Linked Life Data

11013348

Source:http://linkedlifedata.com/resource/pubmed/id/11013348

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-12-11
pubmed:abstractText
It has been suggested that 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD) is a T-cell differentiation marker in mice. In the human, this enzyme has generally been associated with types 1 and 2 17beta-HSDs, which belong to the short-chain alcohol dehydrogenase family, whereas the rat, rabbit, pig and bovine 20alpha-HSDs are members of the aldoketo reductase superfamily, which also includes the 3alpha-HSD family. In this study, we report the cloning, from a human skin cDNA library, of a cDNA that shows, after transfection into human embryonic kidney (HEK-293) cells, high 20alpha-HSD activity but negligible 3alpha- and 17beta-hydroxysteroid dehydrogenase activities. A comparison of the amino acid sequence of the human 20alpha-HSD with those of other related 20alpha- and 3alpha-HSDs indicates that the human 20alpha-HSD shares 79.9, 68.7 and 52.3% identity with rabbit, rat and bovine 20alpha-HSDs, whereas it shows 97, 84 and 65% identity with human type 3, type 1 and rat 3alpha-HSDs. In contrast, the enzyme shares only 15.2 and 15.0% identity with type 1 and type 2 human 17beta-HSDs. DNA analysis predicts a protein of 323 amino acids, with a calculated molecular weight of 36 767 Da. In intact transfected cells, the human 20alpha-HSD preferentially catalyzes the reduction of progesterone to 20alpha-hydroxyprogesterone with a K(m) value of 0.6 microM, the reverse reaction (oxidation) being negligible. In a cell cytosolic preparation, the enzyme could use both NADPH and NADH as cofactors, but NADPH, which gave 4-fold lower K(m) values, was preferred. We detected the expression of 20alpha-HSD mRNA in liver, prostate, testis, adrenal, brain, uterus and mammary-gland tissues and in human keratinocyte (HaCaT) cells. The present study clearly indicates that the genuine human 20alpha-HSD belongs to the aldoketo reductase family, like the 20alpha-HSDs from other species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0952-5041
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
221-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11013348-20-Hydroxysteroid Dehydrogenases, pubmed-meshheading:11013348-20-alpha-Hydroxysteroid Dehydrogenase, pubmed-meshheading:11013348-Amino Acid Sequence, pubmed-meshheading:11013348-Animals, pubmed-meshheading:11013348-Base Sequence, pubmed-meshheading:11013348-Cattle, pubmed-meshheading:11013348-Cell Line, pubmed-meshheading:11013348-Cloning, Molecular, pubmed-meshheading:11013348-DNA, Complementary, pubmed-meshheading:11013348-DNA Primers, pubmed-meshheading:11013348-Female, pubmed-meshheading:11013348-Gene Expression, pubmed-meshheading:11013348-Humans, pubmed-meshheading:11013348-Male, pubmed-meshheading:11013348-Mice, pubmed-meshheading:11013348-Molecular Sequence Data, pubmed-meshheading:11013348-NADP, pubmed-meshheading:11013348-RNA, Messenger, pubmed-meshheading:11013348-Rabbits, pubmed-meshheading:11013348-Rats, pubmed-meshheading:11013348-Sequence Homology, Amino Acid, pubmed-meshheading:11013348-Tissue Distribution, pubmed-meshheading:11013348-Transfection
pubmed:year
2000
pubmed:articleTitle
Characterization of a human 20alpha-hydroxysteroid dehydrogenase.
pubmed:affiliation
Oncology and Molecular Endocrinology Research Center, CHUQ PCHUL and Laval University, Quebec, Quebec G1V 4G2, Canada.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't