PMID- 10425199
OWN - NLM
STAT- MEDLINE
DCOM- 19990908
LR  - 20200124
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 261
IP  - 2
DP  - 1999 Aug 2
TI  - Molecular cloning of rat efp: expression and regulation in primary osteoblasts.
PG  - 412-8
AB  - 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.
CI  - Copyright 1999 Academic Press.
FAU - Inoue, S
AU  - Inoue S
AD  - Department of Biochemistry, Saitama Medical School, 38 Moro-Hongo,
      Moroyama-machi, Iruma-gun, Saitama, 350-0495, Japan.
FAU - Urano, T
AU  - Urano T
FAU - Ogawa, S
AU  - Ogawa S
FAU - Saito, T
AU  - Saito T
FAU - Orimo, A
AU  - Orimo A
FAU - Hosoi, T
AU  - Hosoi T
FAU - Ouchi, Y
AU  - Ouchi Y
FAU - Muramatsu, M
AU  - Muramatsu M
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (DNA, Complementary)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Estrogens)
RN  - 0 (RNA, Messenger)
RN  - 0 (Transcription Factors)
RN  - 0 (Transforming Growth Factor beta)
RN  - 0 (Trim25 protein, mouse)
RN  - 0 (Trim25 protein, rat)
RN  - 0 (Tripartite Motif Proteins)
RN  - EC 2.3.2.27 (TRIM25 protein, human)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
RN  - FXC9231JVH (Calcitriol)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Calcitriol/pharmacology
MH  - Cell Differentiation/drug effects/physiology
MH  - Cells, Cultured
MH  - Cloning, Molecular
MH  - DNA, Complementary/genetics
MH  - DNA-Binding Proteins/chemistry/*genetics/metabolism
MH  - Down-Regulation/drug effects
MH  - Estrogens/metabolism
MH  - Gene Expression Regulation
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Osteoblasts/cytology/drug effects/*metabolism
MH  - RNA, Messenger/genetics/metabolism
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Species Specificity
MH  - Transcription Factors/chemistry/*genetics/metabolism
MH  - Transforming Growth Factor beta/pharmacology
MH  - Tripartite Motif Proteins
MH  - Ubiquitin-Protein Ligases
MH  - Zinc Fingers/genetics
EDAT- 1999/07/30 00:00
MHDA- 1999/07/30 00:01
CRDT- 1999/07/30 00:00
PHST- 1999/07/30 00:00 [pubmed]
PHST- 1999/07/30 00:01 [medline]
PHST- 1999/07/30 00:00 [entrez]
AID - 10.1006/bbrc.1999.0874 [doi]
AID - S0006-291X(99)90874-4 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Aug 2;261(2):412-8. doi: 10.1006/bbrc.1999.0874.