SLC26A9 is encoded by the SLC26A9 gene and is also known as Solute carrier family 26 member 9, Anion transporter/exchanger protein. It is a member of the SLC26 family of anion transporters with strong expression at apical and intracellular membranes of the lung and stomach. SLC26A9 is cloned on the basis of homology to other SLC26 isoforms. In humans, SLC26A9 maps to chromosome 1 and encodes a 791-amino-acid protein. SLC26A9 can function in three distinct modes, including electrogenic Cl-/HCO3- exchange, chloride channel, and sodium chloride cotransport.
|Basic Information of SLC26A9|
|Protein Name||Solute carrier family 26 member 9|
|Aliases||Anion transporter/exchanger protein 9|
|Organism||Homo sapiens (Human)|
SLC26A9 is abundantly expressed in the stomach and lung, with lower levels in the kidney. SLC26A9 can function in three distinct modes, including electrogenic Cl-/HCO3- exchange, chloride channel, and sodium chloride cotransport. In the stomach, SLC26A9 is located on the apical membrane of surface epithelial cells and in the tubulovesicles of gastric parietal cells and regulates gastric acid secretion. A recent study using SLC26A9 KO mice showed a significant reduction in renal chloride excretion compared with wild-type animals when fed a diet high in salt or when subjected to water deprivation. These results suggest that SLC26A9 has an important role in renal chloride/fluid excretion and arterial pressure regulation. It was proposed that impaired SLC26A9 activity in humans may interfere with the excretion of excess salt and result in hypertension. Meanwhile, SLC26A9 is reported to be a regulator of renal salt excretion and blood pressure and SLC26A9 predominantly functions as a chloride channel in medullary collecting duct cells.
Fig.1 A schematic diagram depicting the localization of SLC26A9 in the kidney. (Soleimani, 2013)
This article proposes that SLC26A9 predominantly functions as a chloride channel in medullary collecting duct cells because SLC26A9 deletion resulted in the complete loss of gastric acid secretion, indicating an essential role of this channel/transporter in gastric acid secretion.
This article reports that SLC26A9 functions as an anion conductance in the apical membranes of HBE cells. At the same time, SLC26A9 contributes to transepithelial chloride currents under basal and cAMP/protein kinase A-stimulated conditions, and its activity in HBE cells requires functional CFTR.
This article shows that the association of meconium ileus and SLC26A9 variants may be related to maldigestion and impaired downstream signaling caused by loss of upper GI tract digestive functions, aggravating the situation of lack of secretion and sticky mucus at the site of obstruction in cystic fibrosis intestine.
This article shows that the co-expression between SLC26A9 and F508del CFTR, and the co-expression trafficking defect leads to a PDZ motif-sensitive intracellular retention of SLC26A9.
The findings of this article indicate CFTR is required to the SLC26A9 airway modification at the cell surface. Meanwhile, the variants of SLC26A9 are important to respond to CFTR-directed therapeutics.
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