| pubmed-article:8713080 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8713080 | lifeskim:mentions | umls-concept:C0038317 | lld:lifeskim |
| pubmed-article:8713080 | lifeskim:mentions | umls-concept:C0010124 | lld:lifeskim |
| pubmed-article:8713080 | lifeskim:mentions | umls-concept:C0242643 | lld:lifeskim |
| pubmed-article:8713080 | lifeskim:mentions | umls-concept:C0033308 | lld:lifeskim |
| pubmed-article:8713080 | lifeskim:mentions | umls-concept:C0011710 | lld:lifeskim |
| pubmed-article:8713080 | lifeskim:mentions | umls-concept:C0042523 | lld:lifeskim |
| pubmed-article:8713080 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:8713080 | lifeskim:mentions | umls-concept:C1148926 | lld:lifeskim |
| pubmed-article:8713080 | lifeskim:mentions | umls-concept:C1709060 | lld:lifeskim |
| pubmed-article:8713080 | pubmed:dateCreated | 1996-9-12 | lld:pubmed |
| pubmed-article:8713080 | pubmed:abstractText | P-glycoprotein (P-gp) is a membranous ATPase responsible for the multidrug resistance (MDR) phenotype. Using membrane vesicles prepared from the highly resistant cell line DC-3F/ADX we studied the influence of P-gp ATPase activity of four progesterone derivatives which specifically bind to P-gp and reverse MDR. Progesterone and desoxycorticosterone stimulate P-gp ATPase activity with, respectively, apparent concentrations giving half-maximal activation of 20-25 microM and 40-50 microM, and activation factors of 2.3 (at 100 microM progesterone) and 1.8 (at 170 microM desoxycorticosterone). Hydrocortisone above 100 microM stimulates P-gp ATPase activity while corticosterone has no apparent stimulating effect. Our data are consistent with the location of the binding sites for the progesterone derivatives on the P-gp membranous domain. The effects of these steroids on verapamil-stimulated P-gp ATPase activity support a non-competitive mechanism, i.e. the binding sites for verapamil and steroids are mutually non-exclusive for P-gp ATPase modulation. A similar non-competitive inhibition of progesterone-stimulated P-gp ATPase activity by desoxycorticosterone or by corticosterone leads to the conclusion that these steroids, although sharing related structures, have distinct modulating sites on P-gp. As expected from their mutually non-exclusive interactions on P-gp, progesterone and verapamil when mixed induce a synergistic modulation of P-gp ATPase activity. Since drug transport by P-gp is believed to be coupled to its ATPase activity, a corresponding synergistic effect of these two modulators for the inhibition of P-gp-mediated drug resistance can be expected. | lld:pubmed |
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| pubmed-article:8713080 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8713080 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8713080 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8713080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8713080 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8713080 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8713080 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8713080 | pubmed:author | pubmed-author:BelehradekJJJ... | lld:pubmed |
| pubmed-article:8713080 | pubmed:author | pubmed-author:OrlowskiSS | lld:pubmed |
| pubmed-article:8713080 | pubmed:author | pubmed-author:PENS CSC | lld:pubmed |
| pubmed-article:8713080 | pubmed:author | pubmed-author:GarrigosMM | lld:pubmed |
| pubmed-article:8713080 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8713080 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8713080 | pubmed:volume | 317 ( Pt 2) | lld:pubmed |
| pubmed-article:8713080 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8713080 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8713080 | pubmed:pagination | 515-22 | lld:pubmed |
| pubmed-article:8713080 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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