Functional expression of the human MDR1 gene in Escherichia coli
In this preliminary study, we report the cloning of the human MDR1 cDNA into a prokaryotic expression vector and the consequent functional expression of heterologous P-glycoprotein in Escherichia coli. We demonstrate increased resistance to the P-glycoprotein substrates TPA+, TPP+, and puromycin; re...
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Veröffentlicht in: | Archives of biochemistry and biophysics 1996-09, Vol.333 (1), p.66-74 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | In this preliminary study, we report the cloning of the human MDR1 cDNA into a prokaryotic expression vector and the consequent functional expression of heterologous P-glycoprotein in Escherichia coli. We demonstrate increased resistance to the P-glycoprotein substrates TPA+, TPP+, and puromycin; reduced accumulation of TPP+ and tetracycline by resistant cells; and the expression of a full-length immunoreactive P-glycoprotein molecule in the membrane fraction of resistant cells. The obvious structural and functional similarities of P-gp to prokaryotic ABC transporters and other efflux transporters argues for a more complete study of the consequences pertaining to the expression of human P-glycoprotein in E. coli. |
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ISSN: | 0003-9861 |
DOI: | 10.1006/abbi.1996.0365 |