scholarly journals Characterization of the Transport of a Cationic Octapeptide, Octreotide, in Rat Bile Canalicular Membrane: Possible Involvement of P-Glycoprotein.

1998 ◽  
Vol 21 (8) ◽  
pp. 874-878 ◽  
Author(s):  
Tadashi YAMADA ◽  
Yukio KATO ◽  
Hiroyuki KUSUHARA ◽  
Michel LEMAIRE ◽  
Yuichi SUGIYAMA
Keyword(s):  
Canalicular Membrane ◽  
P Glycoprotein ◽  
Bile Canalicular Membrane ◽  
Rat Bile

scholarly journals mdr2 encodes P-glycoprotein expressed in the bile canalicular membrane as determined by isoform-specific antibodies.

1992 ◽  
Vol 267 (25) ◽  
pp. 18093-18099
Author(s):  
E Buschman ◽  
R.J. Arceci ◽  
J.M. Croop ◽  
M Che ◽  
I.M. Arias ◽  
...  
Keyword(s):  
Canalicular Membrane ◽  
Specific Antibodies ◽  
P Glycoprotein ◽  
Bile Canalicular Membrane

Region-dependent disappearance of vinblastine in rat small intestine and characterization of its P-glycoprotein-mediated efflux system

2000 ◽  
Vol 11 (4) ◽  
pp. 317-324 ◽  
Author(s):  
Akira Nakayama ◽  
Hiroshi Saitoh ◽  
Masako Oda ◽  
Masahiko Takada ◽  
Bruce J Aungst
Keyword(s):  
Small Intestine ◽  
Rat Small Intestine ◽  
Efflux System ◽  
P Glycoprotein

ATP-activated chloride channel inhibited by an antibody to P glycoprotein

1994 ◽  
Vol 267 (4) ◽  
pp. C1095-C1102 ◽  
Author(s):  
J. J. Zhang ◽  
T. J. Jacob
Keyword(s):  
Single Channel ◽  
Disulfonic Acid ◽  
Fiber Cells ◽  
Cl Channel ◽  
P Glycoprotein ◽  
Voltage Curve ◽  
Current Voltage ◽  
Single Channel Activity ◽  
Current Voltage Curve

In this report, we present the characteristics of a Cl- channel found in lens fiber cells. The single channel has a conductance of 17 pS, a linear current-voltage curve, is activated by ATP or strong depolarization and is blocked by verapamil, quinidine, 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid, 5-nitro-2-(3- phenylpropylamino)benzoate, dideoxyforskolin, and tamoxifen. These properties are similar to those reported for a volume-activated Cl- channel associated with the multidrug resistance (MDR) gene product, P glycoprotein (24). Confirming this connection, we demonstrate that our lens Cl- channel is inhibited by an antibody to P glycoprotein. The data we present here may, therefore, be the first characterization of the single channel activity of the Cl- channel associated with P glycoprotein.

Establishment and characterization of an MDCK cell line stably-transfected with chicken Abcb1 encoding P-glycoprotein

2016 ◽  
Vol 106 ◽  
pp. 37-44 ◽  
Author(s):  
Yong Sun ◽  
Tingting Guo ◽  
Dawei Guo ◽  
Li Guo ◽  
Li Chen ◽  
...  
Keyword(s):  
Cell Line ◽  
Mdck Cell ◽  
Mdck Cell Line ◽  
P Glycoprotein

scholarly journals Functional characterization of a glycine 185-to-valine substitution in human P-glycoprotein by using a vaccinia-based transient expression system.

1996 ◽  
Vol 7 (10) ◽  
pp. 1485-1498 ◽  
Author(s):  
M Ramachandra ◽  
S V Ambudkar ◽  
M M Gottesman ◽  
I Pastan ◽  
C A Hrycyna
Keyword(s):  
Drug Resistance ◽  
Atpase Activity ◽  
Cyclosporin A ◽  
Transient Expression ◽  
Expression System ◽  
Rhodamine 123 ◽  
Wild Type ◽  
P Glycoprotein ◽  
Transient Expression System

Human P-glycoprotein (Pgp) is a 170-kDa plasma membrane protein that confers multidrug resistance to otherwise sensitive cells. A mutation in Pgp, G185-->V, originally identified as a spontaneous mutation, was shown previously to alter the drug resistance profiles in cell lines that are stably transfected with the mutant MDR1 cDNA and selected with cytotoxic agents. To understand the mechanism by which the V185 mutation leads to an altered drug resistance profile, we used a transient expression system that eliminates the need for drug selection to attain high expression levels and allows for the rapid characterization of many aspects of Pgp function and biosynthesis. The mutant and wild-type proteins were expressed at similar levels after 24-48 h in human osteosarcoma (HOS) cells by infection with a recombinant vaccinia virus encoding T7 RNA polymerase and simultaneous transfection with a plasmid containing MDR1 cDNA controlled by the T7 promoter. For both mutant and wild-type proteins, photolabeling with [3H]azidopine and [125I]iodoarylazidoprazosin, drug-stimulated ATPase activity, efflux of rhodamine 123, and accumulation of radiolabeled vinblastine and colchicine were evaluated. In crude membrane preparations from HOS cells, a higher level of basal Pgp-ATPase activity was observed for the V185 variant than for the wild-type, suggesting partial uncoupling of drug-dependent ATP hydrolysis by the mutant. Several compounds, including verapamil, nicardipine, tetraphenylphosphonium, and prazosin, stimulated ATPase activities of both the wild-type and mutant similarly, whereas cyclosporin A inhibited the ATPase activity of the mutant more efficiently than that of the wild-type. This latter observation explains the enhanced potency of cyclosporin A as an inhibitor of the mutant Pgp. No differences were seen in verapamil-inhibited rhodamine 123 efflux, but the rate of accumulation was slower for colchicine and faster for vinblastine in cells expressing the mutant protein, as compared with those expressing wild-type Pgp. We conclude that the G185-->V mutation confers pleiotropic alterations on Pgp, including an altered basal ATPase activity and altered interaction with substrates and the inhibitor cyclosporin A.

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