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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2001-5-23
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pubmed:abstractText |
P-glycoprotein (P-gp) is an ATP-dependent drug pump that confers multidrug resistance (MDR). In addition to its ability to efflux toxins, P-gp can also inhibit apoptosis induced by a wide array of cell death stimuli that rely on activation of intracellular caspases for full function. We therefore hypothesized that P-gp may have additional functions in addition to its role in effluxing xenotoxins that could provide protection to tumor cells against a host response. There have been a number of contradictory reports concerning the role of P-gp in regulating complement activation. Given the disparate results obtained by different laboratories and our published results demonstrating that P-gp does not affect cell death induced by another membranolytic protein, perforin, we decided to assess the role of P-gp in regulating cell lysis induced by a number of different pore-forming proteins. Testing a variety of different P-gp-expressing MDR cell lines produced following exposure of cells to chemotherapeutic agents or by retroviral gene transduction in the complete absence of any drug selection, we found no difference in sensitivity of P-gp(+ve) or P-gp(-ve) cells to the pore-forming proteins complement, perforin, or pneumolysin. Based on these results, we conclude that P-gp does not affect cell lysis induced by pore-forming proteins.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/CD71 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Doxorubicin,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/P-Glycoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/Perforin,
http://linkedlifedata.com/resource/pubmed/chemical/Pore Forming Cytotoxic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgG,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rubidium,
http://linkedlifedata.com/resource/pubmed/chemical/Vincristine
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16667-73
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11278745-Antibodies,
pubmed-meshheading:11278745-Antibodies, Monoclonal,
pubmed-meshheading:11278745-Antigens, CD,
pubmed-meshheading:11278745-Antigens, Differentiation, B-Lymphocyte,
pubmed-meshheading:11278745-Cell Survival,
pubmed-meshheading:11278745-Doxorubicin,
pubmed-meshheading:11278745-Drug Resistance, Multiple,
pubmed-meshheading:11278745-Humans,
pubmed-meshheading:11278745-K562 Cells,
pubmed-meshheading:11278745-Kinetics,
pubmed-meshheading:11278745-Leukemia, T-Cell,
pubmed-meshheading:11278745-Membrane Glycoproteins,
pubmed-meshheading:11278745-P-Glycoprotein,
pubmed-meshheading:11278745-Perforin,
pubmed-meshheading:11278745-Pore Forming Cytotoxic Proteins,
pubmed-meshheading:11278745-Receptors, IgG,
pubmed-meshheading:11278745-Receptors, Transferrin,
pubmed-meshheading:11278745-Recombinant Proteins,
pubmed-meshheading:11278745-Rubidium,
pubmed-meshheading:11278745-Transfection,
pubmed-meshheading:11278745-Tumor Cells, Cultured,
pubmed-meshheading:11278745-Vincristine
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pubmed:year |
2001
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pubmed:articleTitle |
P-glycoprotein does not protect cells against cytolysis induced by pore-forming proteins.
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pubmed:affiliation |
Peter MacCallum Cancer Institute, Trescowthick Research Laboratories, St. Andrews Place, East Melbourne 3002, Victoria, Australia. r.johnstone@pmci.unimelb.edu.au
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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