Polymorphisms in human organic anion-transporting polypeptide 1A2 (OATP1A2): implications for altered drug disposition and central nervous system drug entry

J Biol Chem. 2005 Mar 11;280(10):9610-7. doi: 10.1074/jbc.M411092200. Epub 2005 Jan 4.

Abstract

Organic anion-transporting polypeptide 1A2 (OATP1A2) is a drug uptake transporter known for broad substrate specificity, including many drugs in clinical use. Therefore, genetic variation in SLCO1A2 may have important implications to the disposition and tissue penetration of substrate drugs. In the present study, we demonstrate OATP1A2 protein expression in human brain capillary and renal distal nephron using immunohistochemistry. We also determined the extent of single nucleotide polymorphisms in SLCO1A2 upon analyses of ethnically defined genomic DNA samples (n = 95 each for African-, Chinese-, European-, and Hispanic-Americans). We identified six nonsynonymous polymorphisms within the coding region of SLCO1A2 (T38C (I13T), A516C (E172D), G559A (A187T), A382T (N128Y), A404T (N135I), and C2003G (T668S)), the allelic frequencies of which appeared to be ethnicity-dependent. In vitro functional assessment revealed that the A516C and A404T variants had markedly reduced capacity for mediating the cellular uptake of OATP1A2 substrates, estrone 3-sulfate and two delta-opioid receptor agonists, deltorphin II, and [D-penicillamine(2,5)]-enkephalin. On the other hand, the G559A and C2003G variants appeared to have substrate-dependent changes in transport activity. Cell surface biotinylation and immunofluorescence confocal microscopy suggested that altered plasma membrane expression of the transporter may contribute to reduced transport activity associated with the A516C, A404T, and C2003G variants. The A404T (N135I) variant also showed a shift in the apparent molecular size, indicative of alterations in glycosylation status. Taken together, these data suggest that SLCO1A2 polymorphisms may be an important yet unrecognized contributor to inter-individual variability in drug disposition and central nervous system entry of substrate drugs.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Brain / physiology
  • Enkephalin, D-Penicillamine (2,5)- / pharmacology
  • Estrone / analogs & derivatives*
  • Estrone / pharmacology
  • Humans
  • Kidney / physiology
  • Kinetics
  • Liver / physiology
  • Liver-Specific Organic Anion Transporter 1 / chemistry
  • Liver-Specific Organic Anion Transporter 1 / genetics*
  • Models, Molecular
  • Molecular Sequence Data
  • Oligopeptides / pharmacology
  • Organ Specificity
  • Polymorphism, Genetic*
  • Polymorphism, Single Nucleotide
  • Protein Conformation
  • Protein Structure, Secondary

Substances

  • Liver-Specific Organic Anion Transporter 1
  • Oligopeptides
  • deltorphin II, Ala(2)-
  • Estrone
  • Enkephalin, D-Penicillamine (2,5)-
  • estrone sulfate