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IL13 increases pendrin abundance to the cell surface via Rho/actin signaling, an effect reversed by theophylline.
Results indicate that the variant G539R in the SLC26A6 gene is associated with kidney stone risk, providing a clear clue to further achieve insight into oxalate transport in kidney stone formation.
Results indicate the involvement of SLC26A6 along with SLC26A3 in transporting HCO3(-) essential for embryo cleavage, possibly working in concert with CFTR through a Cl(-) recycling pathway.
Endogenous oestrogen upregulates the expressions and functional activities of CFTR and SLC26A6 in duodenal mucosa.
IL-4 induces demethylation of specific CpG sites within the pendrin promoter. These epigenetic alterations are cell type specific, and may in part dictate pendrin mRNA transcription
Helicobacter pylori infection impairs the expressions and functional activities of duodenal mucosal bicarbonate transport proteins, CFTR and SLC26A6, which contributes to the development of duodenal ulcer.
Molecular dynamics simulations of the STAS domains of rat prestin and human pendrin 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 (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.
lysophosphatidic acid stimulates apical Cl(-)/OH(-) exchange activity and surface levels of SCL26A3 and SCL26A6 in intestinal epithelial cells
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.
No mutation was found in the coding regions and intron-exon boundaries of the genes for CA II, CA IV, CA XIV, kNCB1, NHE3, NHE8, NHRF1, NHRF2 and SLC26A6 amplified from genomic DNA of family members with pRTA.
Low extracellular Cl(-) affinity and electroneutrality of oxalate efflux characterizing human SLC26A6 explain the high human susceptibility to nephrolithiasis relative to mice. SLC26A6 sequence variant(s) are candidate risk modifiers for nephrolithiasis.
involvement of IRF-1 in the regulation of SLC26A6 gene expression by IFNgamma in the human intestine
SLC26A6 was effectively ruled out as the disease gene in this non-PH1/PH2 cohort. Phenotypic and functional analysis excluded a significant effect of identified variants on oxalate excretion.
Though the SLC26A6 206M polymorphism did not correlate with kidney stone development in primary hyperparathyroidism, PHPT stone-formers harbouring the M allele had a lower hypercalciuria
findings indicate that Slc26a6 is located at the apical membrane of salivary gland acinar cells, where it mediates Cl(-)/oxalate exchange and plays a critical role in the secretion of oxalate into saliva.
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 are novel participants in the extracellular transport of bicarbonate during enamel maturation.
expressed in ameloblasts but not alone critical for formation of dental enamel
Results suggest that PAT1 slows down APP 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.
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 in its absence, therefore mediating 2:1 exchange.
Data demonstrate functional Pat-1 Cl)/HCO3) exchange activity in the lower villus epithelium of the murine duodenum which, in previous studies, had been obscured by the inclusion of luminal glucose as a metabolic substrate.
This study showed a functionally active CFTR is an absolute requirement for Slc26-mediated duodenal bicarbonate secretion, but not for Slc26-mediated fluid absorption.
study concludes Pat-1 Cl(-)/HCO(3)(-) exchange contributes to pH(i) regulation in the duodenal villous epithelium during H(+)-dipeptide absorption, possibly by providing a HCO(3)(-) import pathway
mediates specificity of anion exchange
An anion transporter expressed on the apical surface of renal proximal tubule cells and capable of mediating Cl(-)-formate exchange.
encodes an apical Cl(-)/formate/oxalate and Cl(-)/base exchanger and reveals significant mechanistic differences between apical and basolateral oxalate exchangers of the proximal tubule
The regulation of SLC26A6 in response to stimulation of the alpha1a adrenergic receptor is reported.
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.
anion transporter 1
, pendrin L1
, solute carrier family 26 member 6
, solute carrier family 26, member 6
, sulfate anion transporter
, SLC26A6a anion exchanger