NDLI: Vinblastine and sulfinpyrazone export by the multidrug resistance protein MRP2 is associated with glutathione export

Content Provider	PubMed Central
Author	Evers, R. Haas, M. De Sparidans, R. Beijnen, J. Wielinga, P. R. Lankelma, J. Borst, P.
Copyright Year	2000
Abstract	The multidrug resistance proteins MRP1 and MRP2 are members of the same subfamily of ATP-binding cassette transporters. Besides organic molecules conjugated to negatively charged ligands, these proteins also transport cytotoxic drugs for which no negatively charged conjugates are known to exist. In polarized MDCKII cells, MRP1 routes to the lateral plasma membrane, and MRP2 to the apical plasma membrane. In these cells MRP1 transports daunorubicin, and MRP2 vinblastine; both transporters export reduced glutathione (GSH) into the medium. We demonstrate that glutathione transport in MDCKII-MRP1 cells is inhibited by the inhibitors of organic anion transporters sulfinpyrazone, indomethacin, probenecid and benzbromarone. In MDCKII-MRP2 cells, GSH export is stimulated by low concentrations of sulfinpyrazone or indomethacin, whereas export is inhibited down to control levels at high concentrations. We find that unmodified sulfinpyrazone is a substrate for MRP2, also at concentrations where GSH export is inhibited. We also show that GSH export in MDCKII-MRP2 cells increases in the presence of vinblastine, and that the stochiometry between drug and GSH exported is between two and three. Our data indicate that transport of sulfinpyrazone and vinblastine is associated with GSH export. However, at high sulfinpyrazone concentrations this compound is transported without GSH. Models of MRP action are discussed that could explain these results. © 2000 Cancer Research Campaign
Related Links	http://dx.doi.org/10.1054/bjoc.2000.1262
Starting Page	375
File Format	PDF
ISSN	15321827
e-ISSN	15321827
Journal	British Journal of Cancer
Issue Number	3
Volume Number	83
Language	English
Publisher	Nature Publishing Group
Publisher Date	2000-07-01
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cancer Research Oncology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Vinblastine and sulfinpyrazone export by the multidrug resistance protein MRP2 is associated with glutathione export

Role of glutathione in the export of compounds from cells by the multidrug-resistance-associated protein.

Regulation by glutathione of drug transport in multidrug-resistant human lung tumour cell lines overexpressing multidrug resistance-associated protein.

Regulation by glutathione of drug transport in multidrug-resistant human lung tumour cell lines overexpressing multidrug resistance-associated protein

Role of multidrug resistance protein 2 (MRP2) in chemoresistance and clinical outcome in oesophageal squamous cell carcinoma

Quantitative Immunofluorescent Blotting of the Multidrug Resistance-associated Protein 2 (MRP2)

Cytotoxicity of rhein, the active metabolite of sennoside laxatives, is reduced by multidrug resistance-associated protein 1

A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1

Multidrug Resistance-Associated Protein 2 (Mrp2) is Primarily Responsible for the Biliary Excretion of Fexofenadine in Mice

Vinblastine and sulfinpyrazone export by the multidrug resistance protein MRP2 is associated with glutathione export

Similar Documents

Vinblastine and sulfinpyrazone export by the multidrug resistance protein MRP2 is associated with glutathione export

Role of glutathione in the export of compounds from cells by the multidrug-resistance-associated protein.

Regulation by glutathione of drug transport in multidrug-resistant human lung tumour cell lines overexpressing multidrug resistance-associated protein.

Regulation by glutathione of drug transport in multidrug-resistant human lung tumour cell lines overexpressing multidrug resistance-associated protein

Role of multidrug resistance protein 2 (MRP2) in chemoresistance and clinical outcome in oesophageal squamous cell carcinoma

Quantitative Immunofluorescent Blotting of the Multidrug Resistance-associated Protein 2 (MRP2)

Cytotoxicity of rhein, the active metabolite of sennoside laxatives, is reduced by multidrug resistance-associated protein 1

A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1

Multidrug Resistance-Associated Protein 2 (Mrp2) is Primarily Responsible for the Biliary Excretion of Fexofenadine in Mice

Vinblastine and sulfinpyrazone export by the multidrug resistance protein MRP2 is associated with glutathione export