Proiactin binding in rat langerhans islets

Membrane preparations of collagenase-dispersed Langerhans islets of female Wistar rats exhibit specific binding sites for 125I labelled ovine prolactin (125I-oPrl). Almost negligible binding was detected in islets of male animals. The binding is a saturable and time-temperature dependent process, eq...

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Detalles Bibliográficos
Publicado: 1980
Materias:
prolactin
prolactin i 125
radioisotope
animal experiment
cell membrane
endocrine system
in vitro study
pancreas islet cell
rat
Animal
Cell Membrane
Diabetes Mellitus, Experimental
Female
Islets of Langerhans
Male
Phospholipase C
Prolactin
Protease Inhibitors
Rats
Rats, Inbred Strains
Receptors, Cell Surface
Receptors, Prolactin
Sex Factors
Temperature
Trypsin
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10799893_v1_n3_p355_Tesone
http://hdl.handle.net/20.500.12110/paper_10799893_v1_n3_p355_Tesone
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_10799893_v1_n3_p355_Tesone
record_format dspace
spelling paper:paper_10799893_v1_n3_p355_Tesone2023-06-08T16:05:38Z Proiactin binding in rat langerhans islets prolactin prolactin i 125 radioisotope animal experiment cell membrane endocrine system in vitro study pancreas islet cell rat Animal Cell Membrane Diabetes Mellitus, Experimental Female Islets of Langerhans Male Phospholipase C Prolactin Protease Inhibitors Rats Rats, Inbred Strains Receptors, Cell Surface Receptors, Prolactin Sex Factors Temperature Trypsin Membrane preparations of collagenase-dispersed Langerhans islets of female Wistar rats exhibit specific binding sites for 125I labelled ovine prolactin (125I-oPrl). Almost negligible binding was detected in islets of male animals. The binding is a saturable and time-temperature dependent process, equilibrium being reached after 16 h incubation at 0°C. The bound oPrl is not displaceable by hFSH, hLH, bGH or hGH. In contrast with other cell fractions, the 12,000 g pellet accounts for more than 80% of the specific binding of 125I-oPrl. Scatchard plots of data obtained in saturation studies indicate a single class of binding sites with Ka = 0.21 × 1010 M-1. Protein and phospholipid moieties are essential for the receptor activity, since after trypsin or phospholipase C digestions marked loss of binding was verified. In islets of streptozotocin diabetic rats a marked reduction in the number of binding sites was observed. These findings may suggest that some of the actions of prolactin on endocrine pancreas could be explained by its specific interaction with islet cell membranes. © 1980 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted. 1980 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10799893_v1_n3_p355_Tesone http://hdl.handle.net/20.500.12110/paper_10799893_v1_n3_p355_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 prolactin
prolactin i 125
radioisotope
animal experiment
cell membrane
endocrine system
in vitro study
pancreas islet cell
rat
Animal
Cell Membrane
Diabetes Mellitus, Experimental
Female
Islets of Langerhans
Male
Phospholipase C
Prolactin
Protease Inhibitors
Rats
Rats, Inbred Strains
Receptors, Cell Surface
Receptors, Prolactin
Sex Factors
Temperature
Trypsin
spellingShingle prolactin
prolactin i 125
radioisotope
animal experiment
cell membrane
endocrine system
in vitro study
pancreas islet cell
rat
Animal
Cell Membrane
Diabetes Mellitus, Experimental
Female
Islets of Langerhans
Male
Phospholipase C
Prolactin
Protease Inhibitors
Rats
Rats, Inbred Strains
Receptors, Cell Surface
Receptors, Prolactin
Sex Factors
Temperature
Trypsin
Proiactin binding in rat langerhans islets
topic_facet prolactin
prolactin i 125
radioisotope
animal experiment
cell membrane
endocrine system
in vitro study
pancreas islet cell
rat
Animal
Cell Membrane
Diabetes Mellitus, Experimental
Female
Islets of Langerhans
Male
Phospholipase C
Prolactin
Protease Inhibitors
Rats
Rats, Inbred Strains
Receptors, Cell Surface
Receptors, Prolactin
Sex Factors
Temperature
Trypsin
description Membrane preparations of collagenase-dispersed Langerhans islets of female Wistar rats exhibit specific binding sites for 125I labelled ovine prolactin (125I-oPrl). Almost negligible binding was detected in islets of male animals. The binding is a saturable and time-temperature dependent process, equilibrium being reached after 16 h incubation at 0°C. The bound oPrl is not displaceable by hFSH, hLH, bGH or hGH. In contrast with other cell fractions, the 12,000 g pellet accounts for more than 80% of the specific binding of 125I-oPrl. Scatchard plots of data obtained in saturation studies indicate a single class of binding sites with Ka = 0.21 × 1010 M-1. Protein and phospholipid moieties are essential for the receptor activity, since after trypsin or phospholipase C digestions marked loss of binding was verified. In islets of streptozotocin diabetic rats a marked reduction in the number of binding sites was observed. These findings may suggest that some of the actions of prolactin on endocrine pancreas could be explained by its specific interaction with islet cell membranes. © 1980 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.
title Proiactin binding in rat langerhans islets
title_short Proiactin binding in rat langerhans islets
title_full Proiactin binding in rat langerhans islets
title_fullStr Proiactin binding in rat langerhans islets
title_full_unstemmed Proiactin binding in rat langerhans islets
title_sort proiactin binding in rat langerhans islets
publishDate 1980
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10799893_v1_n3_p355_Tesone
http://hdl.handle.net/20.500.12110/paper_10799893_v1_n3_p355_Tesone
_version_ 1768543433623863296

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