Functional reconstitution of RLIP76 catalyzing ATP-dependent transport of glutathione-conjugates.

Abstract:

:RLIP76, a stress-responsive, multi-functional protein with multi-specific transport activity towards glutathione-conjugates (GS-E) and chemotherapeutic agents is frequently overexpressed in malignant cells. Our recent studies suggest that it plays a prominent anti-apoptotic role selectively in cancer cells. The present studies were performed to compare RLIP76 activity towards glutathione-conjugates in recombinant and K562 human erythroleukemia cells. The purity and identity of recombinant and K562 RLIP76 was established by SDS-PAGE and Western blot analysis. These studies confirmed the origin of the 38 kDa protein, previously referred to as DNP-SG ATPase, from RLIP76. Comparison of ATPase activity and transport kinetics for DNP-SG and GS-HNE between recombinant vs. K562 RLIP76 revealed higher specific activity of ATPase and transport for recombinant purified RLIP76, indicating that additional factors present in recombinant purified RLIP76 can modulate its transport activity.

journal_name

Int J Oncol

authors

Singhal SS,Sehrawat A,Mehta A,Sahu M,Awasthi S

subject

Has Abstract

pub_date

2009-01-01 00:00:00

pages

191-9

issue

1

eissn

1019-6439

issn

1791-2423

journal_volume

34

pub_type

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