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Evidence for an androgen receptor in human testis.
Am J Obstet Gynecol. 1984 Nov 01; 150(5 Pt 1):534-41.AJ

Abstract

The present study identified and characterized an androgen-binding protein in human testicular tissue. Human testes were homogenized in dilute Tris buffer containing thioglycerol, phenylmethylsulfonylfluoride, and molybdate. The supernatant (termed cytosol) was incubated with radiolabeled androgen methyltrienolone (tritium-labeled R1881), and nonspecific binding was determined by adding 100-fold excess of unlabeled R1881 together with [3H]R1881 to cytosol. Specific binding with saturation at 24 hours was observed. Scatchard analysis of the specific binding with the use of increasing concentrations of [3H]R1881 alone and [3H]R1881 plus 200-fold excess unlabeled R1881 demonstrated a high-affinity (dissociation constant = 2.18 X 10(-10) mol/L), low-capacity (2924 molecules per cell) class of binding sites. A second class of lower-affinity sites was identified with a dissociation constant equaling 1.2 X 10(-8) and 26,300 molecules per cell. The bulk of the higher-affinity class of sites was precipitated at 35% ammonium sulfate. In competitive binding assays, dihydrotestosterone and testosterone greatly diminished binding to this high-affinity class of sites. Progesterone also diminished binding but to a lesser degree. Estradiol, estriol, and estrone failed to compete for these sites. Analysis of the receptor, using sucrose gradients, revealed a major peak in the 4S region and a small peak at 8S. A similar high-affinity (dissociation constant = 4.28 X 10(-9), low-capacity (4860 molecules per cell) binding protein was identified in purified nuclei. Binding to nuclear chromatin was demonstrated in the cell-free binding assay, and nuclear binding was further illustrated in the biopsy assay of intact tissue, suggesting translocation in vivo. These properties are characteristic of the androgen receptor and suggest that human testis is a target tissue for androgen, as has been found in animal tissue.

Authors

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

Pub Type(s)

Journal Article

Language

eng

PubMed ID

6333821

Citation

Graham, M L., et al. "Evidence for an Androgen Receptor in Human Testis." American Journal of Obstetrics and Gynecology, vol. 150, no. 5 Pt 1, 1984, pp. 534-41.
Graham ML, Razel AJ, Spelsberg TC, et al. Evidence for an androgen receptor in human testis. Am J Obstet Gynecol. 1984;150(5 Pt 1):534-41.
Graham, M. L., Razel, A. J., Spelsberg, T. C., & Coulam, C. B. (1984). Evidence for an androgen receptor in human testis. American Journal of Obstetrics and Gynecology, 150(5 Pt 1), 534-41.
Graham ML, et al. Evidence for an Androgen Receptor in Human Testis. Am J Obstet Gynecol. 1984 Nov 1;150(5 Pt 1):534-41. PubMed PMID: 6333821.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Evidence for an androgen receptor in human testis. AU - Graham,M L,2nd AU - Razel,A J, AU - Spelsberg,T C, AU - Coulam,C B, PY - 1984/11/1/pubmed PY - 1984/11/1/medline PY - 1984/11/1/entrez SP - 534 EP - 41 JF - American journal of obstetrics and gynecology JO - Am J Obstet Gynecol VL - 150 IS - 5 Pt 1 N2 - The present study identified and characterized an androgen-binding protein in human testicular tissue. Human testes were homogenized in dilute Tris buffer containing thioglycerol, phenylmethylsulfonylfluoride, and molybdate. The supernatant (termed cytosol) was incubated with radiolabeled androgen methyltrienolone (tritium-labeled R1881), and nonspecific binding was determined by adding 100-fold excess of unlabeled R1881 together with [3H]R1881 to cytosol. Specific binding with saturation at 24 hours was observed. Scatchard analysis of the specific binding with the use of increasing concentrations of [3H]R1881 alone and [3H]R1881 plus 200-fold excess unlabeled R1881 demonstrated a high-affinity (dissociation constant = 2.18 X 10(-10) mol/L), low-capacity (2924 molecules per cell) class of binding sites. A second class of lower-affinity sites was identified with a dissociation constant equaling 1.2 X 10(-8) and 26,300 molecules per cell. The bulk of the higher-affinity class of sites was precipitated at 35% ammonium sulfate. In competitive binding assays, dihydrotestosterone and testosterone greatly diminished binding to this high-affinity class of sites. Progesterone also diminished binding but to a lesser degree. Estradiol, estriol, and estrone failed to compete for these sites. Analysis of the receptor, using sucrose gradients, revealed a major peak in the 4S region and a small peak at 8S. A similar high-affinity (dissociation constant = 4.28 X 10(-9), low-capacity (4860 molecules per cell) binding protein was identified in purified nuclei. Binding to nuclear chromatin was demonstrated in the cell-free binding assay, and nuclear binding was further illustrated in the biopsy assay of intact tissue, suggesting translocation in vivo. These properties are characteristic of the androgen receptor and suggest that human testis is a target tissue for androgen, as has been found in animal tissue. SN - 0002-9378 UR - https://www.unboundmedicine.com/medline/citation/6333821/Evidence_for_an_androgen_receptor_in_human_testis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0002-9378(84)90435-6 DB - PRIME DP - Unbound Medicine ER -