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Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. De plus, nous expédions Organic Solute Transporter alpha Anticorps (27) et Organic Solute Transporter alpha Kits (5) et beaucoup plus de produits pour cette protéine.
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SLC51A expression is significantly upregulated in human masticatory mucosa during wound healing
Hepatic OSTalpha-OSTbeta (Montrer OSTBETA Protéines) expression is induced by hypoxia.
Ostbeta (Montrer OSTBETA Protéines) is required for both proper trafficking of Ostalpha and formation of the functional transport unit, and identify specific residues of Ostbeta (Montrer OSTBETA Protéines) critical for these processes.
The present report summarizes the evidence for a pleiotropic role of Ostalpha-Ostbeta (Montrer OSTBETA Protéines) in different tissues.
OSTalpha has roles in biological transport and is widely expressed in human tissues
overexpression of hu (Montrer OSTBETA Protéines)man OSTalpha and OSTbeta facilitated the uptake of conjugated chenodeoxycholate (Montrer NR1H4 Protéines) and the activation of FXR target genes
OSTalpha/OSTbeta (Montrer OSTBETA Protéines) expression is induced by bile acids through ligand-dependent transactivation of both OST (Montrer DDOST Protéines) genes by the nuclear bile acid receptor (Montrer NR1H4 Protéines)/farnesoid X receptor (Montrer xpr1 Protéines) (FXR (Montrer NR1H4 Protéines)).
the selective localization of OSTalpha and OSTbeta (Montrer OSTBETA Protéines) to the basolateral plasma membrane of epithelial cells responsible for bile acid and sterol reabsorption.
These results indicate that expression of Ostalpha and Ostbeta (Montrer OSTBETA Protéines) are highly regulated in response to cholestasis and that this response is dependent on the FXR bile acid receptor (Montrer NR1H4 Protéines).
Demonstrate association of OST-alpha and OST-beta (Montrer OSTBETA Protéines) to determine trafficking to plasma membrane and activity.
Data suggest that transport of bile acid taurocholate is retained when OstB (organic solute transporter beta subunit (Montrer OSTBETA Protéines)) is truncated to contain only the transmembrane domain with 15 additional residues on each side and co-expressed with intact OstA; shorter fragments of OstB (Montrer OSTBETA Protéines) are inactive.
These findings indicate that loss of OSTalpha protects against age-related weight gain and insulin (Montrer INS Protéines) resistance.
Ileal FGF15 expression was directly correlated with plasma cholesterol levels and aortic cholesterol content. In contrast, plasma and hepatic cholesterol levels and atherosclerosis development were not reduced in apoE (Montrer APOE Protéines)(-/-) mice deficient in Ostalpha.
Total ileal FGF15 expression was elevated almost 20-fold in Ostalpha(-/-) mice as a result of increased villus epithelial cell number and ileocyte FGF15 protein expression
Inactivation of FXR (Montrer NR1H4 Protéines) largely unmasked the bile acid malabsorption phenotype and corrected the bile acid homeostasis defect in Ostalpha null mice.
Ostalpha-deficient mice efficiently eliminate excess bile acids via the feces.
OSTalpha is localized to steroidogenic cells of the brain and adrenal gland, and it modulates DHEA/DHEAS (Montrer SULT2A1 Protéines) homeostasis
These findings indicate that loss of Ostalpha provides protection from liver injury in obstructive cholestasis through adaptive responses in both the kidney and liver that enhance clearance of bile acids into urine.
Co-expression of mouse Ostalpha-Ostbeta (Montrer OSTBETA Protéines), but not the individual subunits, stimulated Na(+)-independent bile acid uptake and the apical-to-basolateral transport of taurocholate
OSTalpha and OSTbeta (Montrer OSTBETA Protéines) mRNA levels were induced in the adrenals and kidneys of wild-type, but not FXR (Montrer NR1H4 Protéines)-/-, mice
Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. Efficiently transports the major species of bile acids (By similarity).
organic solute transporter alpha
, organic solute transporter subunit alpha
, organic solute transporter, alpha subunit
, solute carrier family 51 subunit alpha