The activity of 3 beta-hydroxysteroid dehydrogenase delta 4-5 isomerase (3 beta-HSD) was assayed in various tissues microdissected from the freeze-dried human skin of 13 subjects. The sebaceous gland possessed the highest activity of 3 beta-HSD in the skin, while the apocrine sweat gland showed only
cDNA cloning and physical mapping of porcine 3β-hydroxysteroid dehydrogenase/Δ5-Δ4 isomerase
✍ Scribed by A. Von Teichman; H. Joerg; P. Werner; B. Brenig; G. Stranzinger
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 168 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0268-9146
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✦ Synopsis
The 3__β__‐hydroxysteroid dehydrogenase/Δ__5‐Δ__4‐isomerase (3__β‐HSD) enzymes are essential for the biosynthesis of steroid hormones. The 3__β‐HSD gene family has been reported to encode for different isoenzymes which function either as dehydrogenase/isomerase or as reductase. The 3__β__‐HSD enzymes are involved in the formation of the pheromone androstenone (5__α__‐androst‐16‐ene‐3‐one) which contributes to the unpleasant odour present in the meat of uncastrated boars. An reverse‐transcription–polymerase chain reaction (RT–PCR) probe from porcine testicular tissue of a 3__β__‐HSD enzyme was used to screen a porcine adipose tissue cDNA library. Both strands of the positive clones were sequenced and the putative coding sequence of 1122 nucleotides encodes 374 amino acids. Comparison of the putative open reading frame with the bovine and the human type I homologues revealed 85.6 and 79.3% identity, respectively. Fluorescence in situ hybridization (FISH) was performed with a labelled PAC clone containing the gene of interest. The 3__β__‐HSD gene was mapped to the porcine chromosome 4q16‐4q21 which is in accordance with the comparative gene map.
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