VSMC.
Key Words: angiotensin II • receptors, angiotensin • proline-rich tyrosine kinase 2 • c-Src • epidermal growth factors • muscle, smooth, vascular • signal transduction
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A. Sorokin, P. Kozlowski, L. Graves, and A. Philip Protein-tyrosine Kinase Pyk2 Mediates Endothelin-induced p38 MAPK Activation in Glomerular Mesangial Cells J. Biol. Chem., June 8, 2001; 276(24): 21521 - 21528. [Abstract] [Full Text] [PDF]
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P. Rocic and P. A. Lucchesi Down-regulation by Antisense Oligonucleotides Establishes a Role for the Proline-rich Tyrosine Kinase PYK2 in Angiotensin II-induced Signaling in Vascular Smooth Muscle J. Biol. Chem., June 8, 2001; 276(24): 21902 - 21906. [Abstract] [Full Text] [PDF]
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J. S. Grewal, L. M. Luttrell, and J. R. Raymond G Protein-coupled Receptors Desensitize and Down-regulate Epidermal Growth Factor Receptors in Renal Mesangial Cells J. Biol. Chem., July 13, 2001; 276(29): 27335 - 27344. [Abstract] [Full Text] [PDF]
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S. Heeneman, J. Haendeler, Y. Saito, M. Ishida, and B. C. Berk Angiotensin II Induces Transactivation of Two Different Populations of the Platelet-derived Growth Factor beta Receptor. KEY ROLE FOR THE p66 ADAPTOR PROTEIN Shc J. Biol. Chem., May 19, 2000; 275(21): 15926 - 15932. [Abstract] [Full Text] [PDF]
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 K. A. DeFea, Z. D. Vaughn, E. M. O'Bryan, D. Nishijima, O. Dery, and N. W. Bunnett The proliferative and antiapoptotic effects of substance P are facilitated by formation of a beta -arrestin-dependent scaffolding complex PNAS, September 26, 2000; 97(20): 11086 - 11091. [Abstract] [Full Text] [PDF]
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S. S. Wu, T. Chiu, and E. Rozengurt ANG II and LPA induce Pyk2 tyrosine phosphorylation in intestinal epithelial cells: role of Ca2+, PKC, and Rho kinase Am J Physiol Cell Physiol, June 1, 2002; 282(6): C1432 - C1444. [Abstract] [Full Text] [PDF]
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R. Ginnan and H. A. Singer CaM kinase II-dependent activation of tyrosine kinases and ERK1/2 in vascular smooth muscle Am J Physiol Cell Physiol, April 1, 2002; 282(4): C754 - C761. [Abstract] [Full Text] [PDF]
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