Functional expression of human P-glycoprotein in Schizosaccharomyces pombe.

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Ueda K, Shimabuku AM, Konishi H, Fujii Y, Takebe S, Nishi K, Yoshida M, Beppu T, Komano T

Functional expression of human P-glycoprotein in Schizosaccharomyces pombe.

FEBS Lett. 1993 Sep 20;330(3):279-82. doi: 10.1016/0014-5793(93)80888-2.

PubMed ID

7690715 [ View in PubMed

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Abstract

Human MDR1 cDNA was introduced into the human cultured cells KB-3-1 and Schizosaccharomyces pombe pmd1 null mutant KN3. The drug sensitivity of KB-G2 and KN3/pgp, expressing human P-glycoprotein, was examined. KB-G2 was resistant to the peptide antibiotics valinomycin and gramicidin D as well as having a typical multidrug resistance (MDR) phenotype. KN3/pgp was resistant to valinomycin and actinomycin D, but not to adriamycin. The ATP-hydrolysis-deficient mutant did not confer KN3 resistance to these antibiotics. Human P-glycoprotein expressed in S. pombe seemed to lack N-glycosylation. The N-glycosylation-deficient mutant, however, conferred a typical MDR phenotype on KB-3-1. These results suggest that human P-glycoprotein functions as an efflux pump of valinomycin and actinomycin D in the membrane of S. pombe.

DrugBank Data that Cites this Article

Drug Transporters

Drug	Transporter	Kind	Organism	Pharmacological Action	Actions
Valinomycin	P-glycoprotein 1	Protein	Humans	Unknown	Substrate Inhibitor	Details