Androgen resistance due to decreased amounts of androgen receptor

A reinvestigation

Placido B. Grino, Jim Griffin III, Jean D. Wilson

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

To provide insight into the pathogenesis of the androgen resistance in a previously described family with X-linked Reifenstein syndrome, we have systematically assessed a variety of parameters of androgen receptor function in fibroblasts cultured from scrotal skin biopsies. We assessed the amount of high affinity binding, the affinity of ligand binding to the receptor, the upregulation of androgen receptor levels by androgen, the stability of ligand binding in intact fibroblasts at high temperature, the dissociation of ligand from the receptor, the intranuclear localization and salt elution profiles of ligand-receptor complexes, and the ultracentrifugation characteristics of the ligand-receptor complexes. Since the only parameter found to be abnormal is a decreased amount of receptor, we conclude that the underlying mutation in this family influences the amount rather than the structure of the androgen receptor protein.

Original languageEnglish (US)
Pages (from-to)647-654
Number of pages8
JournalJournal of Steroid Biochemistry
Volume35
Issue number6
DOIs
StatePublished - 1990

Fingerprint

Androgen Receptors
Androgens
Ligands
Fibroblasts
Androgen-Insensitivity Syndrome
Biopsy
Ultracentrifugation
Skin
Up-Regulation
Salts
Mutation
Temperature
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

Cite this

Androgen resistance due to decreased amounts of androgen receptor : A reinvestigation. / Grino, Placido B.; Griffin III, Jim; Wilson, Jean D.

In: Journal of Steroid Biochemistry, Vol. 35, No. 6, 1990, p. 647-654.

Research output: Contribution to journalArticle

@article{44e904b1678e4ab5bf8401007e4bd370,
title = "Androgen resistance due to decreased amounts of androgen receptor: A reinvestigation",
abstract = "To provide insight into the pathogenesis of the androgen resistance in a previously described family with X-linked Reifenstein syndrome, we have systematically assessed a variety of parameters of androgen receptor function in fibroblasts cultured from scrotal skin biopsies. We assessed the amount of high affinity binding, the affinity of ligand binding to the receptor, the upregulation of androgen receptor levels by androgen, the stability of ligand binding in intact fibroblasts at high temperature, the dissociation of ligand from the receptor, the intranuclear localization and salt elution profiles of ligand-receptor complexes, and the ultracentrifugation characteristics of the ligand-receptor complexes. Since the only parameter found to be abnormal is a decreased amount of receptor, we conclude that the underlying mutation in this family influences the amount rather than the structure of the androgen receptor protein.",
author = "Grino, {Placido B.} and {Griffin III}, Jim and Wilson, {Jean D.}",
year = "1990",
doi = "10.1016/0022-4731(90)90304-B",
language = "English (US)",
volume = "35",
pages = "647--654",
journal = "Journal of Steroid Biochemistry and Molecular Biology",
issn = "0960-0760",
publisher = "Elsevier Limited",
number = "6",

}

TY - JOUR

T1 - Androgen resistance due to decreased amounts of androgen receptor

T2 - A reinvestigation

AU - Grino, Placido B.

AU - Griffin III, Jim

AU - Wilson, Jean D.

PY - 1990

Y1 - 1990

N2 - To provide insight into the pathogenesis of the androgen resistance in a previously described family with X-linked Reifenstein syndrome, we have systematically assessed a variety of parameters of androgen receptor function in fibroblasts cultured from scrotal skin biopsies. We assessed the amount of high affinity binding, the affinity of ligand binding to the receptor, the upregulation of androgen receptor levels by androgen, the stability of ligand binding in intact fibroblasts at high temperature, the dissociation of ligand from the receptor, the intranuclear localization and salt elution profiles of ligand-receptor complexes, and the ultracentrifugation characteristics of the ligand-receptor complexes. Since the only parameter found to be abnormal is a decreased amount of receptor, we conclude that the underlying mutation in this family influences the amount rather than the structure of the androgen receptor protein.

AB - To provide insight into the pathogenesis of the androgen resistance in a previously described family with X-linked Reifenstein syndrome, we have systematically assessed a variety of parameters of androgen receptor function in fibroblasts cultured from scrotal skin biopsies. We assessed the amount of high affinity binding, the affinity of ligand binding to the receptor, the upregulation of androgen receptor levels by androgen, the stability of ligand binding in intact fibroblasts at high temperature, the dissociation of ligand from the receptor, the intranuclear localization and salt elution profiles of ligand-receptor complexes, and the ultracentrifugation characteristics of the ligand-receptor complexes. Since the only parameter found to be abnormal is a decreased amount of receptor, we conclude that the underlying mutation in this family influences the amount rather than the structure of the androgen receptor protein.

UR - http://www.scopus.com/inward/record.url?scp=0025369909&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025369909&partnerID=8YFLogxK

U2 - 10.1016/0022-4731(90)90304-B

DO - 10.1016/0022-4731(90)90304-B

M3 - Article

VL - 35

SP - 647

EP - 654

JO - Journal of Steroid Biochemistry and Molecular Biology

JF - Journal of Steroid Biochemistry and Molecular Biology

SN - 0960-0760

IS - 6

ER -