Prolactin Receptor and Signal Transduction to Milk Protein Genes
| Autor: | Nathalie Daniel, Pierre Vacher, Jacqueline Paly, Jean Djiane, Michael J. Waters, Christophe Bignon, Bernard Dufy |
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| Přispěvatelé: | Unité de biologie cellulaire et moléculaire, Institut National de la Recherche Agronomique (INRA), ProdInra, Migration |
| Rok vydání: | 1994 |
| Předmět: |
Chloramphenicol O-Acetyltransferase
endocrine system DNA Complementary endocrine system diseases Receptors Prolactin [SDV]Life Sciences [q-bio] Gene Expression 030209 endocrinology & metabolism CHO Cells Biology Transfection General Biochemistry Genetics and Molecular Biology 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Cricetinae Complementary DNA Animals Humans Receptor ComputingMilieux_MISCELLANEOUS 030304 developmental biology 0303 health sciences Chinese hamster ovary cell Prolactin receptor Tyrosine phosphorylation Protein-Tyrosine Kinases Milk Proteins Molecular biology Prolactin [SDV] Life Sciences [q-bio] chemistry Calcium Signal transduction Tyrosine kinase hormones hormone substitutes and hormone antagonists Signal Transduction |
| Zdroj: | Proceedings of the Society for Experimental Biology and Medicine Proceedings of the Society for Experimental Biology and Medicine, Wiley, 1994, 206, pp.299-303 |
| ISSN: | 1535-3699 1535-3702 0037-9727 1525-1373 |
| DOI: | 10.3181/00379727-206-43763 |
| Popis: | After cloning of the mammary gland prolactin (PRL) receptor cDNA, a functional assay was established using co-transfection of PRL receptor cDNA together with a milk protein promoter/chloramphenicol acetyl transferase (CAT) construct in Chinese hamster ovary (CHO) cells. Different mutants of the PRL receptor were tested in this CAT assay to delimit the domains in the receptor necessary for signal transduction to milk protein genes. In CHO cells stably transfected with PRL receptor cDNA, high numbers of PRL receptor are expressed. By metabolic labeling and immunoprecipitation, expressed PRL receptor was identified as a single species of 100 kDa. Using these cells, we analyzed the effects of PRL on intracellular free Ca++ concentration. PRL stimulates Ca++ entry and induces secondary Ca++ mobilization. The entry of Ca++ is a result of an increase in K+ conductance that hyperpolarizes the membranes. We have also analyzed tyrosine phosphorylation induced by PRL. In CHO cells stably transfected with PRL receptor cDNA, PRL induced a very rapid and transient tyrosine phosphorylation of a 100-kDa protein which is most probably the PRL receptor. The same finding was obtained in mammary membranes after PRL injection to lactating rabbits. Whereas tyrosine kinase inhibitors genistein and lavendustin were without effect, PRL stimulation of milk protein gene promoters was partially inhibited by 2 microM herbimycin in CHO cells co-transfected with PRL receptor cDNA and the beta lactoglobulin CAT construct. Taken together these observations indicate that the cytoplasmic domain of the PRL receptor interacts with one or several tyrosine kinases, which may represent early postreceptor events necessary for PRL signal transduction to milk protein genes. |
| Databáze: | OpenAIRE |
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