Kupffer cells alter organic anion transport through multidrug resistance protein 2 in the post-cold ischemic rat liver

Hepatology ◽  
2004 ◽  
Vol 39 (4) ◽  
pp. 1099-1109 ◽  
Author(s):  
Atsushi Kudo ◽  
Satoshi Kashiwagi ◽  
Mayumi Kajimura ◽  
Yasunori Yoshimura ◽  
Koji Uchida ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Rat Liver ◽  
Kupffer Cells ◽  
Organic Anion ◽  
Anion Transport ◽  
Multidrug Resistance Protein ◽  
Organic Anion Transport ◽  
Multidrug Resistance Protein 2 ◽  
Resistance Protein

scholarly journals Anthracyclines modulate multidrug resistance protein (MRP) mediated organic anion transport

1997 ◽  
Vol 1326 (1) ◽  
pp. 12-22 ◽  
Author(s):  
Marc Heijn ◽  
Jan H Hooijberg ◽  
George L Scheffer ◽  
Gabór Szabó ◽  
Hans V Westerhoff ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Organic Anion ◽  
Anion Transport ◽  
Multidrug Resistance Protein ◽  
Organic Anion Transport ◽  
Resistance Protein

scholarly journals Regorafenib Is Transported by the Organic Anion Transporter 1B1 and the Multidrug Resistance Protein 2

2015 ◽  
Vol 38 (4) ◽  
pp. 582-586 ◽  
Author(s):  
Hiroki Ohya ◽  
Yoshihiko Shibayama ◽  
Jiro Ogura ◽  
Katsuya Narumi ◽  
Masaki Kobayashi ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Organic Anion ◽  
Organic Anion Transporter ◽  
Multidrug Resistance Protein ◽  
Multidrug Resistance Protein 2 ◽  
Anion Transporter ◽  
Resistance Protein

scholarly journals Cyclic AMP stimulates sorting of the canalicular organic anion transporter (Mrp2/cMoat) to the apical domain in hepatocyte couplets

1998 ◽  
Vol 111 (8) ◽  
pp. 1137-1145 ◽  
Author(s):  
H. Roelofsen ◽  
C.J. Soroka ◽  
D. Keppler ◽  
J.L. Boyer
Keyword(s):  
Apical Membrane ◽  
Organic Anion ◽  
Anion Transport ◽  
Transport Protein ◽  
Organic Anion Transporter ◽  
Multidrug Resistance Protein ◽  
Multidrug Resistance Protein 2 ◽  
Apical Domain ◽  
Anion Transporter ◽  
Resistance Protein

The canalicular membrane of rat hepatocytes contains an ATP-dependent multispecific organic anion transporter, also named multidrug resistance protein 2, that is responsible for the biliary secretion of several amphiphilic organic anions. This transport function is markedly diminished in mutant rats that lack the transport protein. To assess the role of vesicle traffic in the regulation of canalicular organic anion transport, we have examined the redistribution of the transporter to the canalicular membrane and the effect of cAMP on this process in isolated hepatocyte couplets, which retain secretory polarity. The partial disruption of cell-cell contact, due to the isolation procedure, leaves the couplet with both remnant apical membranes, as a source of apical proteins, and an intact apical domain and lumen, to which these proteins are targeted. The changes in distribution of the transporter were correlated to the apical excretion of a fluorescent substrate, glutathione-methylfluorescein. The data obtained in this study show that the transport protein, endocytosed from apical membrane remnants, first is redistributed along the basolateral plasma membrane. Then it is transcytosed to the remaining apical pole in a microtubule-dependent fashion, followed by the fusion of transporter-containing vesicles with the apical membrane. The cAMP analog dibutyrylcAMP stimulates all three steps, resulting in increased apically located transport protein, glutathione-methylfluorescein transport activity and apical membrane circumference. These findings indicate that the organic anion transport capacity of the apical membrane in hepatocyte couplets is regulated by cAMP-stimulated sorting of the multidrug resistance protein 2 to the apical membrane. The relevance of this phenomenon for the intact liver is discussed.

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