scholarly journals The Functional Expression of Sodium-dependent Bile Acid Transport in Madin-Darby Canine Kidney Cells Transfected with the cDNA for Microsomal Epoxide Hydrolase

1996 ◽  
Vol 271 (30) ◽  
pp. 18176-18180 ◽  
Author(s):  
Patricia von Dippe ◽  
Mehran Amoui ◽  
Robert H. Stellwagen ◽  
Daniel Levy
Keyword(s):  
Bile Acid ◽  
Epoxide Hydrolase ◽  
Functional Expression ◽  
Microsomal Epoxide Hydrolase ◽  
Kidney Cells ◽  
Acid Transport ◽  
Madin Darby Canine Kidney ◽  
Sodium Dependent ◽  
Darby Canine Kidney ◽  
Canine Kidney

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.

scholarly journals Inhibition by brefeldin A of protein secretion from the apical cell surface of Madin-Darby canine kidney cells.

1991 ◽  
Vol 266 (27) ◽  
pp. 17729-17732 ◽  
Author(s):  
S.H. Low ◽  
S.H. Wong ◽  
B.L. Tang ◽  
P. Tan ◽  
V.N. Subramaniam ◽  
...  
Keyword(s):  
Cell Surface ◽  
Protein Secretion ◽  
Apical Cell ◽  
Brefeldin A ◽  
Kidney Cells ◽  
Madin Darby Canine Kidney ◽  
Darby Canine Kidney ◽  
Canine Kidney
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