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Functional expression of human P‐glycoprotein in Schizosaccharomyces pombe
Author(s) -
Ueda Kazumitsu,
Shimabuku Alfredo M.,
Konishi Haruko,
Fujii Yuko,
Takebe So,
Nishi Kazunori,
Yoshida Minoru,
Beppu Teruhiko,
Komano Tohru
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80888-2
Subject(s) - schizosaccharomyces pombe , valinomycin , mutant , biology , p glycoprotein , efflux , glycoprotein , microbiology and biotechnology , biochemistry , chemistry , multiple drug resistance , antibiotics , gene , membrane potential
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 .