Functional expression of human P‐glycoprotein in Schizosaccharomyces pombe

FEBS Letters

Takebe, So²  Fujii, Yuko²  Shimabuku, Alfredo M.³  Nishi, Kazunori¹  Komano, Tohru³  Beppu, Teruhiko¹  Konishi, Haruko³  Ueda, Kazumitsu³  Yoshida, Minoru¹ 

[1] Department of Agricultural Chemistry, University of Tokyo, Tokyo 113, Japan;Department of Food Science, Kyoto Women's University, Kyoto 605, Japan;Laboratory of Biochemistry, Department of Agricultural Chemistry, Kyoto University, Kyoto 606-01, Japan

关键词: P-glycoprotein;    Multidrug resistance;    Yeast;    Schizosaccharomyces pombe;    ATP hydrolysis;    Glycosylation;    MDR;    multidrug resistance;    S. pombe;    Schizosaccharomyces pombe;    nt;    nucleotide;    PCR;    polymerase chain reaction;   

DOI  :  10.1016/0014-5793(93)80888-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Human MDR1 cDNA was introduced into the human cultured cells KB-3-1 and Schizosaccharomyces pombe pmdI 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.

【 授权许可】

Unknown