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P‐glycoprotein transports corticosterone and is photoaffinity‐labeled by the steroid
Author(s) -
Wolf David C.,
Horwitz Susan Band
Publication year - 1992
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910520125
Subject(s) - glycoprotein , corticosterone , p glycoprotein , photoaffinity labeling , efflux , endogeny , membrane glycoproteins , chemistry , steroid , biochemistry , endocrinology , medicine , biology , binding site , multiple drug resistance , hormone , antibiotics
Multi‐drug‐resistant cells overproduce a 130–180‐kDa integral membrane phosphoglycoprotein known as P‐glycoprotein which acts as an energy‐dependent drug efflux pump. While P‐glycoprotein has been shown to transport hydrophobic anti tumor drugs out of multi‐drug‐resistant cells in tissue culture, its endogenous substrates remain unknown. This report shows that 3 H‐corticosterone can specifically photoaffinity label P‐glycoprotein. Furthermore, corticosterone is effluxed from multidrug‐resistant cells by P‐glycoprotein. These data suggest that corticosterone may be an endogenous substrate for P‐glycoprotein. © 1992 Wiley‐Liss, Inc.