Transport of somatostatin and substance P by human P-glycoprotein.

Article Details

Citation

Uchiyama-Kokubu N, Naito M, Nakajima M, Tsuruo T

Transport of somatostatin and substance P by human P-glycoprotein.

FEBS Lett. 2004 Sep 10;574(1-3):55-61. doi: 10.1016/j.febslet.2004.07.084.

PubMed ID
15358539 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Drug Transporters
DrugTransporterKindOrganismPharmacological ActionActions
SomatostatinP-glycoprotein 1ProteinHumans
Unknown
Substrate
Details