Characterization of the ATPase activity of human ATP-binding cassette transporter-2 (ABCA2)

Vladimir Beljanski, Athena Soulika, Jody M. Tucker, Danyelle M. Townsend, Warren Davis, Kenneth D. Tew

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Background: ABCA2 is a member of the ATP binding cassette transporter family with functional roles in cholesterol homeostasis and drug resistance. Materials and methods: In order to characterize its ATPase activity, we transfected HEK293 cells with an ABCA2 mammalian expression system and isolated ABCA2-enriched membranes. Results: We found no measurable ATPase activity of ABCA2 in isolated membranes, except in the presence of the methyl-β-cyclodextrin. However, competitive binding of a pseudo-substrate, 8-azido-[α-32P]-ATP, was demonstrated. CHO cells transfected with ABCA2 did not have a higher rate of endogenous ATP hydrolysis when compared to the mock-transfected cells. Conclusion: Overall, we conclude that, while ABCA2 may have low levels of ATPase activity that can be substrate-stimulated, it is more likely to have a regulatory role in cell physiology.

Original languageEnglish (US)
Pages (from-to)657-660
Number of pages4
JournalIn Vivo
Issue number4
StatePublished - Jul 2005
Externally publishedYes


  • ABCA2 transporter
  • ATPase activity
  • Catalysis
  • Pseudo-substrate

ASJC Scopus subject areas

  • Medicine(all)


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