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P-glycoproteins: mediators of multidrug resistance

U A Germann1, I Pastan, M M Gottesman

  • 1Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.

Seminars in Cell Biology
|February 1, 1993
PubMed

Insights

Multidrug resistance in cancer is often caused by P-glycoprotein, an efflux pump that removes chemotherapy drugs. Recent studies explore its biosynthesis, structure, function, and a newly found chloride channel activity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Multidrug resistance (MDR) is a significant challenge in cancer chemotherapy, particularly for metastatic cancers.
  • Elevated P-glycoprotein (P-gp) levels in cancer cells correlate with resistance to numerous amphiphilic cytotoxic drugs.
  • P-glycoprotein is a plasma membrane protein functioning as an ATP-dependent drug efflux pump.

Purpose of the Study:

  • To review recent research on P-glycoprotein (P-gp).
  • To elucidate the biosynthesis, structure, function, and mechanism of action of P-gp.
  • To investigate the implications of P-gp's multifunctional transport system, including its chloride channel activity.

Main Methods:

  • Review of recent scientific literature on P-glycoprotein.
  • Analysis of studies detailing P-gp biosynthesis and structure.
  • Examination of functional and mechanistic studies of P-gp's drug efflux and channel activities.

Main Results:

  • P-glycoprotein confers multidrug resistance by acting as an energy-dependent drug efflux pump.
  • Recent studies have provided deeper insights into the complex nature of this multifunctional transport system.
  • An additional chloride channel activity associated with P-glycoprotein has been identified.

Conclusions:

  • P-glycoprotein is a key factor in multidrug resistance, acting as a drug efflux pump.
  • Understanding P-gp's complex structure and function, including its chloride channel activity, is crucial for developing new cancer therapies.
  • The precise physiological role of P-glycoprotein requires further investigation.

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