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Research Article

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 and KENNETH D. TEW
In Vivo July 2005, 19 (4) 657-660;
VLADIMIR BELJANSKI
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ATHENA SOULIKA
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JODY M. TUCKER
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DANYELLE M. TOWNSEND
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WARREN DAVIS JR.
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KENNETH D. TEW
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  • For correspondence: tewk@musc.edu
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Abstract

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.

  • ABCA2 transporter
  • ATPase activity
  • pseudo-substrate
  • catalysis

Footnotes

  • ↵* The two authors equally contributed to the work.

    • Received May 12, 2005.
    • Accepted May 20, 2005.
  • Copyright © 2005 International Institute of Anticancer Research (Dr. John G. Delinassios), All rights reserved
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July-August 2005
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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
In Vivo Jul 2005, 19 (4) 657-660;

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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
In Vivo Jul 2005, 19 (4) 657-660;
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