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Cytosol androgen receptor (AR) in human skin fibroblasts: characterization of the binding reaction and differentiation from androgen binding molecules of lower affinity.
Steroids. 1984 Feb; 43(2):159-78.S

Abstract

Androgen binding was studied in cytosol of human fibroblasts at 4 degrees C. When 5 alpha-dihydrotestosterone (DHT) was the ligand, a curvilinear Scatchard plot was seen, which was resolved into two components: I the androgen receptor (AR), Kd = 0.12-0.44 nM, and II a low affinity species, Kd = 6.3-28 nM. The same cytosol demonstrated only type I binding for 3H-methyltrienolone (MTr), Kd = 0.10-0.40 nM. The AR, i.e., 3H-MTr binding activity, eluted at 440,000 d by gel filtration chromatography in pre-labeling and post-labeling experiments. When the ligand was 3H-DHT, binding activity in the 10,000-45,000 d range was seen in addition to AR. Thus, saturable nonreceptor steroid binding was seen for DHT but not for MTr. The latter is the preferred ligand for the study of the AR in this system.

Authors

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

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

6523537

Citation

Keenan, B S., et al. "Cytosol Androgen Receptor (AR) in Human Skin Fibroblasts: Characterization of the Binding Reaction and Differentiation From Androgen Binding Molecules of Lower Affinity." Steroids, vol. 43, no. 2, 1984, pp. 159-78.
Keenan BS, Greger NG, Hedge AM, et al. Cytosol androgen receptor (AR) in human skin fibroblasts: characterization of the binding reaction and differentiation from androgen binding molecules of lower affinity. Steroids. 1984;43(2):159-78.
Keenan, B. S., Greger, N. G., Hedge, A. M., & McNeel, R. L. (1984). Cytosol androgen receptor (AR) in human skin fibroblasts: characterization of the binding reaction and differentiation from androgen binding molecules of lower affinity. Steroids, 43(2), 159-78.
Keenan BS, et al. Cytosol Androgen Receptor (AR) in Human Skin Fibroblasts: Characterization of the Binding Reaction and Differentiation From Androgen Binding Molecules of Lower Affinity. Steroids. 1984;43(2):159-78. PubMed PMID: 6523537.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cytosol androgen receptor (AR) in human skin fibroblasts: characterization of the binding reaction and differentiation from androgen binding molecules of lower affinity. AU - Keenan,B S, AU - Greger,N G, AU - Hedge,A M, AU - McNeel,R L, PY - 1984/2/1/pubmed PY - 1984/2/1/medline PY - 1984/2/1/entrez SP - 159 EP - 78 JF - Steroids JO - Steroids VL - 43 IS - 2 N2 - Androgen binding was studied in cytosol of human fibroblasts at 4 degrees C. When 5 alpha-dihydrotestosterone (DHT) was the ligand, a curvilinear Scatchard plot was seen, which was resolved into two components: I the androgen receptor (AR), Kd = 0.12-0.44 nM, and II a low affinity species, Kd = 6.3-28 nM. The same cytosol demonstrated only type I binding for 3H-methyltrienolone (MTr), Kd = 0.10-0.40 nM. The AR, i.e., 3H-MTr binding activity, eluted at 440,000 d by gel filtration chromatography in pre-labeling and post-labeling experiments. When the ligand was 3H-DHT, binding activity in the 10,000-45,000 d range was seen in addition to AR. Thus, saturable nonreceptor steroid binding was seen for DHT but not for MTr. The latter is the preferred ligand for the study of the AR in this system. SN - 0039-128X UR - https://www.unboundmedicine.com/medline/citation/6523537/Cytosol_androgen_receptor__AR__in_human_skin_fibroblasts:_characterization_of_the_binding_reaction_and_differentiation_from_androgen_binding_molecules_of_lower_affinity_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0039-128X(84)90035-7 DB - PRIME DP - Unbound Medicine ER -