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J. Biol. Chem., Vol. 262, Issue 11, 4939-4942, Apr, 1987

Estrogen induces transcription of the Xenopus laevis serum retinol- binding protein gene

DM McKearin, MC Barton, MJ Keller and DJ Shapiro

We have isolated and sequenced a full-length cDNA cloned tentatively identified as encoding Xenopus laevis serum retinol-binding protein (RBP) mRNA. The derived amino acid sequence of the Xenopus protein is 63% homologous to the sequence of the human RBP. 17 of 19 amino acids identified as critical in the retinol-binding pocket of human RBP are identical or conservative replacements in the Xenopus protein. The RBP cDNA clone has been used as a hybridization probe to demonstrate that administration of estradiol-17 beta to male X. laevis induces hepatic RBP mRNA 10-fold from its constitutive in vivo level of 1,800 molecules/cell to approximately 18,000 molecules/cell. Using a simplified method for determining relative rates of gene transcription, we demonstrate an estrogen-mediated increase in the rate of RBP gene transcription. These quantitative data provide the first demonstration that a steroid hormone regulates the levels of vertebrate retinol- binding protein mRNA.
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D. Bellovino, T. Morimoto, E. Mengheri, G. Perozzi, I. Garaguso, F. Nobili, and S. Gaetani
Unique Biochemical Nature of Carp Retinol-binding Protein. N-LINKED GLYCOSYLATION AND UNCLEAVABLE NH2-TERMINAL SIGNAL PEPTIDE
J. Biol. Chem., April 20, 2001; 276(17): 13949 - 13956.
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