PMID- 16191478
OWN - NLM
STAT- MEDLINE
DCOM- 20060323
LR  - 20131121
IS  - 0960-0760 (Print)
IS  - 0960-0760 (Linking)
VI  - 98
IP  - 1
DP  - 2006 Jan
TI  - Isolation and characterization of a cDNA encoding mouse 3alpha-hydroxysteroid 
      dehydrogenase: an androgen-inactivating enzyme selectively expressed in female 
      tissues.
PG  - 18-24
AB  - 3alpha-Hydroxysteroid dehydrogenase catalyzes the transformation of 
      3-ketosteroids into 3alpha-hydroxysteroids, thus playing an important role in 
      androgen and progesterone metabolism. So far, mouse cDNA and gene encoding 
      3alpha-HSD has not been reported. In this report, we describe the isolation of a 
      mouse 3alpha-HSD cDNA and the characterization of its substrate specificity and 
      tissue distribution. Sequence analysis indicates that m3alpha-HSD shares 87% 
      amino acid identity with rat 3alpha-HSD. Cells stably transfected with this 
      enzyme catalyze the transformation of dihydrotestosterone (DHT), 
      5alpha-androstanedione (5alpha-dione) and dihydroprogesterone (DHP) into 
      5alpha-androstane-3alpha,17beta-diol (3alpha-diol), androsterone (ADT) and 
      5alpha-pregnan-3alpha-ol-20-one (allopregnanolone), respectively. Quantification 
      of mRNA expression levels of this enzyme was determined in male and female mouse 
      sex-specific tissues using quantitative Realtime PCR. We show that this enzyme is 
      mainly expressed in female-specific tissues while being almost absent from 
      male-specific tissues. In the liver, the same expression level is seen in both 
      male and female, while there is 6-fold higher expression level in female 
      pituitary than in male. These results strongly suggest that m3alpha-HSD could 
      play an important role in the female mouse physiology similar to that of type 1 
      5alpha-reductase with which it works in tandem. This role could be related to the 
      inactivation of excess of androgen and progesterone that are more severely 
      regulated than in man.
FAU - Bellemare, Veronique
AU  - Bellemare V
AD  - Oncology and Molecular Endocrinology Research Center, Laval University Medical 
      Center (CHUL), 2705 Laurier Boulevard, Que., Canada G1V 4G2.
FAU - Labrie, Fernand
AU  - Labrie F
FAU - Luu-The, Van
AU  - Luu-The V
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20050926
PL  - England
TA  - J Steroid Biochem Mol Biol
JT  - The Journal of steroid biochemistry and molecular biology
JID - 9015483
RN  - 0 (DNA, Complementary)
RN  - 0 (RNA, Messenger)
RN  - 08J2K08A3Y (Dihydrotestosterone)
RN  - 145-14-2 (20-alpha-Dihydroprogesterone)
RN  - 25126-76-5 (Androstane-3,17-diol)
RN  - 40GP35YQ49 (Desoxycorticosterone)
RN  - C24W7J5D5R (Androsterone)
RN  - EC 1.1.1.50 (3-alpha-Hydroxysteroid Dehydrogenase (B-Specific))
SB  - IM
MH  - 20-alpha-Dihydroprogesterone/metabolism
MH  - 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)/*genetics/metabolism
MH  - Amino Acid Sequence
MH  - Androstane-3,17-diol/metabolism
MH  - Androsterone/metabolism
MH  - Animals
MH  - Cloning, Molecular
MH  - DNA, Complementary/*isolation & purification
MH  - Desoxycorticosterone/metabolism
MH  - Dihydrotestosterone/metabolism
MH  - Female
MH  - Gene Expression Regulation, Enzymologic/*physiology
MH  - Genitalia, Female/*enzymology
MH  - Liver/enzymology
MH  - Male
MH  - Mammary Glands, Animal/*enzymology
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Molecular Sequence Data
MH  - RNA, Messenger/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
MH  - Tissue Distribution
EDAT- 2005/09/30 09:00
MHDA- 2006/03/24 09:00
CRDT- 2005/09/30 09:00
PHST- 2005/02/15 00:00 [received]
PHST- 2005/07/18 00:00 [accepted]
PHST- 2005/09/30 09:00 [pubmed]
PHST- 2006/03/24 09:00 [medline]
PHST- 2005/09/30 09:00 [entrez]
AID - S0960-0760(05)00356-0 [pii]
AID - 10.1016/j.jsbmb.2005.07.004 [doi]
PST - ppublish
SO  - J Steroid Biochem Mol Biol. 2006 Jan;98(1):18-24. doi: 
      10.1016/j.jsbmb.2005.07.004. Epub 2005 Sep 26.