Estrogen receptor in rat pancreatic islets

The cytosol fraction of pancreatic islets of the female rat was found to contain a specifically binding protein for [3H]-estradiol. This protein was heat sensitive and the [3H]-estradiol binding was eliminated by treatment with protease and sulphydryl-blocking agents. Scatchard analysis of the cytos...

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Autores principales: Tesone, Marta, Chazenbalk, Gregorio Daniel, Charreau, Eduardo Hernán
Publicado: 1979
Materias:
rat
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224731_v11_n3_p1309_Tesone
http://hdl.handle.net/20.500.12110/paper_00224731_v11_n3_p1309_Tesone
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spelling paper:paper_00224731_v11_n3_p1309_Tesone2023-06-08T14:50:58Z Estrogen receptor in rat pancreatic islets Tesone, Marta Chazenbalk, Gregorio Daniel Charreau, Eduardo Hernán estradiol estrogen receptor animal article binding competition castration cytosol experimental diabetes mellitus female isolation and purification kinetics metabolism pancreas islet pregnancy rat Animal Binding, Competitive Castration Cytosol Diabetes Mellitus, Experimental Estradiol Female Islets of Langerhans Kinetics Pregnancy Rats Receptors, Estrogen The cytosol fraction of pancreatic islets of the female rat was found to contain a specifically binding protein for [3H]-estradiol. This protein was heat sensitive and the [3H]-estradiol binding was eliminated by treatment with protease and sulphydryl-blocking agents. Scatchard analysis of the cytosol binding reaction, measured by charcoal-dextran assay, indicated a single class of estradiol-binding sites having high affinity (Kd = 2.9 × 10-8 M at 0°C). The number of binding sites was calculated to be 29.6 fmol/mg cytosol protein in whole pancreas and 170 fmol/mg cytosol protein in isolated pancreatic islets after collagenase treatment. Competition studies indicated high specificity for the binding reaction, since excess (100-fold) unlabelled estrogens, diethylstilbestrol and the antiestrogen nafoxidine, all significantly reduced the binding of [3H]-estradiol. On the other hand, the nonestrogenic steroids dihydrotestosterone, corticosterone and progesterone had no significant effects on [3H]-estradiol binding. The complex had a sedimentation coefficient of 4-5 S in sucrose density gradient centrifugation in low salt. In streptozotocin-diabetic and in 3-wk pregnant rats a significant decrease in the binding of estradiol to pancreas islet cytosol was found. © 1979. Fil:Tesone, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Chazenbalk, G.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Charreau, E.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1979 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224731_v11_n3_p1309_Tesone http://hdl.handle.net/20.500.12110/paper_00224731_v11_n3_p1309_Tesone
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic estradiol
estrogen receptor
animal
article
binding competition
castration
cytosol
experimental diabetes mellitus
female
isolation and purification
kinetics
metabolism
pancreas islet
pregnancy
rat
Animal
Binding, Competitive
Castration
Cytosol
Diabetes Mellitus, Experimental
Estradiol
Female
Islets of Langerhans
Kinetics
Pregnancy
Rats
Receptors, Estrogen
spellingShingle estradiol
estrogen receptor
animal
article
binding competition
castration
cytosol
experimental diabetes mellitus
female
isolation and purification
kinetics
metabolism
pancreas islet
pregnancy
rat
Animal
Binding, Competitive
Castration
Cytosol
Diabetes Mellitus, Experimental
Estradiol
Female
Islets of Langerhans
Kinetics
Pregnancy
Rats
Receptors, Estrogen
Tesone, Marta
Chazenbalk, Gregorio Daniel
Charreau, Eduardo Hernán
Estrogen receptor in rat pancreatic islets
topic_facet estradiol
estrogen receptor
animal
article
binding competition
castration
cytosol
experimental diabetes mellitus
female
isolation and purification
kinetics
metabolism
pancreas islet
pregnancy
rat
Animal
Binding, Competitive
Castration
Cytosol
Diabetes Mellitus, Experimental
Estradiol
Female
Islets of Langerhans
Kinetics
Pregnancy
Rats
Receptors, Estrogen
description The cytosol fraction of pancreatic islets of the female rat was found to contain a specifically binding protein for [3H]-estradiol. This protein was heat sensitive and the [3H]-estradiol binding was eliminated by treatment with protease and sulphydryl-blocking agents. Scatchard analysis of the cytosol binding reaction, measured by charcoal-dextran assay, indicated a single class of estradiol-binding sites having high affinity (Kd = 2.9 × 10-8 M at 0°C). The number of binding sites was calculated to be 29.6 fmol/mg cytosol protein in whole pancreas and 170 fmol/mg cytosol protein in isolated pancreatic islets after collagenase treatment. Competition studies indicated high specificity for the binding reaction, since excess (100-fold) unlabelled estrogens, diethylstilbestrol and the antiestrogen nafoxidine, all significantly reduced the binding of [3H]-estradiol. On the other hand, the nonestrogenic steroids dihydrotestosterone, corticosterone and progesterone had no significant effects on [3H]-estradiol binding. The complex had a sedimentation coefficient of 4-5 S in sucrose density gradient centrifugation in low salt. In streptozotocin-diabetic and in 3-wk pregnant rats a significant decrease in the binding of estradiol to pancreas islet cytosol was found. © 1979.
author Tesone, Marta
Chazenbalk, Gregorio Daniel
Charreau, Eduardo Hernán
author_facet Tesone, Marta
Chazenbalk, Gregorio Daniel
Charreau, Eduardo Hernán
author_sort Tesone, Marta
title Estrogen receptor in rat pancreatic islets
title_short Estrogen receptor in rat pancreatic islets
title_full Estrogen receptor in rat pancreatic islets
title_fullStr Estrogen receptor in rat pancreatic islets
title_full_unstemmed Estrogen receptor in rat pancreatic islets
title_sort estrogen receptor in rat pancreatic islets
publishDate 1979
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00224731_v11_n3_p1309_Tesone
http://hdl.handle.net/20.500.12110/paper_00224731_v11_n3_p1309_Tesone
work_keys_str_mv AT tesonemarta estrogenreceptorinratpancreaticislets
AT chazenbalkgregoriodaniel estrogenreceptorinratpancreaticislets
AT charreaueduardohernan estrogenreceptorinratpancreaticislets
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