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  • Title: Functional modulation of ATPase of P-glycoprotein by C219, a monoclonal antibody against P-glycoprotein.
    Author: Kokubu N, Cohen D, Watanabe T.
    Journal: Biochem Biophys Res Commun; 1997 Jan 13; 230(2):398-401. PubMed ID: 9016791.
    Abstract:
    P-glycoprotein functions as an ATP-driven efflux pump for antitumor agents. C219 is a monoclonal antibody which recognizes regions near both ATP binding domains in each half of P-glycoprotein. In this study, we have demonstrated that C219 inhibits the ATPase activity of P-glycoprotein based on the following findings: 1) the inhibition of total ATPase activity by C219 was selective to P-glycoprotein-positive membranes; 2) the C219-sensitive fraction of ATPase correlated the expression of P-glycoprotein; and 3) modulators of P-glycoprotein ATPase, verapamil and cyclosporin A, affected the C219-sensitive fraction of ATPase. The photolabeling of P-glycoprotein with 8-azido-[alpha-32P]ATP was inhibited by C219, suggesting that the inhibition of ATP binding by C219 reduced the activity. Since C219 interacts with P-glycoprotein ATPase, C219 might become a useful tool for studying the role of P-glycoprotein ATPase.
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