Disease relevance of Akr1c6

• Moreover, based on the molecular weights and the co-substrate specificities microsomal mouse liver MPON reductase and Pseudomonas 3 alpha-HSD seem to be members of the short-chain alcohol dehydrogenase family [1].

High impact information on Akr1c6

• ALLO and THDOC are synthesized in the brain from progesterone or deoxycorticosterone, respectively, by the sequential action of two enzymes: 5alpha-reductase (5alpha-R) type I and 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD) [2].
• Using glutamic acid decarboxylase 67/65 antibodies to mark GABAergic neurons, we failed to detect 5alpha-R type I and 3alpha-HSD in cortical and hippocampal GABAergic interneurons [2].
• Neither 5alpha-R type I nor 3alpha-HSD mRNAs are expressed in S100beta- or glial fibrillary acidic protein-positive glial cells [2].
• We demonstrate that 5alpha-R type I and 3alpha-HSD colocalize in cortical, hippocampal, and olfactory bulb glutamatergic principal neurons and in some output neurons of the amygdala and thalamus [2].
• This study evaluates 5alpha-R type I and 3alpha-HSD mRNA expression level in mouse brain by using in situ hybridization combined with glutamic acid decarboxylase 67/65, vesicular glutamate transporter 2, glial fibrillary acidic protein, and S100beta immunohistochemistry [2].

Chemical compound and disease context of Akr1c6

• 3 Alpha-hydroxysteroid dehydrogenase (3 alpha-HSD) from Pseudomonas testosteroni was shown to reduce the xenobiotic carbonyl compound metyrapone (MPON) [1].

Biological context of Akr1c6

• The transfection of vectors expressing types 1 and 3 3 alpha-HSD in transformed human embryonic kidney (HEK-293) cells indicates that both enzymes efficiently catalyze the transformation of dihydrotestosterone into 3 alpha-diol in intact cells [3].
• Based on enzymatic characteristics and sequence homology, it is suggested that type 1 3 alpha-HSD is an ortholog of rat 3 alpha-HSD while type 3 3 alpha-HSD, which must have diverged recently, seems unique to human and is probably more involved in intracrine activity [3].
• In this report, we describe the isolation of a mouse 3alpha-HSD cDNA and the characterization of its substrate specificity and tissue distribution [4].

Anatomical context of Akr1c6

• Reversely, MPON reductase purified from mouse liver microsomes and previously characterized as aldehyde reductase, was competitively inhibited by 3 alpha-HSD steroid substrates [1].

Associations of Akr1c6 with chemical compounds

• The purified enzyme was a 36-kDa monomer, and showed both 17beta-HSD and 3alpha-HSD activities in the presence of NADP(H) as the coenzymes [5].
• The best known 3 alpha-HSD activity is the transformation of the most potent natural androgen, dihydrotestosterone, into 5 alpha-androstan-3 alpha,17 beta-diol (3 alpha-diol), a compound having much lower activity [3].
• The mechanism by which fluoxetine and other selective serotonin reuptake inhibitors normalize 3alpha,5alpha-TH PROG CSF levels appears to involve a direct stimulation of 3alpha-hydroxysteroidoxidoreductase (3alpha-HSD), an enzyme that catalyses the reduction of 5alpha-DH PROG into 3alpha,5alpha-TH PROG [6].
• 5. Synthesis and inactivation of 5alpha-dihydrotestosterone occur through 5alpha-reductase and 3alpha-HSD activities, respectively [7].

Other interactions of Akr1c6

• The properties of AKR1C20 are distinct from those of previously known mouse 17beta-HSD type 5 (AKR1C6), 3alpha-HSD (AKR1C14) and other members of the AKR1C subfamily [5].

Analytical, diagnostic and therapeutic context of Akr1c6

• Sequence analysis indicates that m3alpha-HSD shares 87% amino acid identity with rat 3alpha-HSD [4].

References