![]()
|
|
||||||||
J. Biol. Chem., Vol. 262, Issue 11, 4939-4942, Apr, 1987
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.
Estrogen induces transcription of the Xenopus laevis serum retinol- binding protein gene
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
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. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |