Transport of somatostatin and substance P by human P-glycoprotein

FEBS Letters
Noriko Uchiyama-KokubuTakashi Tsuruo

Abstract

P-glycoprotein is an efflux pump for a broad spectrum of hydrophobic agents. We found that bioactive peptides including somatostatin and substance P inhibit ATP-dependent vincristine binding to P-glycoprotein-overexpressing K562/ADM membrane vesicles. Some of these bioactive peptides including somatostatin stimulate basal ATPase activity of P-glycoprotein; in contrast, other peptides including substance P inhibit it. The K562/ADM membrane vesicles showed an ATP-dependent, osmotically sensitive uptake of somatostatin and substance P, which was inhibited by valspodar, an inhibitor of P-glycoprotein. These findings suggested that certain bioactive peptides such as somatostatin and substance P directly interact with human P-glycoprotein as endogenous substrates for P-glycoprotein-mediated transport.

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Citations

Dec 1, 2005·European Journal of Pharmacology·Gérard SiestSophie Visvikis-Siest
Feb 12, 2013·International Journal of Molecular Sciences·Igor PrudovskyDavid Neivandt

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