Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1993-5-20
pubmed:abstractText
A 56 kDa protein expressed in human genital skin fibroblasts was first identified by independent laboratories on the basis of its specific expression in androgen target cells and its ability to covalently bind androgenic affinity ligands. Recently, immunoscreening of a cDNA library with antisera directed against this protein resulted in the isolation of a partial cDNA clone identical to human cytosolic aldehyde dehydrogenase (ALDH1). We report here the preparation of a full-length cDNA encoding ALDH1 from human genital fibroblasts. Translation of the encoded protein in a cell-free system yields a 56 kDa product that can be covalently radiolabeled with [3H]dihydrotestosterone 17 beta-bromoacetate (DHT-BA). Expression of the full-length clone in mammalian cells also results in expression of a 56 kDa DHT-BA binding protein. The covalent binding of DHT-BA by ALDH1 is an intrinsic property of the enzyme and is not dependent on androgen receptor expression.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
An androgenic affinity ligand covalently binds to cytosolic aldehyde dehydrogenase from human genital skin fibroblasts.
pubmed:affiliation
Department of Medicine, Vanderbilt University School of Medicine, Nashville, TN 37232.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't