| Literature DB >> 27416800 |
Cara H Nelson1, Chi-Chi Peng1, Justin D Lutz1, Catherine K Yeung1, Alex Zelter2, Nina Isoherranen1.
Abstract
Cellular retinoic acid binding proteins (CRABPs) bind all-trans-retinoic acid (atRA) tightly. This study aimed to determine whether atRA is channeled directly to cytochrome P450 (CYP) CYP26B1 by CRABPs, and whether CRABPs interact directly with CYP26B1. atRA bound to CRABPs (holo-CRABP) was efficiently metabolized by CYP26B1. Isotope dilution experiments showed that delivery of atRA to CYP26B1 in solution was similar with or without CRABP. Holo-CRABPs had higher affinity for CYP26B1 than free atRA, but both apo-CRABPs inhibited the formation of 4-OH-RA by CYP26B1. Similar protein-protein interactions between soluble binding proteins and CYPs may be important for other lipophilic CYP substrates.Entities:
Keywords: binding proteins; cytochrome P450; retinoic acid; substrate channeling
Mesh:
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Year: 2016 PMID: 27416800 PMCID: PMC4997814 DOI: 10.1002/1873-3468.12303
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124