1991-12-01

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Hepatocellular bile salt uptake is mediated predominantly by the Na + -taurocholate cotransport proteins Ntcp (rodents) and NTCP (humans) and by the Na + -independent organic anion-transporting polypeptides Oatp1, Oatp2, and Oatp4 (rodents) and OATP-C (humans). After diffusion (bound by intracellular bile salt–binding proteins) to the canalicular

To this end, NTCP was precipitated 2021-01-20 Sodium/bile acid cotransporter also known as the Na + - taurocholate cotransporting polypeptide (NTCP) or liver bile acid transporter (LBAT) is a protein that in humans is encoded by the SLC10A1 (solute carrier family 10 member 1) gene. The importance of membrane voltage in uptake of bile salts into hepatocytes is not known. Electrogenicity of the primary bile salt transport process, Na-bile salt cotransport, has been difficult to determine because the large K and Cl conductances of the sinusoidal membrane (GK and GCl, respectively) obscure any transport associated currents. Bile salts are the major organic solutes in bile and undergo extensive enterohepatic circulation. Hepatocellular bile salt uptake is mediated predominantly by the Na(+)-taurocholate cotransport proteins Ntcp (rodents) and NTCP (humans) and by the Na(+)-independent organic anion-transporting polypept …. Bile salts are the major organic solutes in It has been proposed that the hepatocellular Na (+)-dependent bile salt uptake system exhibits a broad substrate specificity in intact hepatocytes. In contrast, recent expression studies in mammalian cell lines have suggested that the cloned rat liver Na (+)-taurocholate cotransporting polypeptide (Ntcp) may transport only taurocholate.

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The importance of membrane voltage in uptake of bile salts into hepatocytes is not known. Electrogenicity of the primary bile salt transport process, Na-bile salt cotransport, has been difficult to determine because the large K and Cl conductances of the sinusoidal membrane (GK and GCl, respectively) obscure any transport associated currents. Hepatocellular bile salt uptake is mediated predominantly by the Na(+)-taurocholate cotransport proteins Ntcp (rodents) and NTCP (humans) and by the Na(+)-independent organic anion-transporting polypeptides Oatp1, Oatp2, and Oatp4 (rodents) and OATP-C (humans). After diffusion (bound by intracellular bile salt-binding proteins) to the canalicular membrane, monoanionic bile salts are secreted into bile canaliculi by the bile salt export pump Bsep (rodents) or BSEP (humans). The pre-S1 domain of the large HBsAg protein promotes attachment and entry of HBV into the hepatocyte via liver cell–specific receptor recently identified as Na (sodium) taurocholate cotransporting polypeptide (NTCP), which is an integral membrane protein used in bile acid transport. 23,24 There is evidence that hepatocyte entry may be a multistep process including binding to heparan sulfate proteoglycans, 25 which are found on a variety of cells, and clathrin-mediated endocytosis. 26 The SLC10 family of sodium/bile salt cotransporters contains over 50 members in animal, plant and bacterial species.

It has been proposed that the hepatocellular Na(+)-dependent bile salt uptake system exhibits a broad substrate specificity in intact hepatocytes. In contrast, recent expression studies in mammalian cell lines have suggested that the cloned rat liver Na(+)-taurocholate cotransporting polypeptide (Ntcp) may transport only taurocholate.

Results: LPS caused gene expression bile salt transporter (Ntcp) has been cloned.7 In addition, of the hepatocyte basolateral sodium-dependent tauro-the electrochemical … Hepatocellular bile salt uptake is mediated predominantly by the Na + -taurocholate cotransport proteins Ntcp (rodents) and NTCP (humans) and by the Na + -independent organic anion-transporting polypeptides Oatp1, Oatp2, and Oatp4 (rodents) and OATP-C (humans). After diffusion (bound by intracellular bile salt–binding proteins) to the canalicular 1991-12-01 These results suggest that the proteins involved in Na + /bile salt cotransport are similar in renal and ileal brush-border membranes, but differ from those in hepatocytes. The system operates by a sodium ion cotransport mechanism, and it functions in maintaining a normal enterohepatic circulation of bile salts.

Na bile salt cotransport

1 ways to abbreviate Na(+)-bile Salt Co-transporter. How to abbreviate Na(+)-bile Salt Co-transporter? Get the most popular abbreviation for Na(+)-bile Salt Co-transporter updated in 2021

Get the most popular abbreviation for Na(+)-bile Salt Co-transporter updated in 2021 bile salt carriers, membranelipid compositionandflu-idity are also majordeterminants of bile salt excretion (15, 16).

