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XB-ART-633
Biochem Biophys Res Commun 2006 Apr 21;3424:1114-22. doi: 10.1016/j.bbrc.2006.02.064.
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Molecular cloning and functional expression of a sodium bicarbonate cotransporter from guinea-pig parotid glands.

Koo NY , Li J , Hwang SM , Choi SY , Lee SJ , Oh SB , Kim JS , Lee JH , Park K .


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We recently found that the concentration of HCO3- in guinea-pig saliva is very similar to that of human saliva; however, the entity that regulates HCO3- transport has not yet been fully characterized. In order to investigate the mechanism of HCO3- transport, we identified, cloned, and characterized a sodium bicarbonate (Na(+)/HCO3- cotransporter found in guinea-pig parotid glands (gpNBC1). The gpNBC1 gene encodes a 1079-amino acid protein that has 95% and 96% homology with human and mouse parotid NBC1, respectively. Oocytes expressing gpNBC1 were exposed to HCO3- or Na(+)-free solutions, which resulted in a marked change in membrane potentials (V(m)), suggesting that gpNBC1 is electrogenic. Likewise, a gpNBC1-mediated pH recovery was observed in gpNBC1 transfected human hepatoma cells; however, in the presence of 4, 4-diisothiocyanostilbene-2,2-disulfonic acid, a specific NBC1 inhibitor, such changes in V(m) and pH(i) were not observed. Together, the data show that the cloned guinea-pig gene is a functional, as well as sequence homologue of human NBC1.

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Species referenced: Xenopus laevis
Genes referenced: slc4a4