Effects of Cys Mutation on Taurocholic Acid Transport by Mouse Ileal and Hepatic Sodium-dependent Bile Acid Transporters

2002 ◽  
Vol 66 (2) ◽  
pp. 467-470 ◽  
Author(s):  
Tohru SAEKI ◽  
Toshinori KURODA ◽  
Makiko MATSUMOTO ◽  
Ryuhei KANAMOTO ◽  
Kimikazu IWAMI
Keyword(s):  
Bile Acid ◽  
Taurocholic Acid ◽  
Acid Transport ◽  
Bile Acid Transporters ◽  
Sodium Dependent

Enterobacteria Modulate Intestinal Bile Acid Transport and Homeostasis through Apical Sodium-Dependent Bile Acid Transporter (SLC10A2) Expression

2010 ◽  
Vol 336 (1) ◽  
pp. 188-196 ◽  
Author(s):  
Masaaki Miyata ◽  
Hiroki Yamakawa ◽  
Mayumi Hamatsu ◽  
Hideaki Kuribayashi ◽  
Yuki Takamatsu ◽  
...  
Keyword(s):  
Bile Acid ◽  
Acid Transport ◽  
Bile Acid Transport ◽  
Sodium Dependent ◽  
Bile Acid Transporter ◽  
Acid Transporter

Effect of olsalazine on sodium-dependent bile acid transport in rat ileum

1995 ◽  
Vol 40 (5) ◽  
pp. 943-948 ◽  
Author(s):  
Anupama Chawla ◽  
Peter I. Karl ◽  
Rosandra N. Reich ◽  
Gopal Narasimhan ◽  
Gregory A. Michaud ◽  
...  
Keyword(s):  
Bile Acid ◽  
Acid Transport ◽  
Rat Ileum ◽  
Bile Acid Transport ◽  
Sodium Dependent

scholarly journals A novel bioluminescence-based method to investigate uptake of bile acids in living cells

2018 ◽  
Vol 315 (4) ◽  
pp. G529-G537 ◽  
Author(s):  
Alexander L. Ticho ◽  
Hyunjin Lee ◽  
Ravinder K. Gill ◽  
Pradeep K. Dudeja ◽  
Seema Saksena ◽  
...  
Keyword(s):  
Bile Acid ◽  
Bile Acids ◽  
Real Time ◽  
Sodium Taurocholate ◽  
In Vivo Studies ◽  
Dependent Manner ◽  
Bile Acid Transporters ◽  
Sodium Dependent ◽  
Bile Acid Transporter ◽  
Acid Transporter

Bile acid transporters, including the ileal apical sodium-dependent bile acid transporter (ASBT) and the hepatic sodium-taurocholate cotransporting polypeptide (NTCP), are crucial for the enterohepatic circulation of bile acids. Our objective was to develop a method for measuring bile acid transporter activity in real time to precisely evaluate rapid changes in their function. We designed a reporter system relying on a novel probe: cholic acid attached to luciferin via a disulfide-containing, self-immolating linker (CA-SS-Luc). Incubation of human embryonic kidney-293 cells coexpressing luciferase and ASBT with different concentrations of CA-SS-Luc (0.01–1 μM) resulted in bioluminescence with an intensity that was concentration- and time-dependent. The bioluminescence measured during incubation with 1 μM CA-SS-Luc was dependent on the levels of ASBT or NTCP expressed in the cells. Coincubation of CA-SS-Luc with natural bile acids enhanced the bioluminescence in a concentration-dependent manner with kinetic parameters for ASBT similar to those previously reported using conventional methods. These findings suggest that this method faithfully assesses ASBT function. Further, incubation with tyrosine phosphatase inhibitor III (PTPIII) led to significantly increased bioluminescence in cells expressing ASBT, consistent with previous studies showing an increase in ASBT function by PTPIII. We then investigated CA-SS-Luc in isolated mouse intestinal epithelial cells. Ileal enterocytes displayed significantly higher luminescence compared with jejunal enterocytes, indicating a transport process mediated by ileal ASBT. In conclusion, we have developed a novel method to monitor the activity of bile acid transporters in real time that has potential applications both for in vitro and in vivo studies.NEW & NOTEWORTHY This article reports the development of a real-time method for measuring the uptake of bile acids using a bioluminescent bile acid-based probe. This method has been validated for measuring uptake via the apical sodium-dependent bile acid transporter and the sodium-taurocholate cotransporting polypeptide in cell culture and ex vivo intestinal models.

scholarly journals SBS- Associated Liver Disease: Fatty Liver and Altered Bile Acid Transport in the Small Intestine but No Change in Bile Acid Transporters Within the Liver

2011 ◽  
Vol 140 (5) ◽  
pp. S-171
Author(s):  
Prue M. Pereira-Fantini ◽  
Sarah Thomas ◽  
Guin Wilson ◽  
Winita Hardikar ◽  
Peter Fuller ◽  
...  
Keyword(s):  
Small Intestine ◽  
Liver Disease ◽  
Bile Acid ◽  
Fatty Liver ◽  
Acid Transport ◽  
Bile Acid Transport ◽  
Bile Acid Transporters

Na(+)-dependent bile acid transport by hepatocytes is mediated by a protein similar to microsomal epoxide hydrolase

1993 ◽  
Vol 264 (3) ◽  
pp. G528-G534 ◽  
Author(s):  
P. Von Dippe ◽  
M. Amoui ◽  
C. Alves ◽  
D. Levy
Keyword(s):  
Plasma Membrane ◽  
Bile Acid ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Epoxide Hydrolase ◽  
Sodium Dodecyl ◽  
Microsomal Epoxide Hydrolase ◽  
Acid Transport ◽  
Bile Acid Transport ◽  
Sodium Dependent

A protein mediating hepatocyte sodium-dependent bile acid transport across the sinusoidal plasma membrane has been purified by immunoprecipitation with monoclonal antibody (MAb) 25D-1, which specifically recognizes this protein on the surface of intact hepatocytes (Ananthanarayanan et al. J. Biol. Chem. 263: 8338-8343, 1988). The function of this protein was further established by proteoliposome reconstitution (von Dippe et al. J. Biol. Chem. 265: 14812-14816, 1990). NH2-terminal amino acid sequence analysis and amino acid composition revealed this protein to be closely related to the enzyme microsomal epoxide hydrolase (mEH). Both proteins exhibited the same elution times on a reverse-phase high-pressure liquid chromatography column, comigrated with an apparent molecular weight of 49,000 as measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and possessed identical isoelectric points of 8.2. The MAb was capable of immunoprecipitating chromatographically purified mEH, as well as a protein derived from the sinusoidal plasma membrane that exhibited mEH activity comparable to that of the protein isolated from the endoplasmic reticulum. The subtilisin fragmentation patterns derived from chromatographically purified mEH and the MAb-precipitated plasma membrane protein were also identical. Hydropathy profile analysis of the amino acid sequence of mEH suggested the presence of four transmembrane domains. The results of these studies indicate that a protein that is involved in mediating sodium-dependent bile acid transport is closely related to mEH.

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