Retinoyl beta-glucuronide: lack of binding to receptor proteins of retinoic acid as related to biological activity.
Biochem Pharmacol
; 43(4): 919-22, 1992 Feb 18.
Article
em En
| MEDLINE
| ID: mdl-1311592
ABSTRACT
Retinoid beta-glucuronides have emerged as biologically active, water-soluble, natural retinoids with relatively few toxic and teratogenic effects. The mechanism of action of these glucuronides in the control of epithelial differentiation, growth, and tumorigenesis is unknown. Since retinoyl beta-glucuronide (RAG) contains a free carboxyl group, we studied the interactions of RAG with cellular retinoic acid-binding protein (CRABP) and nuclear receptors of retinoic acid (RARs), the possible mediators of the biological action of retinoic acid (RA). RAG did not exhibit any significant affinity to bind either CRABP or RARs. During 24- and 48-hr incubations of RAG in chick cytosol, detectable amounts of RA were generated which interacted with the RA receptors. In chick skin, the biological activity of RAG may be due to this slowly released RA. Other possible modes of action of RAG are suggested.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pele
/
Tretinoína
/
Proteínas Nucleares
/
Proteínas de Transporte
Limite:
Animals
Idioma:
En
Revista:
Biochem Pharmacol
Ano de publicação:
1992
Tipo de documento:
Article