Na bile salt cotransport

SLC10A1 (sodium taurocholate cotransporting polypeptide [NTCP]) and SLC10A2 (apical sodium-dependent bile salt transporter [ASBT]) transport bile salts and play an important role in maintaining enterohepatic circulation of bile salts. Na+-dependent bile salt transport system in the hepatocytes of the adult lamprey, with a very low affinity for TCA (K m = 115 ± 8.7 µM). This is strikingly different from previous observations in isolated hepatocytes from skate and rainbow trout1,2 that appear to lack a Na+-dependent TCA transporter. 2000-04-01 · In addition to sodium/bile salt cotransport, sodium-independent bile salt transport pathways are also present at the basolateral plasma membranes of hepatocytes (8, 9, 11). These sodium-independent bile salt uptake systems have been less well characterized compared with the sodium-coupled uptake carrier, a fact that is reflected by the broad range of reported apparent K m values between 9 and However, both stomatin overexpression and knockdown increased NTCP-mediated taurocholate uptake while NTCP abundance at the plasma membrane was only increased in stomatin depleted cells. These findings identify stomatin as an interactor of NTCP and show that the interaction modulates bile salt transport.
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A cDNA encoding the rat liver bile acid uptake system has been isolated by expression cloning in Xenopus laevis oocytes. The cloned transporter is strictly sodium-dependent and can be inhibited by various non-bile-acid organic compounds. 1989-07-01 · Whether these discrepancies can be explained by a more complex model of Na*- coupled bile salt cotransport such as, for example, (Na"*')2 Cl'/bile acid symport [2] requires further ex- perimentation. Interestingly, however; the presence of chloride is an impci iciiit requirement for maximal Na^dependent bile salt uptake rates being observed in isolated vesicles [9] as well as in isolated It has been proposed that the hepatocellular Na(+)-dependent bile salt uptake system exhibits a broad substrate specificity in intact hepatocytes. In contrast, recent expression studies in mammalian cell lines have suggested that the cloned rat liver Na(+)-taurocholate cotransporting polypeptide (Ntcp) may transport only taurocholate.

Pflugers  porting polypeptide (NTCP), the bile salt export pump. (BSEP), the apical sinusoidal membrane by the Na + taurocholate cotransport- ing polypeptide with   They are related to the human bile acid:sodium symporters (TC 2.A.28) functioning in the liver in the uptake of bile acids from portal blood plasma, a process mediated by the co-transport of Na+ Indriolo E, Na G, Ellis D, Salt DE, Bile secretion depends on the function of membrane transport systems in hepatocytes and cholangiocytes and on K14341, solute carrier family 10 ( sodium/bile acid cotransporter), member 1 K11822, bile-salt sulfotransferase [ EC:2.8.
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Hepatocellular bile salt uptake is mediated predominantly by the Na + -taurocholate cotransport proteins Ntcp (rodents) and NTCP (humans) and by the Na + -independent organic anion-transporting polypeptides Oatp1, Oatp2, and Oatp4 (rodents) and OATP-C (humans). After diffusion (bound by intracellular bile salt–binding proteins) to the canalicular membrane, monoanionic bile salts are secreted into bile canaliculi by the bile salt export pump Bsep (rodents) or BSEP (humans).

Na(+)-independent uptake of bile salts is mediated by the organic anion transporting polypeptides, a superfamily of multispecific bile salt and amphipathic substrate transporters. Sodium/bile acid cotransporter 7 From Wikipedia, the free encyclopedia Sodium/bile acid cotransporter 7 is a protein which in humans is encoded by the SLC10A7 gene. Methods: mRNA levels (real time PCR) and protein expression (immunofluorescence microscopy) were investigated for the Na(+)-taurocholate cotransport protein (Ntcp), the organic anion transporting polypeptides (Oatp1a1, Oatp1a4, Oatp1b2), the multidrug resistance associated proteins (Mrp2, Mrp6) and the bile salt export pump (Bsep).


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One example is the SLC12A1, a Na-K-Cl-cotransporter that mediates active reabsorption of SLC10 The sodium bile salt cotransport family. 7.

SLC10A1 (sodium taurocholate cotransporting polypeptide [NTCP]) and SLC10A2 (apical sodium-dependent bile salt transporter [ASBT]) transport bile salts and play an important role in maintaining enterohepatic circulation of bile salts. Na+-dependent bile salt transport system in the hepatocytes of the adult lamprey, with a very low affinity for TCA (K m = 115 ± 8.7 µM). This is strikingly different from previous observations in isolated hepatocytes from skate and rainbow trout1,2 that appear to lack a Na+-dependent TCA transporter. 2000-04-01 · In addition to sodium/bile salt cotransport, sodium-independent bile salt transport pathways are also present at the basolateral plasma membranes of hepatocytes (8, 9, 11). These sodium-independent bile salt uptake systems have been less well characterized compared with the sodium-coupled uptake carrier, a fact that is reflected by the broad range of reported apparent K m values between 9 and However, both stomatin overexpression and knockdown increased NTCP-mediated taurocholate uptake while NTCP abundance at the plasma membrane was only increased in stomatin depleted cells. These findings identify stomatin as an interactor of NTCP and show that the interaction modulates bile salt transport. petromyzonol sulfate (its endogenous bile salt) with high affinity, but taurocholate with low affinity.