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The protein encoded by SLC26A3 is a transmembrane glycoprotein that transports chloride ions across the cell membrane in exchange for bicarbonate ions. Additionally we are shipping SLC26A3 Antibodies (16) and SLC26A3 Kits (1) and many more products for this protein.
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We report the first Tunisian case of SLC26A3 gene mutation in congenital chloride diarrhea. Our patient was homozygous for G187X mutation. Both parents were heterozygous for the same mutation.
Expression of NHE3 and DRA was reduced with high tacrolimus levels and impaired renal function after intestinal transplantation.
A variety of mutations in SLC26A3 are responsible for CCD (show RUNX2 Proteins). A total of 55 mutations in SLC26A3 have been reported
Data demonstrate an upregulation of SLC26A3 via activation of the ERK1/2 pathway that may underlie potential antidiarrheal effects of Bifidobacterium sp.
Efficacy of lactobacillus acidophilus or its secreted soluble factors in alleviating inflammation and inflammation-associated dysregulation of DRA activity could justify their therapeutic potential in inflammatory diarrheal diseases.
The SLC26A3-NHERF4 (show PDZD3 Proteins) interaction was modulated by phosphorylation; serine 329 of NHERF4 (show PDZD3 Proteins)-PDZ3 played a critical role in modulating binding selectivity.
few patients develop illnesses because of SLC26A3 mutations.
Slc26a3 contributes to sulfate secretion via DIDS-senstive bicarbonate-sulfate exchange in addition to being the principal DIDS-resistant chloride-bicarbonate exchanger (show SLC4A2 Proteins).
these data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
Data from pediatric patients with congenital chloride diarrhea identifies 7 novel mutations in SLC26A3, including 3 missense changes of highly conserved residues.
DRA surface expression was reduced partly via an increase in DRA endocytosis and a decrease in exocytosis
Both PAT-1 and DRA significantly contribute to intestinal fluid absorption and enterocyte acid/base balance but are activated by different ion gradients.
Data indicate that solute carrier (show SERTAD2 Proteins) family 26, member 3 protein (Slc26a3) is expressed in male reproductive tract, and its expression pattern is related to the function.
Deletion of DRA results in severely reduced colonic HCO3 (-) secretory rate, a loss of colonic fluid absorption, a lack of a firmly adherent mucus layer and a severely reduced colonic mucosal resistance to dextran sodium sulphate damage.
DRA mediates a predominance of the apical uptake of oxalate and Cl(-) absorbed in the small and large intestine of mice under short-circuit conditions.
Endogenous and recombinant human/mouse Slc26a3 do not exhibit electrogenic 2Cl-/1HCO- exchange. Acute induction of Slc26a3 Cl-/HCO3- exchange is associated with secondary membrane potential changes representing homeostatic responses.
This study showed a functionally active CFTR (show CFTR Proteins) is an absolute requirement for Slc26-mediated duodenal bicarbonate secretion, but not for Slc26-mediated fluid absorption.
demonstrate that the double-mutant mice present with a defect in intestinal water absorption and that Hnf1alpha (show HNF1A Proteins) and beta directly control the expression of Slc26a3.
The protein encoded by this gene is a transmembrane glycoprotein that transports chloride ions across the cell membrane in exchange for bicarbonate ions. It is localized to the mucosa of the lower intestinal tract, particularly to the apical membrane of columnar epithelium and some goblet cells. The protein is essential for intestinal chloride absorption, and mutations in this gene have been associated with congenital chloride diarrhea.
solute carrier family 26, member 3
, down-regulated in adenoma protein
, chloride anion exchanger-like
, chloride anion exchanger
, down-regulated in adenoma
, solute carrier family 26 member 3
, down-regulated in adenoma DRA