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

Sharad S. Singhal, Archana Sehrawat, Amee Mehta, Mukesh Sahu, Sanjay Awasthi

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


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 SDSPAGE 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.

Original languageEnglish (US)
Pages (from-to)191-199
Number of pages9
JournalInternational Journal of Oncology
Issue number1
StatePublished - 2009
Externally publishedYes


  • 4HNE
  • Drug-resistance
  • Glutathioneconjugate
  • K562
  • RLIP76
  • Transport

ASJC Scopus subject areas

  • Oncology
  • Cancer Research


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