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Originally published In Press as doi:10.1074/jbc.M010834200 on February 16, 2001

J. Biol. Chem., Vol. 276, Issue 20, 17339-17346, May 18, 2001
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Bradykinin B2 Receptors Activate Na+/H+ Exchange in mIMCD-3 Cells via Janus Kinase 2 and Ca2+/Calmodulin*

Yurii V. MukhinDagger , Tamara VlasovaDagger , Ayad A. Jaffa§, Georgiann CollinsworthDagger , John L. BellDagger , Baby G. TholanikunnelDagger , Tobiah Pettus, Wayne FitzgibbonDagger , David W. PlothDagger , John R. RaymondDagger , and Maria N. GarnovskayaDagger ||

From the Medical and Research Services of the Ralph H. Johnson Veterans Affairs Medical Center, and Departments of Medicine (Dagger  Nephrology and § Endocrinology Divisions) and  Pharmacology of the Medical University of South Carolina, Charleston, South Carolina 29425

We used a cultured murine cell model of the inner medullary collecting duct (mIMCD-3 cells) to examine the regulation of the ubiquitous sodium-proton exchanger, Na+/H+ exchanger isoform 1 (NHE-1), by a prototypical G protein-coupled receptor, the bradykinin B2 receptor. Bradykinin rapidly activates NHE-1 in a concentration-dependent manner as assessed by proton microphysiometry of quiescent cells and by 2'-7'-bis[2-carboxymethyl]-5(6)-carboxyfluorescein fluorescence measuring the accelerated rate of pHi recovery from an imposed acid load. The activation of NHE-1 is blocked by inhibitors of the bradykinin B2 receptor, phospholipase C, Ca2+/calmodulin (CaM), and Janus kinase 2 (Jak2), but not by pertussis toxin or by inhibitors of protein kinase C and phosphatidylinositol 3'-kinase. Immunoprecipitation studies showed that bradykinin stimulates the assembly of a signal transduction complex that includes CaM, Jak2, and NHE-1. CaM appears to be a direct substrate for phosphorylation by Jak2 as measured by an in vitro kinase assay. We propose that Jak2 is a new indirect regulator of NHE-1 activity, which modulates the activity of NHE-1 by increasing the tyrosine phosphorylation of CaM and most likely by increasing the binding of CaM to NHE-1.

* This work was supported by grants from the Department of Veterans Affairs (Merit Awards to M. N. G., D. W. P., and J. R. R. and a REAP Award to Y. V. M., A. A. J., J. R. R., and M. N. G.), National Institutes of Health Grants DK52448 (to J. R. R.) and K01-DK02694 (to Y. V. M.), laboratory endowments jointly supported by the Medical University of South Carolina Division of Nephrology and Dialysis Clinics, Incorporated (to D. W. P. and J. R. R.), an American Heart Association Fellowship Award (to Y. V. M.), and a Medical University of South Carolina University Research Foundation award (to M. N. G.). The FLIPRTM is a shared Medical University of South Carolina resource obtained with Public Health Service Grant S10 RR13005. The microphysiometer is a shared Veterans Affairs resource obtained with a Veterans Affairs large equipment grant.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: Rm. 829 CSB, Medical University of South Carolina, 171 Ashley Ave., Charleston, SC 29425-2227. Tel.: 843-876-5128; Fax: 843-792-8399; E-mail: garnovsk@musc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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