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J Biol Chem, Vol. 275, Issue 18, 13420-13426, May 5, 2000

Inhibition of AT1 Receptor Internalization by Concanavalin A Blocks Angiotensin II-induced ERK Activation in Vascular Smooth Muscle Cells
INVOLVEMENT OF EPIDERMAL GROWTH FACTOR RECEPTOR PROTEOLYSIS BUT NOT AT1 RECEPTOR INTERNALIZATION*

Hua Tang, Toshihide Nishishita, Trinita Fitzgerald, Erwin J. LandonDagger , and Tadashi Inagami§

From the Departments of Biochemistry and Dagger  Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232

Recent studies of beta 2-adrenergic receptor suggest that agonist-promoted receptor internalization may play an important role in extracellular signal-regulated kinase (ERK) activation by G protein-coupled receptors. In the present study, we explored the effects of angiotensin II (Ang II) type-1 receptor (AT1) internalization on Ang II-induced activation of ERK using the receptor internalization blocker concanavalin A (ConA) and the carboxyl terminus-truncated receptor mutants with impaired internalization. ConA inhibited AT1 receptor internalization without affecting ligand binding to the receptor, Ang II-induced generation of second messengers, and activation of tyrosine kinases Src and Pyk2 in vascular smooth muscle cells (VSMC). ConA blocked ERK activation evoked by Ang II and the calcium ionophore A23187. Impairment of AT1 receptor internalization by truncating the receptor carboxyl terminus did not affect Ang II-induced ERK activation. ConA induced proteolytic cleavage of the epidermal growth factor (EGF) receptor at carboxyl terminus and abolished Ang II-induced transactivation of the EGF receptor, which is critical for ERK activation by Ang II in VSMC. ConA also induced proteolysis of erbB-2 but not platelet-derived growth factor receptor. Thus, ConA blocks Ang II-induced ERK activation in VSMC through a distinct mechanism, the ConA-mediated proteolysis of the EGF receptor.

* This work was supported in part by National Institutes of Health Grants HL-58205.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: 663 Light Hall, Dept. of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232. Tel.: 615-322-4347; Fax: 615-322-3201; E-mail: Hua.Tang@vanderbilt.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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