Hepatobiliary elimination of the peroxisome proliferator nafenopin by conjugation and subsequent atp-dependent transport across the canalicular membrane

1994 ◽  
Vol 48 (6) ◽  
pp. 1113-1120 ◽  
Author(s):  
Gabriele Jedlitschky ◽  
Inka Leier ◽  
Matthias Böhme ◽  
Ulrike Buchholz ◽  
Jacob Bar-Tana ◽  
...  
Keyword(s):  
Peroxisome Proliferator ◽  
Canalicular Membrane ◽  
Dependent Transport ◽  
Hepatobiliary Elimination

ATP-dependent transport of beta-estradiol 17-(beta-D-glucuronide) in rat canalicular membrane vesicles

1996 ◽  
Vol 271 (5) ◽  
pp. G791-G798
Author(s):  
M. Vore ◽  
T. Hoffman ◽  
M. Gosland
Keyword(s):  
Bile Acid ◽  
Transport System ◽  
Organic Anion ◽  
Membrane Vesicles ◽  
Anion Transport ◽  
Organic Anion Transport ◽  
Canalicular Membrane ◽  
P Glycoprotein ◽  
Anion Transport System ◽  
Dependent Transport

The ATP-dependent transport of beta-estradiol 17-(beta-D-glucuronide) (E217G), a cholestatic metabolite of estradiol, was investigated in rat liver canalicular membrane vesicles. ATP-dependent transport was dependent on time and temperature and occurred into an osmotically sensitive space; kinetic analysis indicated a saturable transport system (Michaelis-Menten constant value, 75 microM; maximum transport rate, 598 pmol.min-1.mg protein-1). The steroid conjugates estradiol glucuronide, estriol 3-glucuronide, estriol 16 alpha-glucuronide, testosterone glucuronide, and the three-sulfate conjugate of 17G were effective inhibitors of transport. Bromosulfophthalein, S-(2,4-dinitrophenyl)glutathione, and glutathione disulfide, all substrates of the canalicular ATP-dependent non-bile acid organic anion transport system, were also effective inhibitors, whereas taurocholate had no effect on transport. Conversely, E217G inhibited the ATP-dependent transport of S-(2,4-dinitrophenyl)glutathione. Daunorubicin, vinblastine, etoposide, cyclosporin, and PSC-833, substrates/modulators of P-glycoprotein, were also potent inhibitors of E217G transport, and E217G competitively inhibited the ATP-dependent transport of daunorubicin. C219, a monoclonal antibody against P-glycoprotein, inhibited ATP-dependent transport of E217G and daunorubicin but not of taurocholate or S-(2,4-dinitrophenyl)glutathione. These data indicate that E217G is substrate of both the non-bile acid organic anion transport system and P-glycoprotein but not of the ATP-dependent bile acid transport system in canalicular membranes.

scholarly journals ATP-dependent transport of taurocholate across the hepatocyte canalicular membrane mediated by a 110-kDa glycoprotein binding ATP and bile salt.

1991 ◽  
Vol 266 (28) ◽  
pp. 18920-18926 ◽  
Author(s):  
M. Müller ◽  
T. Ishikawa ◽  
U. Berger ◽  
C. Klünemann ◽  
L. Lucka ◽  
...  
Keyword(s):  
Bile Salt ◽  
Canalicular Membrane ◽  
Dependent Transport

scholarly journals ATP-dependent transport of amphiphilic cations across the hepatocyte canalicular membrane mediated bymdr1P-glycoprotein

FEBS Letters ◽  
1994 ◽  
Vol 343 (2) ◽  
pp. 168-172 ◽  
Author(s):  
Michael Müller ◽  
Rosmarie Mayer ◽  
Ulrike Hero ◽  
Dietrich Keppler
Keyword(s):  
Canalicular Membrane ◽  
Dependent Transport

Regulation and translocation of ATP-dependent apical membrane proteins in rat liver

1997 ◽  
Vol 272 (5) ◽  
pp. G1041-G1049 ◽  
Author(s):  
Z. C. Gatmaitan ◽  
A. T. Nies ◽  
I. M. Arias
Keyword(s):  
Leucine Aminopeptidase ◽  
Specific Activity ◽  
Membrane Vesicles ◽  
Transport Proteins ◽  
Transport Processes ◽  
Western Blots ◽  
Canalicular Membrane ◽  
Transport Studies ◽  
Bile Canalicular Membrane ◽  
Dependent Transport

The bile canalicular membrane contains four specific ATP-dependent transport processes that are involved in secretion of bile acids, non-bile acid organic anions (mrp1), phospholipids (mdr2), and organic cations (mdr3). The aim of this study was to determine how the canalicular presence of these transport proteins is regulated. Canalicular membrane vesicles (CMV) were prepared from livers of rats treated with taurocholate (TC) and/or dibutyryl-adenosine 3',5'-cycle monophosphate (DBcAMP) with and without pretreatment with colchicine. Transport studies were performed with radiolabeled substrates. Changes in the relative amounts of transport proteins were determined by Western blots. Compared with controls, the specific activity of each of the transport processes was enhanced 1.5- and 3-fold with TC and DBcAMP treatments, respectively. Western blots revealed the same increases with mdr2 and mdr3. Pretreatment of rats with colchicine prevented these responses fully with TC treatment, whereas only partial prevention was obtained with DBcAMP treatment. Besides the ATP-dependent transporters, the relative specific activities of the canalicular membrane ectoenzyme markers, leucine aminopeptidase and gamma-glutamyltranspeptidase, were also affected the same way. These results suggest that TC and DBcAMP increase the specific activity of the canalicular ATP-dependent transport proteins and some canalicular membrane ectoenzymes by stimulating an increase in the relative amounts of these proteins in the membrane.

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