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Papers In Press, published online ahead of print October 21, 2003
Department of Internal Medicine and Nephrology, University of Texas Southwestern Medical Center, Dallas, TX 75390-8856
Corresponding Author: francesca.disole{at}utsouthwestern.edu
Adenosine is an autocoid that regulates renal Na+ transport. Activation of adenosine A1 receptor (A1R) by CPA (N6-cyclopentidyladenosine) inhibits the Na+/H+ exchanger NHE3 via PLC/Ca2+/PKC signaling pathway. Mutation of PKC phosphorylation sites on NHE3 does not affected regulation of NHE3 by CPA but amino acid residues 462 and 552 are essential for A1R-dependent control of NHE3 activity. One binding partner of the NHE family is calcineurin homologous protein (CHP). We tested the role of NHE3-CHP interaction in mediating CPA-induced inhibition of NHE3 in opossum kidney (OK) and Xenopus laevis uroepithelial (A6) cells. Both native and transfected NHE3 and CHP are present in the same immunocomplex by co-immunoprecipitation. CPA (10-6 M) increases CHP-NHE3 interaction by 30-60% (native and transfected proteins). Direct CHP-NHE3 interaction is evident by yeast-two-hybrid assay (bait: NHE3C-terminus; prey: CHP); the minimal interacting region is localized to the juxtamembrane region of NHE3C-terminus (aa 462-552 opossum NHE3). The yeast data was confirmed in OK cells where truncated NHE3 (NHE3552) still shows CPA-stimulated CHP interaction. Overexpression of the polypeptide from the CHP-binding region (NHE3462-552) interferes with the ability of CPA to inhibit NHE3 activity and to increase CHP-NHE3Full length interaction. Reduction of native CHP expression by siRNA abolishes the ability of CPA to inhibit NHE3 activity. We conclude that CHP-NHE3 interaction is regulated by A1R activation and this interaction is a necessary and integral part of the signaling pathway between adenosine and NHE3.
J. Biol. Chem, 10.1074/jbc.M306838200
Submitted on June 26, 2003
Revised on October 21, 2003
Accepted on October 20, 2003
Acute regulation of Na/H exchanger NHE3 by adenosine A1 receptors is mediated by calcineurin homologous protein (CHP)
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