Drug-transporter proteins in clinical multidrug resistance
Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified...
Ausführliche Beschreibung
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1992 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Clinica Chimica Acta - Amsterdam : Elsevier, 206(1992), 1-2, Seite 25-32 |
| Übergeordnetes Werk: |
volume:206 ; year:1992 ; number:1-2 ; pages:25-32 |
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NLEJ186154321 |
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| 520 | |a Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified at the molecular level. The mdr1 gene-encoded P-gp acts as a drug efflux pump, lowering intracellular drug concentration by active extrusion of drugs from the cell. The role of P-gp in determining clinical resistance to multiple anticancer drugs is likely to be largely different for various tumor types. Recently we selected a monoclonal antibody (mAb LRP56) for strong, granular cytoplasmic reactivity with MDR tumor cell lines without P-gp (over)expression. None or weak reactivity was observed with parental and P-gp positive cell lines. We hypothesize that as yet-undefined drug transport-mediating proteins are inserted in intracellular membranes lining the exocytotic compartment and thus may contribute to clinical multidrug resistance. | ||
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(DE-627)NLEJ186154321 (DE-599)GBVNLZ186154321 DE-627 ger DE-627 rakwb eng Drug-transporter proteins in clinical multidrug resistance 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified at the molecular level. The mdr1 gene-encoded P-gp acts as a drug efflux pump, lowering intracellular drug concentration by active extrusion of drugs from the cell. The role of P-gp in determining clinical resistance to multiple anticancer drugs is likely to be largely different for various tumor types. Recently we selected a monoclonal antibody (mAb LRP56) for strong, granular cytoplasmic reactivity with MDR tumor cell lines without P-gp (over)expression. None or weak reactivity was observed with parental and P-gp positive cell lines. We hypothesize that as yet-undefined drug transport-mediating proteins are inserted in intracellular membranes lining the exocytotic compartment and thus may contribute to clinical multidrug resistance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Scheper, R.J. oth Broxterman, H.J. oth Scheffer, G.L. oth Meijer, C.J.L.M. oth Pinedo, H.M. oth in Clinica Chimica Acta Amsterdam : Elsevier 206(1992), 1-2, Seite 25-32 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:206 year:1992 number:1-2 pages:25-32 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(92)90005-B GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 206 1992 1-2 25-32 |
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(DE-627)NLEJ186154321 (DE-599)GBVNLZ186154321 DE-627 ger DE-627 rakwb eng Drug-transporter proteins in clinical multidrug resistance 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified at the molecular level. The mdr1 gene-encoded P-gp acts as a drug efflux pump, lowering intracellular drug concentration by active extrusion of drugs from the cell. The role of P-gp in determining clinical resistance to multiple anticancer drugs is likely to be largely different for various tumor types. Recently we selected a monoclonal antibody (mAb LRP56) for strong, granular cytoplasmic reactivity with MDR tumor cell lines without P-gp (over)expression. None or weak reactivity was observed with parental and P-gp positive cell lines. We hypothesize that as yet-undefined drug transport-mediating proteins are inserted in intracellular membranes lining the exocytotic compartment and thus may contribute to clinical multidrug resistance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Scheper, R.J. oth Broxterman, H.J. oth Scheffer, G.L. oth Meijer, C.J.L.M. oth Pinedo, H.M. oth in Clinica Chimica Acta Amsterdam : Elsevier 206(1992), 1-2, Seite 25-32 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:206 year:1992 number:1-2 pages:25-32 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(92)90005-B GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 206 1992 1-2 25-32 |
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(DE-627)NLEJ186154321 (DE-599)GBVNLZ186154321 DE-627 ger DE-627 rakwb eng Drug-transporter proteins in clinical multidrug resistance 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified at the molecular level. The mdr1 gene-encoded P-gp acts as a drug efflux pump, lowering intracellular drug concentration by active extrusion of drugs from the cell. The role of P-gp in determining clinical resistance to multiple anticancer drugs is likely to be largely different for various tumor types. Recently we selected a monoclonal antibody (mAb LRP56) for strong, granular cytoplasmic reactivity with MDR tumor cell lines without P-gp (over)expression. None or weak reactivity was observed with parental and P-gp positive cell lines. We hypothesize that as yet-undefined drug transport-mediating proteins are inserted in intracellular membranes lining the exocytotic compartment and thus may contribute to clinical multidrug resistance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Scheper, R.J. oth Broxterman, H.J. oth Scheffer, G.L. oth Meijer, C.J.L.M. oth Pinedo, H.M. oth in Clinica Chimica Acta Amsterdam : Elsevier 206(1992), 1-2, Seite 25-32 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:206 year:1992 number:1-2 pages:25-32 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(92)90005-B GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 206 1992 1-2 25-32 |
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(DE-627)NLEJ186154321 (DE-599)GBVNLZ186154321 DE-627 ger DE-627 rakwb eng Drug-transporter proteins in clinical multidrug resistance 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified at the molecular level. The mdr1 gene-encoded P-gp acts as a drug efflux pump, lowering intracellular drug concentration by active extrusion of drugs from the cell. The role of P-gp in determining clinical resistance to multiple anticancer drugs is likely to be largely different for various tumor types. Recently we selected a monoclonal antibody (mAb LRP56) for strong, granular cytoplasmic reactivity with MDR tumor cell lines without P-gp (over)expression. None or weak reactivity was observed with parental and P-gp positive cell lines. We hypothesize that as yet-undefined drug transport-mediating proteins are inserted in intracellular membranes lining the exocytotic compartment and thus may contribute to clinical multidrug resistance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Scheper, R.J. oth Broxterman, H.J. oth Scheffer, G.L. oth Meijer, C.J.L.M. oth Pinedo, H.M. oth in Clinica Chimica Acta Amsterdam : Elsevier 206(1992), 1-2, Seite 25-32 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:206 year:1992 number:1-2 pages:25-32 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(92)90005-B GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 206 1992 1-2 25-32 |
