Retinyl methyl ether: binding to transport proteins and effect on transcriptional regulation.
Retinyl methyl ether (RME) which prevents cancers of the rat mammary gland, binds to cellular retinol-binding protein and serum retinol- binding protein but not to cellular retinoic acid-binding protein or to the nuclear retinoid receptors, RARs/RXRs. Since the biochemical effects of retinoids likely involve activation or suppression of RAR/RXR-mediated gene transcription, we evaluated such activity of RME by performing cotransfection assays involving CV-1 cells, expression vectors containing RAR and/or RXR cDNA, and an appropriate reporter vector. In the concentration range of 10(-9)-10(-6), RME did not activate transcription by either of the heterodimers (RARalpha, beta or gamma/RXR alpha) or the homodimer (RARalpha/RARalpha). The retinoid, however, exhibited concentration-dependent inhibitory effects on the basal level of transcriptional activity (no other retinoid added) of both the RAR beta- and RARgamma/RXRalpha heterodimers and of the retinoic acid-induced transcriptional activation of the RARgamma/RXRalpha receptors. Thus, RME acted as a retinoic acid antagonist, a role possibly involved in its cancer preventive activity.[1]References
- Retinyl methyl ether: binding to transport proteins and effect on transcriptional regulation. Sani, B.P., Zhang, X., Hill, D.L., Shealy, Y.F. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
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