Rational use of in vitro P-glycoprotein assays in drug discovery.

P-glycoprotein (Pgp) affects the absorption, distribution, and clearance of a variety of compounds. Thus, identification of compounds that are Pgp substrates can aid drug candidate selection and optimization. Our goal was to evaluate three assays used to determine whether compounds are Pgp substrates. Sixty-six compounds were tested in monolayer efflux, ATPase, and calcein-AM assays. Assay results yielded two categories of compounds. Category I (n = 35) exhibited concordance across the assays. Category II (n = 31) revealed differences among the assays that related to the apparent permeability (P(app)) of the compounds. Within category II, two groups were discerned based on the absence (group IIA, n = 10, nontransported substrates) or presence (group IIB, n = 21, transported substrates) of monolayer efflux. Detection of efflux (group IIB) was associated with compounds having low/moderate P(app) values (mean = 16.6 nm/s), whereas inability to detect efflux (group IIA) was associated with compounds having high P(app) values (mean = 535 nm/s). The calcein-AM and ATPase assays revealed Pgp interactions for highly permeable group IIA compounds but were less responsive than monolayer efflux for low/moderate P(app) compounds of group IIB. All assays detected substrates across a broad range of P(app), but the efflux assay was more prone to fail at high P(app), whereas the calcein-AM and ATPase assays were more prone to fail at low P(app). When P(app) is low, efflux is a greater factor in the disposition of Pgp substrates. The efflux assay is more reliable at low/moderate P(app) and is the method of choice for evaluating drug candidates despite low throughput and reliance on liquid chromatography with tandem mass spectrometry.

[1]  T. Litman,et al.  Structure-activity relationships of P-glycoprotein interacting drugs: kinetic characterization of their effects on ATPase activity. , 1997, Biochimica et biophysica acta.

[2]  F. Loor,et al.  Ranking of P-glycoprotein substrates and inhibitors by a calcein-AM fluorometry screening assay. , 1996, Anti-cancer drugs.

[3]  A. Seelig A general pattern for substrate recognition by P-glycoprotein. , 1998, European journal of biochemistry.

[4]  G. A. Scarborough Drug-stimulated ATPase activity of the human P-glycoprotein , 1995, Journal of bioenergetics and biomembranes.

[5]  M. Kool,et al.  Drug export activity of the human canalicular multispecific organic anion transporter in polarized kidney MDCK cells expressing cMOAT (MRP2) cDNA. , 1998, The Journal of clinical investigation.

[6]  J. Schellens,et al.  P-glycoprotein system as a determinant of drug interactions: the case of digoxin-verapamil. , 1999, Pharmacological research.

[7]  J Ferté,et al.  Analysis of the tangled relationships between P-glycoprotein-mediated multidrug resistance and the lipid phase of the cell membrane. , 2000, European journal of biochemistry.

[8]  G Ecker,et al.  Structure-activity relationship studies of propafenone analogs based on P-glycoprotein ATPase activity measurements. , 1999, Biochemical pharmacology.

[9]  W. Kirch,et al.  P-glycoprotein inhibitor erythromycin increases oral bioavailability of talinolol in humans. , 2000, International journal of clinical pharmacology and therapeutics.

[10]  Y. Assaraf,et al.  The Role of Passive Transbilayer Drug Movement in Multidrug Resistance and Its Modulation* , 1996, The Journal of Biological Chemistry.

[11]  J. Beijnen,et al.  Limited oral bioavailability and active epithelial excretion of paclitaxel (Taxol) caused by P-glycoprotein in the intestine. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[12]  R. Larsson,et al.  Microfluorometric evaluation of calcein acetoxymethyl ester as a probe for P-glycoprotein-mediated resistance: effects of cyclosporin A and its nonimmunosuppressive analogue SDZ PSC 833. , 1994, Experimental cell research.

[13]  M. Fromm,et al.  P-glycoprotein: a defense mechanism limiting oral bioavailability and CNS accumulation of drugs. , 2000, International journal of clinical pharmacology and therapeutics.

[14]  D. Roden,et al.  The drug transporter P-glycoprotein limits oral absorption and brain entry of HIV-1 protease inhibitors. , 1998, The Journal of clinical investigation.

[15]  P. Roepe,et al.  The P-Glycoprotein Efflux Pump: How Does it Transport Drugs? , 1998, The Journal of Membrane Biology.

[16]  K. Paull,et al.  P-glycoprotein substrates and antagonists cluster into two distinct groups. , 1997, Molecular pharmacology.

[17]  Morton B. Brown,et al.  Role of intestinal P‐glycoprotein (mdr1) in interpatient variation in the oral bioavailability of cyclosporine , 1997, Clinical pharmacology and therapeutics.

[18]  A. Schinkel,et al.  P-Glycoprotein, a gatekeeper in the blood-brain barrier. , 1999, Advanced drug delivery reviews.

[19]  M. Fromm,et al.  Characterization of the major metabolites of verapamil as substrates and inhibitors of P-glycoprotein. , 2000, The Journal of pharmacology and experimental therapeutics.