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Am J Physiol Cell Physiol (July 25, 2007). doi:10.1152/ajpcell.00157.2007
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Submitted on April 16, 2007
Accepted on May 29, 2007

Interactions of Transmembrane Carbonic Anhydrase, CAIX, with Bicarbonate Transporters

Patricio Eduardo Morgan1, Silvia Pastorekova2, Alan K Stuart-Tilley3, Seth L. Alper4, and Joseph R. Casey1*

1 Physiology, University of Alberta, Edmonton, Canada
2 Centre of Molecular Medicine, Slovak Academy of Sciences, Bratislava, Slovakia
3 Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts, United States
4 Molecular Medicine and Renal Units, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts, United States

* To whom correspondence should be addressed. E-mail: joe.casey{at}ualberta.ca.

Association of some plasma membrane bicarbonate transporters with carbonic anhydrase enzymes forms a bicarbonate transport metabolon to facilitate metabolic CO2-HCO3- conversions and coupled HCO3- transport. The transmembrane carbonic anhydrase, CAIX, with its extracellular catalytic site, is highly expressed in parietal and other cells of gastric mucosa, suggesting a role in acid secretion. We examined in transfected HEK293 cells the functional and physical interactions between CAIX and the parietal cell Cl-/HCO3- exchanger AE2 or the putative Cl-/HCO3- exchanger, SLC26A7. Co-expression of CAIX increased AE2 transport activity by 28 ± 7% and also activated transport mediated by AE1 and AE3 (32 ± 10% and 37 ± 9%, respectively). In contrast, despite a transport rate comparable to that of AE3, co-expressed CAIX did not alter transport associated with SLC26A7. The CAIX-associated increase of AE2 activity did not result from altered AE2 expression or cell surface processing. CAIX was co-immunoprecipitated with the co-expressed SLC4 polypeptides AE1, AE2 and AE3, but not with SLC26A7. GST pull-down assays with a series of domain-deleted forms of CAIX revealed that the catalytic domain of CAIX mediated interaction with AE2. AE2 and CAIX co-localized in human gastric mucosa, as indicated by co-immunofluorescence. This is the first example of a functional and physical interaction between a bicarbonate transporter and a transmembrane carbonic anhydrase. We conclude that CAIX can bind to some Cl-/HCO3- exchangers to form a bicarbonate transport metabolon.




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