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Am J Physiol Renal Physiol 283: F876-F887, 2002; doi:10.1152/ajprenal.00148.2002
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Vol. 283, Issue 5, F876-F887, November 2002

INVITED REVIEW
Structural determinants and significance of regulation of electrogenic Na+-HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> cotransporter stoichiometry

Eitan Gross1 and Ira Kurtz2

1 Departments of Urology and Physiology and Biophysics, Case Western Reserve University, and Veterans Affairs Medical Center, Cleveland, Ohio 44106; and 2 Division of Nephrology, David Geffen School of Medicine, University of California, Los Angeles, California 90095

Na+-HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> cotransporters play an important role in intracellular pH regulation and transepithelial HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> transport in various tissues. Of the characterized members of the HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> transporter superfamily, NBC1 and NBC4 proteins are known to be electrogenic. An important functional property of electrogenic Na+-HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> cotransporters is their HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>:Na+ coupling ratio, which sets the transporter reversal potential and determines the direction of Na+-HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> flux. Recent studies have shown that the HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>:Na+ transport stoichiometry of NBC1 proteins is either 2:1 or 3:1 depending on the cell type in which the transporters are expressed, indicating that the HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>:Na+ coupling ratio can be regulated. Mutational analysis has been very helpful in revealing the molecular mechanisms and signaling pathways that modulate the coupling ratio. These studies have demonstrated that PKA-dependent phosphorylation of the COOH terminus of NBC1 proteins alters the transport stoichiometry. This cAMP-dependent signaling pathway provides HCO<UP><SUB>3</SUB><SUP>−</SUP></UP>-transporting epithelia with an efficient mechanism for modulating the direction of Na+-HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> flux through the cotransporter.

bicarbonate; transport; sodium


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