Studies on the pathogenesis of the incomplete forms of androgen resistance in man

Jim Griffin III, J. D. Wilson

Research output: Contribution to journalArticle

62 Citations (Scopus)

Abstract

The affinity and turnover of the specific dihydrotestosterone binding protein have been assessed in fibroblasts cultured from genital skin from a variety of control subjects and from 4 patients with incomplete hereditary male pseudohermaphroditism due to androgen resistance (incomplete testicular feminization and Reifenstein syndrome). Whereas the amount of dihydrotestosterone binding in the 4 mutant cell strains is low, both the affinity of the protein for dihydrotestosterone as assessed by the concentration at which half-maximal binding occurs (averaging 0.2 nM) and the turnover of the binding protein (average half-life of 11-13 h) are within the normal range. Since no qualitative abnormality could be detected, these data suggest that the mutations in these two disorders affect the synthesis of the dihydrotestosterone binding protein.

Original languageEnglish (US)
Pages (from-to)1137-1143
Number of pages7
JournalJournal of Clinical Endocrinology and Metabolism
Volume45
Issue number6
StatePublished - 1977

Fingerprint

Dihydrotestosterone
Androgens
Androgen-Insensitivity Syndrome
Carrier Proteins
XY Disorders of Sex Development 46
Fibroblasts
Half-Life
Skin
Reference Values
Mutation
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology, Diabetes and Metabolism

Cite this

Studies on the pathogenesis of the incomplete forms of androgen resistance in man. / Griffin III, Jim; Wilson, J. D.

In: Journal of Clinical Endocrinology and Metabolism, Vol. 45, No. 6, 1977, p. 1137-1143.

Research output: Contribution to journalArticle

@article{c83226b517b648b4bcbdf2bfaee0c00d,
title = "Studies on the pathogenesis of the incomplete forms of androgen resistance in man",
abstract = "The affinity and turnover of the specific dihydrotestosterone binding protein have been assessed in fibroblasts cultured from genital skin from a variety of control subjects and from 4 patients with incomplete hereditary male pseudohermaphroditism due to androgen resistance (incomplete testicular feminization and Reifenstein syndrome). Whereas the amount of dihydrotestosterone binding in the 4 mutant cell strains is low, both the affinity of the protein for dihydrotestosterone as assessed by the concentration at which half-maximal binding occurs (averaging 0.2 nM) and the turnover of the binding protein (average half-life of 11-13 h) are within the normal range. Since no qualitative abnormality could be detected, these data suggest that the mutations in these two disorders affect the synthesis of the dihydrotestosterone binding protein.",
author = "{Griffin III}, Jim and Wilson, {J. D.}",
year = "1977",
language = "English (US)",
volume = "45",
pages = "1137--1143",
journal = "Journal of Clinical Endocrinology and Metabolism",
issn = "0021-972X",
publisher = "The Endocrine Society",
number = "6",

}

TY - JOUR

T1 - Studies on the pathogenesis of the incomplete forms of androgen resistance in man

AU - Griffin III, Jim

AU - Wilson, J. D.

PY - 1977

Y1 - 1977

N2 - The affinity and turnover of the specific dihydrotestosterone binding protein have been assessed in fibroblasts cultured from genital skin from a variety of control subjects and from 4 patients with incomplete hereditary male pseudohermaphroditism due to androgen resistance (incomplete testicular feminization and Reifenstein syndrome). Whereas the amount of dihydrotestosterone binding in the 4 mutant cell strains is low, both the affinity of the protein for dihydrotestosterone as assessed by the concentration at which half-maximal binding occurs (averaging 0.2 nM) and the turnover of the binding protein (average half-life of 11-13 h) are within the normal range. Since no qualitative abnormality could be detected, these data suggest that the mutations in these two disorders affect the synthesis of the dihydrotestosterone binding protein.

AB - The affinity and turnover of the specific dihydrotestosterone binding protein have been assessed in fibroblasts cultured from genital skin from a variety of control subjects and from 4 patients with incomplete hereditary male pseudohermaphroditism due to androgen resistance (incomplete testicular feminization and Reifenstein syndrome). Whereas the amount of dihydrotestosterone binding in the 4 mutant cell strains is low, both the affinity of the protein for dihydrotestosterone as assessed by the concentration at which half-maximal binding occurs (averaging 0.2 nM) and the turnover of the binding protein (average half-life of 11-13 h) are within the normal range. Since no qualitative abnormality could be detected, these data suggest that the mutations in these two disorders affect the synthesis of the dihydrotestosterone binding protein.

UR - http://www.scopus.com/inward/record.url?scp=0017587326&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017587326&partnerID=8YFLogxK

M3 - Article

C2 - 591611

AN - SCOPUS:0017587326

VL - 45

SP - 1137

EP - 1143

JO - Journal of Clinical Endocrinology and Metabolism

JF - Journal of Clinical Endocrinology and Metabolism

SN - 0021-972X

IS - 6

ER -