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The blood-brain barrier thyroxine transporter organic anion-transporting polypeptide 1c1 displays atypical transport kinetics.
Westholm, Daniel E; Salo, David R; Viken, Kevin J; Rumbley, Jon N; Anderson, Grant W.
Afiliación
  • Westholm DE; Department of Pharmacy Practice and Pharmaceutical Sciences, College of Pharmacy, University of Minnesota-Duluth, Duluth, Minnesota 55812, USA.
Endocrinology ; 150(11): 5153-62, 2009 Nov.
Article en En | MEDLINE | ID: mdl-19819953
Organic anion-transporting polypeptide (Oatp) 1c1 is a high-affinity T(4) transporter expressed in brain barrier cells. Oatp1c1 transports a variety of additional ligands including the conjugated sterol estradiol 17beta-glucuronide (E(2)17betaG). Intriguingly, published data suggest that E(2)17betaG inhibition of Oatp1c1-mediated T(4) transport exhibits characteristics suggestive of atypical transport kinetics. To determine whether Oatp1c1 exhibits atypical transport kinetics, we first performed detailed T(4) and E(2)17betaG uptake assays using Oatp1c1 stably transfected HEK293 cells and a wide range of T(4) and E(2)17betaG concentrations (100 pm to 300 nm and 27 nm to 200 mum, respectively). Eadie-Hofstee plots derived from these detailed T(4) and E(2)17betaG uptake experiments display a biphasic profile consistent with atypical transport kinetics. These data along with T(4) and E(2)17betaG cis-inhibition dose-response measurements revealed shared high- and low-affinity Oatp1c1 binding sites for T(4) and E(2)17betaG. T(4) and E(2)17betaG recognized these Oatp1c1 binding sites with opposite preferences. In addition, sterols glucuronidated in the 17 or 21 position, exhibited preferential substrate-dependent inhibition of Oatp1c1 transport, inhibiting Oatp1c1-mediated E(2)17betaG transport more strongly than T(4) transport. Together these data reveal that Oatp1c1-dependent substrate transport is a complex process involving substrate interaction with multiple binding sites and competition for binding with a variety of other substrates. A thorough understanding of atypical Oatp1c1 transport processes and substrate-dependent inhibition will allow better prediction of endo- and xenobiotic interactions with the Oatp transporter.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tiroxina / Barrera Hematoencefálica / Proteínas de Transporte de Catión Orgánico Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Endocrinology Año: 2009 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tiroxina / Barrera Hematoencefálica / Proteínas de Transporte de Catión Orgánico Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Endocrinology Año: 2009 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos