An androgenic affinity ligand covalently binds to cytosolic aldehyde dehydrogenase from human genital skin fibroblasts

Daniel K. McCammon, Ping Zhou, Maxine K. Turney, Michael J. McPhaul, William J. Kovacs

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

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 17β-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.

Original languageEnglish (US)
Pages (from-to)177-183
Number of pages7
JournalMolecular and Cellular Endocrinology
Volume91
Issue number1-2
DOIs
StatePublished - Feb 1993
Externally publishedYes

Keywords

  • (Human)
  • Aldehyde dehydrogenase (ALDH1)
  • Androgenic affinity ligand
  • Genital fibroblast

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Fingerprint Dive into the research topics of 'An androgenic affinity ligand covalently binds to cytosolic aldehyde dehydrogenase from human genital skin fibroblasts'. Together they form a unique fingerprint.

  • Cite this