Apical/Basolateral Surface Expression of Drug Transporters and its Role in Vectorial Drug Transport View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-09-22

AUTHORS

Kousei Ito, Hiroshi Suzuki, Toshiharu Horie, Yuichi Sugiyama

ABSTRACT

It is well known that transporter proteins play a key role in governing drug absorption, distribution, and elimination in the body, and, accordingly, they are now considered as causes of drug–drug interactions and interindividual differences in pharmacokinetic profiles. Polarized tissues directly involved in drug disposition (intestine, kidney, and liver) and restricted distribution to naive sanctuaries (blood–tissue barriers) asymmetrically express a variety of drug transporters on the apical and basolateral sides, resulting in vectorial drug transport. For example, the organic anion transporting polypeptide (OATP) family on the sinusoidal (basolateral) membrane and multidrug resistance-associated protein 2 (MRP2/ABCC2) on the apical bile canalicular membrane of hepatocytes take up and excrete organic anionic compounds from blood to bile. Such vectorial transcellular transport is fundamentally attributable to the asymmetrical distribution of transporter molecules in polarized cells. Besides the apical/basolateral sorting direction, distribution of the transporter protein between the membrane surface (active site) and the intracellular fraction (inactive site) is of practical importance for the quantitative evaluation of drug transport processes. The most characterized drug transporter associated with this issue is MRP2 on the hepatocyte canalicular (apical) membrane, and it is linked to a genetic disease. Dubin–Johnson syndrome is sometimes caused by impaired canalicular surface expression of MRP2 by a single amino acid substitution. Moreover, single nucleotide polymorphisms in OATP-C/SLC21A6 (SLCO1B1) also affect membrane surface expression, and actually lead to the altered pharmacokinetic profile of pravastatin in healthy subjects. In this review article, the asymmetrical transporter distribution and altered surface expression in polarized tissues are discussed. More... »

PAGES

1559-1577

References to SciGraph publications

  • 2004-10. Functional Analysis of SNPs Variants of BCRP/ABCG2 in PHARMACEUTICAL RESEARCH
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  • 2002-02-01. Tissue Distribution and Induction of Human Multidrug Resistant Protein 3 in LABORATORY INVESTIGATION
  • 2003-04-01. Detection of the Human Organic Anion Transporters SLC21A6 (OATP2) and SLC21A8 (OATP8) in Liver and Hepatocellular Carcinoma in LABORATORY INVESTIGATION
  • 2001-12. The Role of Half-Transporters in Multidrug Resistance in JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
  • 2002-06-17. Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes in NATURE GENETICS
  • 2003-08-07. The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology in PFLÜGERS ARCHIV - EUROPEAN JOURNAL OF PHYSIOLOGY
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  • 2001-08. Characterizing the Expression of CYP3A4 and Efflux Transporters (P-gp, MRP1, and MRP2) in CYP3A4-Transfected Caco-2 Cells After Induction with Sodium Butyrate and the Phorbol Ester 12-O-Tetradecanoylphorbol-13-Acetate in PHARMACEUTICAL RESEARCH
  • 2001-08. Sinusoidal Efflux of Taurocholate Is Enhanced in Mrp2-Deficient Rat Liver in PHARMACEUTICAL RESEARCH
  • 1999-01. Primary systemic carnitine deficiency is caused by mutations in a gene encoding sodium ion-dependent carnitine transporter in NATURE GENETICS
  • 2001-08-24. Localization of organic anion transporting polypeptide 4 (Oatp4) in rat liver and comparison of its substrate specificity with Oatp1, Oatp2 and Oatp3 in PFLÜGERS ARCHIV - EUROPEAN JOURNAL OF PHYSIOLOGY
  • 2003-06-04. Polymorphisms of OATP‐C (SLC21A6) and OAT3 (SLC22A8) genes: Consequences for pravastatin pharmacokinetics in CLINICAL PHARMACOLOGY & THERAPEUTICS
  • 2004-05-17. Subcellular localization of the ABCG2 transporter in normal and malignant human gallbladder epithelium in LABORATORY INVESTIGATION
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s11095-005-6810-2

    DOI

    http://dx.doi.org/10.1007/s11095-005-6810-2

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1012773557

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/16180115


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    97 naive sanctuaries
    98 nucleotide polymorphisms
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    107 process
    108 profile
    109 protein
    110 protein 2
    111 quantitative evaluation
    112 resistance
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    114 role
    115 side
    116 single amino acid substitution
    117 single nucleotide polymorphisms
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    119 subjects
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    121 surface
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    124 tissue
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    126 transport
    127 transport processes
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