Progestin-binding protein in human benign prostatic hypertrophy.

Abstract

Cytosols from human benign prostatic hypertrophy contained progestin-binding components which bound to R 5020, ORG 2058 and progesterone in high affinity fashion. Most of the protein bound to R 5020 was recovered in the precipitate with 0-30% saturation of ammonium sulfate. The R 5020-binding protein showed sedimentation coefficients of 3.6S and 8.4S, and was eluted in the void volume of a Sephadex G-200 column. This protein was clearly distinguished from the dihydrotestosterone-binding protein by its precipitability by ammonium sulfate, heat stability and susceptibility to delipidization. R 5020 and ORG 2058 binding were markedly inhibited by the addition of R 1881, therefore, most of the binding to progestin in cytosols from the benign prostatic hypertrophy seems to be also the sites for R 1881. Although nuclear extract by 0.4 M KCl showed R 1881 binding, the extract did not contain the R 5020-binding protein, and this suggested that the progestin-binding protein observed in the cytosols does not seem to be the steroid receptor.

• Authors: T Kodama, M Ito, R Sato, H Ito, J Shimazaki
• Journal: Endocrinologia japonica (Endocrinol Jpn) Vol. 28 Issue 2 Pg. 175-85 (Apr 1981) ISSN: 0013-7219 [Print] Japan
• PMID: 6171422 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Carrier Proteins
• Norpregnenes
• Pregnenediones
• Progestins
• Receptors, Progesterone
• 16 alpha-ethyl-21-hydroxy-19-nor-4-pregnene-3,20-dione
• Promegestone

Topics

• Carrier Proteins (isolation & purification, metabolism)
• Cell Nucleus (metabolism)
• Cytosol (metabolism)
• Humans
• Male
• Norpregnenes (metabolism)
• Pregnenediones (metabolism)
• Progestins (metabolism)
• Promegestone (metabolism)
• Prostatic Hyperplasia (metabolism)
• Receptors, Progesterone (metabolism)