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Publication : Molecular cloning of rat efp: expression and regulation in primary osteoblasts.

First Author  Inoue S Year  1999
Journal  Biochem Biophys Res Commun Volume  261
Issue  2 Pages  412-8
PubMed ID  10425199 Mgi Jnum  J:56705
Mgi Id  MGI:1342199 Doi  10.1006/bbrc.1999.0874
Citation  Inoue S, et al. (1999) Molecular cloning of rat efp: expression and regulation in primary osteoblasts. Biochem Biophys Res Commun 261(2):412-8
abstractText  We have previously identified an estrogen-responsive gene, efp (estrogen-responsive finger protein), by genomic binding-site cloning method. Here, we isolated a rat homologue of efp cDNA that encodes an open reading frame of 644 amino acids sharing high homology with human efp (69% identity at the protein level) and mouse efp (80% identity at the protein level). The efp protein has a RING finger, a variant type of zinc finger motif, B1 box and B2 box, each having a pair of zinc fingers, and coiled-coil domain, belonging to the RING finger-B box-Coiled Coil (RBCC) family. Several members of RBCC family including efp have characteristic C-terminal domain, forming a subfamily. Next, we detected efp mRNA in primary osteoblasts, one of estrogen target cells, derived from the calvariae of rat fetus. An anti-efp antibody revealed the efp protein is expressed and regulated by estrogen in the primary osteoblasts. Interestingly, the efp protein in primary osteoblasts is down-regulated by 1alpha,25-dihydroxyvitamin D(3) treatment that promotes the differentiation of the cells, whereas it is up-regulated by TGF-beta1 treatment that inhibits the differentiation of the cells. These findings suggest the possible involvement of the efp in the differentiation of osteoblastic cells. Copyright 1999 Academic Press.
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