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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todo:paper_10799893_v1_n3_p355_Tesone2023-10-03T16:03:43Z Proiactin binding in rat langerhans islets Tesone, M. Oliveira-Filho, R.M. Charreau, E.H. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Tesone, M. Oliveira-Filho, R.M. Charreau, E.H. 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. |
| format |
JOUR |
| author |
Tesone, M. Oliveira-Filho, R.M. Charreau, E.H. |
| author_facet |
Tesone, M. Oliveira-Filho, R.M. Charreau, E.H. |
| author_sort |
Tesone, M. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_10799893_v1_n3_p355_Tesone |
| work_keys_str_mv |
AT tesonem proiactinbindinginratlangerhansislets AT oliveirafilhorm proiactinbindinginratlangerhansislets AT charreaueh proiactinbindinginratlangerhansislets |
| _version_ |
1807321049800376320 |