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(DE-627)NLEJ186154321 (DE-599)GBVNLZ186154321 DE-627 ger DE-627 rakwb eng Drug-transporter proteins in clinical multidrug resistance 1992 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified at the molecular level. The mdr1 gene-encoded P-gp acts as a drug efflux pump, lowering intracellular drug concentration by active extrusion of drugs from the cell. The role of P-gp in determining clinical resistance to multiple anticancer drugs is likely to be largely different for various tumor types. Recently we selected a monoclonal antibody (mAb LRP56) for strong, granular cytoplasmic reactivity with MDR tumor cell lines without P-gp (over)expression. None or weak reactivity was observed with parental and P-gp positive cell lines. We hypothesize that as yet-undefined drug transport-mediating proteins are inserted in intracellular membranes lining the exocytotic compartment and thus may contribute to clinical multidrug resistance. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Scheper, R.J. oth Broxterman, H.J. oth Scheffer, G.L. oth Meijer, C.J.L.M. oth Pinedo, H.M. oth in Clinica Chimica Acta Amsterdam : Elsevier 206(1992), 1-2, Seite 25-32 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:206 year:1992 number:1-2 pages:25-32 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(92)90005-B GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 206 1992 1-2 25-32 |
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Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified at the molecular level. The mdr1 gene-encoded P-gp acts as a drug efflux pump, lowering intracellular drug concentration by active extrusion of drugs from the cell. The role of P-gp in determining clinical resistance to multiple anticancer drugs is likely to be largely different for various tumor types. Recently we selected a monoclonal antibody (mAb LRP56) for strong, granular cytoplasmic reactivity with MDR tumor cell lines without P-gp (over)expression. None or weak reactivity was observed with parental and P-gp positive cell lines. We hypothesize that as yet-undefined drug transport-mediating proteins are inserted in intracellular membranes lining the exocytotic compartment and thus may contribute to clinical multidrug resistance. |
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Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified at the molecular level. The mdr1 gene-encoded P-gp acts as a drug efflux pump, lowering intracellular drug concentration by active extrusion of drugs from the cell. The role of P-gp in determining clinical resistance to multiple anticancer drugs is likely to be largely different for various tumor types. Recently we selected a monoclonal antibody (mAb LRP56) for strong, granular cytoplasmic reactivity with MDR tumor cell lines without P-gp (over)expression. None or weak reactivity was observed with parental and P-gp positive cell lines. We hypothesize that as yet-undefined drug transport-mediating proteins are inserted in intracellular membranes lining the exocytotic compartment and thus may contribute to clinical multidrug resistance. |
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Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified at the molecular level. The mdr1 gene-encoded P-gp acts as a drug efflux pump, lowering intracellular drug concentration by active extrusion of drugs from the cell. The role of P-gp in determining clinical resistance to multiple anticancer drugs is likely to be largely different for various tumor types. Recently we selected a monoclonal antibody (mAb LRP56) for strong, granular cytoplasmic reactivity with MDR tumor cell lines without P-gp (over)expression. None or weak reactivity was observed with parental and P-gp positive cell lines. We hypothesize that as yet-undefined drug transport-mediating proteins are inserted in intracellular membranes lining the exocytotic compartment and thus may contribute to clinical multidrug resistance. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ186154321</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506090811.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1992 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ186154321</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ186154321</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Drug-transporter proteins in clinical multidrug resistance</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1992</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Upon exposure to chemotherapeutic drugs, mammalian cells can acquire resistance to structurally and functionally unrelated compounds, a property known as multidrug resistance (MDR). One MDR mechanism, i.e. by the overexpression of a plasma membrane protein, P-glycoprotein (P-gp), has been identified at the molecular level. The mdr1 gene-encoded P-gp acts as a drug efflux pump, lowering intracellular drug concentration by active extrusion of drugs from the cell. The role of P-gp in determining clinical resistance to multiple anticancer drugs is likely to be largely different for various tumor types. Recently we selected a monoclonal antibody (mAb LRP56) for strong, granular cytoplasmic reactivity with MDR tumor cell lines without P-gp (over)expression. None or weak reactivity was observed with parental and P-gp positive cell lines. We hypothesize that as yet-undefined drug transport-mediating proteins are inserted in intracellular membranes lining the exocytotic compartment and thus may contribute to clinical multidrug resistance.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Scheper, R.J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Broxterman, H.J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Scheffer, G.L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Meijer, C.J.L.M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Pinedo, H.M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Clinica Chimica Acta</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">206(1992), 1-2, Seite 25-32</subfield><subfield code="w">(DE-627)NLEJ184917921</subfield><subfield code="w">(DE-600)1499920-1</subfield><subfield code="x">0009-8981</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:206</subfield><subfield code="g">year:1992</subfield><subfield code="g">number:1-2</subfield><subfield code="g">pages:25-32</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0009-8981(92)90005-B</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">206</subfield><subfield code="j">1992</subfield><subfield code="e">1-2</subfield><subfield code="h">25-32</subfield></datafield></record></collection>
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7.40158 |