SLC26A6 is encoded by the SLC26A6 gene and is also known as Solute carrier family 26 member 6, Anion exchange transporter, Pendrin-like protein 1 and Pendrin-L1. SLC26A6 was identified exclusively through database mining based on homology to SLC26A3 and pendrin. SLC26A6 gene encodes an integral membrane protein of 738 amino acids with a predicted topology of 11 transmembrane helices and an intracellular -NH2 and -COOH terminus. In silico analysis showed that the structure of the TMDs of SLC26 transporters is predicted to be most similar to that of the CLC transporters.
|Basic Information of SLC26A6|
|Protein Name||Solute carrier family 26 member 6|
|Aliases||Anion exchange transporter, Pendrin-like protein 1, Pendrin-L1|
|Organism||Homo sapiens (Human)|
Both SLC26A3 and A6 mediate apical Cl-/HCO3- exchange. However, function and expression studies suggest that these two exchangers do not exhibit parallel activities; rather they show predominance over one another in different regions of the intestine. SLC26A6 is important for the apical Cl- base exchange in the upper GI tract and SLC26A3 in the lower GI tract. In addition, it is suggested that loss of SLC26A6 may lead to a significant phenotype in pathophysiological states. Interestingly, mice deficient in SLC26A6 exhibited enhanced oxalate absorption in the small intestine, with subsequent increase in urine oxalate excretion and kidney oxalate stone formation. Therefore, the role of SLC26A6 as the major oxalate-secreting pathway in the small intestine has emerged. Collectively, several in vitro and KO mice model studies suggest that SLC26A6 can function in both Cl-/HCO3- exchange (predominantly detected in the proximal portion of the small intestine) and Cl- oxalate exchange mode, predominantly detected in the kidney proximal tubule and the ileum.
Fig.1 The putative structure of SLC26A6 TMDs. (Ohana, 2011)
This article reports that a unique feature of SLC26A6 is that it can function simultaneously as obligate Cl-/ HCO3- exchangers and can conduct anionic currents. These findings reveal the central role of the conserved Glu in determining the SLC26A6 transporter properties and raise the possibility of a similar role of the conserved Glu in coupled and uncoupled transport by the CLC and SLC26A6 transporters.
This article demonstrates that cardiac myocytes express different isoforms of SLC26A6, which encode electrogenic Cl-/HCO3- and Cl-/oxalate exchangers. The electrogenic nature of the Cl-/HCO3- exchange of cardiac SLC26A6 suggests important roles in regulating acid-base balance in the heart.
The studies in this article indicate that oxalate transport function of SLC26A6 is critically dependent on glycosylation and that exoglycosidase-mediated deglycosylation of SLC26A6 has the capacity to profoundly modulate SLC26A6 function.
This article reports that endogenous oestrogen upregulates the expressions and functional activities of CFTR and SLC26A6 in duodenal mucosa, which could contribute to the protection of the duodenum and explain the sex difference in the prevalence of duodenal ulcer.
Authors in this article demonstrate that deletion of SLC26A6 alters the apparent stoichiometry of apical Cl-/HCO3- exchange in the native pancreatic duct. The results of this article are consistent with SLC26A6 mediating 1:2 Cl-/HCO3- exchange, and the exchanger upregulated in its absence, most probably SLC26A3, mediating 2:1 exchange.
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