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Titolo:
Application of photoaffinity labeling with [H-3] all trans- and 9-cis-retinoic acids for characterization of cellular retinoic acid-binding proteins I and II
Autore:
Radominska-Pandya, A; Chen, GP; Samokyszyn, VM; Little, JM; Gall, WE; Zawada, G; Terrier, N; Magdalou, J; Czernik, P;
Indirizzi:
Univ Arkansas Med Sci, Dept Biochem & Mol Biol, Little Rock, AR 72205 USA Univ Arkansas Med Sci Little Rock AR USA 72205 Little Rock, AR 72205 USA Univ Arkansas Med Sci, Dept Pharmacol & Toxicol, Little Rock, AR 72205 USAUniv Arkansas Med Sci Little Rock AR USA 72205 Little Rock, AR 72205 USA Univ Henri Poincare, CNRS, UMR 7561, Fac Med, Vandoeuvre Nancy, France Univ Henri Poincare Vandoeuvre Nancy France d, Vandoeuvre Nancy, France
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 1, volume: 10, anno: 2001,
pagine: 200 - 211
SICI:
0961-8368(200101)10:1<200:AOPLW[>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-LIVER MICROSOMES; CHEMICAL SYNTHESIS; BETA-GLUCURONIDE; 13-CIS-RETINOYL GLUCURONIDES; BIOLOGICAL-ACTIVITY; METABOLISM INVIVO; BILE-ACIDS; RAT-LIVER; BIOSYNTHESIS; EXPRESSION;
Keywords:
cellular retinoic acid-binding protein; photoaffinity labeling; all-trans-retinoic acid; 9-cis-retinoic acid; retinoic acid glucuronide; 5,6-epoxy-retinoic acid;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Radominska-Pandya, A Univ Arkansas Med Sci, Dept Biochem & Mol Biol, 4301 W Markham,Slot 516, Little Rock, AR 72205 USA Univ Arkansas Med Sci 4301 W Markham,Slot 516 Little Rock AR USA 72205
Citazione:
A. Radominska-Pandya et al., "Application of photoaffinity labeling with [H-3] all trans- and 9-cis-retinoic acids for characterization of cellular retinoic acid-binding proteins I and II", PROTEIN SCI, 10(1), 2001, pp. 200-211

Abstract

Cellular retinoic acid-binding proteins (CRABPs) are carrier proteins thought to play a crucial role in the transport and metabolism of all-trans-retinoic acid (atRA) and its derivatives within the cell. This report describes a novel photoaffinity-based binding assay involving competition between potential ligands of CRABP and [H-3]atRA or [H-3]-9-cis-RA for binding to the atRA-binding sites of CRABP I and II. Photoaffinity labeling of purified CRABPs with [H-3]atRA was light- and concentration-dependent, saturable, and protected by several retinoids in a concentration-dependent manner, indicating that binding occurred in the CRABP atRA-binding site. Structure-function relationship studies demonstrated that oxidative changes to the atRA beta -ionone ring did not affect ligand potency. However, derivatives lackinga terminal carboxyl group and some cis isomers did not bind to CRABPs, These studies also identified two novel ligands for CRABPs: 5,6-epoxy-RA and retinoyl-beta -D-glucuronide (RAG), The labeling of both CRABPs with 9-cis-RA occurred with much lower affinity. Experimental evidence excluded nonspecific binding of RAG to CRABPs and UDP-glucuronosyltransferases, the enzymesresponsible for RAG synthesis. These results established that RAG is an effective ligand of CRABPs. Therefore, photoaffinity labeling with [H-3]atRA can be used to identify new ligands for CRABP and retinoid nuclear receptors and also provide information concerning the identity of amino acid(s) localized in the atRA-binding site of these proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 19:28:20