| pubmed-article:7744732 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7744732 | lifeskim:mentions | umls-concept:C0242643 | lld:lifeskim |
| pubmed-article:7744732 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:7744732 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:7744732 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:7744732 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:7744732 | pubmed:dateCreated | 1995-6-15 | lld:pubmed |
| pubmed-article:7744732 | pubmed:abstractText | Studies with inside-out plasma membrane vesicles from multidrug-resistant (MDR 3) murine erythroleukemia (MEL/VCR-6) cells have provided evidence for down-modulation of P-glycoprotein (P-gp) function by Ca(2+)-calmodulin (CLM). These studies showed that CLM in the presence or absence of Ca2+ had no effect on binding of [3H]vinblastine (VBL) by P-gp in inside-out plasma membrane vesicles. However, profound inhibition of ATP-dependent [3H]VBL efflux by these vesicles was demonstrated by the addition of subnanomolar concentrations of CLM (IC50 = 0.15 +/- 0.02 nM). The addition of 1 microM Ca2+ reduced the inhibition of [3H]VBL efflux by CLM, shifting the concentration required for inhibition to the nM range (IC50 = 2.55 +/- 0.35 nM). The inhibition of as 0.01 mM Ca2+, and no inhibition occurred with concentrations greater than 0.2 mM Ca2+. Binding of CLM, itself, to P-gp was demonstrated in two ways. The P-gp content of detergent-solubilized plasma membrane from MEL/VCR-6 cells could be appreciably depleted by treating this material with CLM-Sepharose beads as shown by SDS-polyacrylamide gel electrophoresis (PAGE) and Western blotting with anti-P-gp antibody (C219) before and after CLM-Sepharose treatment. Also, depletion of P-gp from solution by CLM was less in the presence of 1 mM Ca2+. Blotting of P-gp after SDS-PAGE of plasma membrane from MEL/VCR-6 cells was also obtained using 125I-CLM as a probe. These results strongly suggest that the MDR 3 homolog of P-gp is a CLM-binding protein and that direct interaction of Ca(2+)-CLM with P-gp, while not affecting its binding of [3H]VBL, down-modulates the translocation of this agent in the presence of ATP. | lld:pubmed |
| pubmed-article:7744732 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7744732 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7744732 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7744732 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7744732 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7744732 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7744732 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7744732 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7744732 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7744732 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7744732 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7744732 | pubmed:month | May | lld:pubmed |
| pubmed-article:7744732 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7744732 | pubmed:author | pubmed-author:YangC HCH | lld:pubmed |
| pubmed-article:7744732 | pubmed:author | pubmed-author:SirotnakF MFM | lld:pubmed |
| pubmed-article:7744732 | pubmed:author | pubmed-author:SchlemmerS... | lld:pubmed |
| pubmed-article:7744732 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7744732 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:7744732 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7744732 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7744732 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7744732 | pubmed:pagination | 11040-2 | lld:pubmed |
| pubmed-article:7744732 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7744732 | pubmed:meshHeading | pubmed-meshheading:7744732-... | lld:pubmed |
| pubmed-article:7744732 | pubmed:meshHeading | pubmed-meshheading:7744732-... | lld:pubmed |
| pubmed-article:7744732 | pubmed:meshHeading | pubmed-meshheading:7744732-... | lld:pubmed |
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| pubmed-article:7744732 | pubmed:meshHeading | pubmed-meshheading:7744732-... | lld:pubmed |
| pubmed-article:7744732 | pubmed:meshHeading | pubmed-meshheading:7744732-... | lld:pubmed |
| pubmed-article:7744732 | pubmed:meshHeading | pubmed-meshheading:7744732-... | lld:pubmed |
| pubmed-article:7744732 | pubmed:meshHeading | pubmed-meshheading:7744732-... | lld:pubmed |
| pubmed-article:7744732 | pubmed:meshHeading | pubmed-meshheading:7744732-... | lld:pubmed |
| pubmed-article:7744732 | pubmed:meshHeading | pubmed-meshheading:7744732-... | lld:pubmed |
| pubmed-article:7744732 | pubmed:meshHeading | pubmed-meshheading:7744732-... | lld:pubmed |
| pubmed-article:7744732 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7744732 | pubmed:articleTitle | Functional modulation of multidrug resistance-related P-glycoprotein by Ca(2+)-calmodulin. | lld:pubmed |
| pubmed-article:7744732 | pubmed:affiliation | Program of Molecular Pharmacology and Experimental Therapeutics, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA. | lld:pubmed |
| pubmed-article:7744732 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7744732 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7744732 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7744732 | lld:pubmed |
