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Regulation of the androgen receptor by androgen in normal and androgen-resistant genital skin fibroblasts.
J Steroid Biochem. 1983 Apr; 18(4):383-90.JS

Abstract

Normal genital skin fibroblast (GSF) monolayers incubated with serum-free medium containing 3 nM [3H]-5 alpha-dihydrotestosterone (DHT) at 37 degrees C for 20 h have about 35% more specific DHT-binding than replicates incubated in serum-free medium with [3H]-DHT for only 1 h to saturate basal specific androgen-receptor activity. If, after 19 h, spent medium is replaced by fresh medium with 3 nM [3H]-DHT for 1 h, specific DHT binding is 85% more than basal. The acquisition of increased binding is temperature dependent (37 greater than 27 degrees C) and cycloheximide (2 microM) suppressible. The increased binding activity is considered to represent an augmentation of androgen receptor concentration because it has the same equilibrium dissociation constant (KD approximately 0.5 nM), rate constant of dissociation (k-1 approximately 6 x 10(-3) min-1) and ligand specificity as basal androgen-receptor activity, and because basal DHT-binding activity is stable in cells preincubated in androgen-free or serum-free medium alone for up to 72 h before assay. Prolonged incubation with methyltrienolone (R1881), a nonmetabolizable synthetic androgen, causes a greater, more persistent increment of androgen receptor activity than does equimolar DHT. The fibroblasts from two subjects with receptor-positive, partial androgen resistance lose their basal receptor activity during prolonged incubation with DHT, but augment it normally with R1881. This suggests that defective DHT metabolism is somehow involved in the pathogenesis of their androgen resistance.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Case Reports
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

6601205

Citation

Kaufman, M, et al. "Regulation of the Androgen Receptor By Androgen in Normal and Androgen-resistant Genital Skin Fibroblasts." Journal of Steroid Biochemistry, vol. 18, no. 4, 1983, pp. 383-90.
Kaufman M, Pinsky L, Hollander R, et al. Regulation of the androgen receptor by androgen in normal and androgen-resistant genital skin fibroblasts. J Steroid Biochem. 1983;18(4):383-90.
Kaufman, M., Pinsky, L., Hollander, R., & Bailey, J. D. (1983). Regulation of the androgen receptor by androgen in normal and androgen-resistant genital skin fibroblasts. Journal of Steroid Biochemistry, 18(4), 383-90.
Kaufman M, et al. Regulation of the Androgen Receptor By Androgen in Normal and Androgen-resistant Genital Skin Fibroblasts. J Steroid Biochem. 1983;18(4):383-90. PubMed PMID: 6601205.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Regulation of the androgen receptor by androgen in normal and androgen-resistant genital skin fibroblasts. AU - Kaufman,M, AU - Pinsky,L, AU - Hollander,R, AU - Bailey,J D, PY - 1983/4/1/pubmed PY - 1983/4/1/medline PY - 1983/4/1/entrez SP - 383 EP - 90 JF - Journal of steroid biochemistry JO - J. Steroid Biochem. VL - 18 IS - 4 N2 - Normal genital skin fibroblast (GSF) monolayers incubated with serum-free medium containing 3 nM [3H]-5 alpha-dihydrotestosterone (DHT) at 37 degrees C for 20 h have about 35% more specific DHT-binding than replicates incubated in serum-free medium with [3H]-DHT for only 1 h to saturate basal specific androgen-receptor activity. If, after 19 h, spent medium is replaced by fresh medium with 3 nM [3H]-DHT for 1 h, specific DHT binding is 85% more than basal. The acquisition of increased binding is temperature dependent (37 greater than 27 degrees C) and cycloheximide (2 microM) suppressible. The increased binding activity is considered to represent an augmentation of androgen receptor concentration because it has the same equilibrium dissociation constant (KD approximately 0.5 nM), rate constant of dissociation (k-1 approximately 6 x 10(-3) min-1) and ligand specificity as basal androgen-receptor activity, and because basal DHT-binding activity is stable in cells preincubated in androgen-free or serum-free medium alone for up to 72 h before assay. Prolonged incubation with methyltrienolone (R1881), a nonmetabolizable synthetic androgen, causes a greater, more persistent increment of androgen receptor activity than does equimolar DHT. The fibroblasts from two subjects with receptor-positive, partial androgen resistance lose their basal receptor activity during prolonged incubation with DHT, but augment it normally with R1881. This suggests that defective DHT metabolism is somehow involved in the pathogenesis of their androgen resistance. SN - 0022-4731 UR - https://www.unboundmedicine.com/medline/citation/6601205/Regulation_of_the_androgen_receptor_by_androgen_in_normal_and_androgen_resistant_genital_skin_fibroblasts_ DB - PRIME DP - Unbound Medicine ER -