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Endogenous oestrogen upregulates the expressions and functional activities of CFTR (show CFTR Proteins) and SLC26A6 in duodenal mucosa.
IL-4 (show IL4 Proteins) induces demethylation of specific CpG sites within the pendrin (show SLC26A4 Proteins) promoter. These epigenetic alterations are cell type specific, and may in part dictate pendrin (show SLC26A4 Proteins) mRNA transcription
Helicobacter pylori infection impairs the expressions and functional activities of duodenal mucosal bicarbonate transport proteins, CFTR (show CFTR Proteins) and SLC26A6, which contributes to the development of duodenal ulcer.
Molecular dynamics simulations of the STAS domains of rat prestin (show SLC26A5 Proteins) and human pendrin (show SLC26A4 Proteins) reveal conformational motions in conserved flexible regions.
Data show that SLC26A6 variants do not alter the risk for the development of chronic pancreatitis.
In the intestinal epithelium, PAT-1 (show APPBP2 Proteins) (SLC26A6) could mediate apical oxalate influx or apical oxalate efflux depending on the magnitude and direction prevailing counterion driver gradients as well as the relative affinities of the transported anions.
orthologous mouse and human SLC26A6 proteins differ in anion selectivity, transport mechanism, and acute regulation, but both mediate electroneutral Cl(-)/HCO(3)(-) exchange
In human kidney SLC26A6 and A7 have a distinct, partially overlapping expression in distal segments of nephrons. The distribution partly differs from that found previously in rodent kidneys.
findings indicate that slc26a6 functions as a coupled 1Cl-/2HCO3- exchanger
Mouse Slc26a6 and human SLC26A6 each mediated electroneutral Cl-/HCO3- and Cl-/OH- exchange. But, whereas Cl-/oxalate exchange by mouse Slc26a6 was electrogenic, that mediated by human SLC26A6 appeared electroneutral.
Slc26a6 is a unique cardiac electrogenic Cl(-)/HCO3(-) transporter in ventricular myocytes, which has roles in regulating pHi, excitability, and contractility.
This study showed that transepithelial sulfate fluxes across the mouse distal ileum demonstrating that DRA (and to a lesser extent, PAT1) secretes sulfate with significant implications for intestinal sulfate absorption and overall homeostasis.
Enzymatic deglycosylation of SLC26A6 expressed on the plasma membrane of intact cells strongly reduced oxalate transport activity.
Slc26a1, Slc26a6 and Slc26a7 (show SLC26A7 Proteins) are novel participants in the extracellular transport of bicarbonate during enamel maturation.
Results suggest that PAT1 (show APPBP2 Proteins) slows down APP (show APP Proteins) trafficking to the cell surface in primary cortical neurons
Both PAT-1 and DRA significantly contribute to intestinal fluid absorption and enterocyte acid/base balance but are activated by different ion gradients.
Cardiac myocytes express different isoforms of Slc26a6, which encode electrogenic Cl(-)/HCO3(-) and Cl(-)/oxalate exchangers.
Slc26a6-null mice exhibited increased renal and intestinal sodium-dependent succinate uptake, as well as urinary hyperoxaluria and hypocitraturia, but no change in urinary pH, indicating enhanced transport activity of NaDC-1 (show SLC13A2 Proteins).
NMR and CE were used to characterize the urinary metabolome in slc26a6 null mice. Clear metabolic differentiation between the urinary profiles of the slc26a6 null and the wild type mice were observed using both methods.
SLC26A6 mediates 1:2 Cl-/HCO3- exchange, and the exchanger most probably upregulates SLC26A3 (show SLC26A3 Proteins) in its absence, therefore mediating 2:1 exchange.
This gene belongs to the solute carrier 26 family, whose members encode anion transporter proteins. This particular family member encodes a protein involved in transporting chloride, oxalate, sulfate and bicarbonate. Several alternatively spliced transcript variants of this gene, encoding distinct isoforms, have been described, but the full-length nature of some of these variants has not been determined.
solute carrier family 26, member 6
, solute carrier family 26 member 6
, SLC26A6a anion exchanger
, anion transporter 1
, pendrin L1
, sulfate anion transporter