Ovine placental lactogen-induced heterodimerization of ovine growth hormone and prolactin receptors in living cells is demonstrated by fluorescence resonance energy transfer microscopy and leads to prolonged phosphorylation of signal transducer and activator of transcription (STAT)1 and STAT3
| Autor: | Brian Herman, Stuart J. Frank, Jean Djiane, Arieh Gertler, Eva Biener, Victoria E. Centonze, Cyril Martin, Nathalie Daniel |
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| Přispěvatelé: | Neurobiologie de l'Olfaction et de la Prise Alimentaire (NOPA), Institut National de la Recherche Agronomique (INRA) |
| Rok vydání: | 2003 |
| Předmět: |
[SDV]Life Sciences [q-bio]
Growth hormone receptor Kidney 0302 clinical medicine Endocrinology ovin Cricetinae Fluorescence Resonance Energy Transfer STAT5 Transcription Factor STAT1 Placental lactogen Phosphorylation STAT3 STAT5 ComputingMilieux_MISCELLANEOUS hormone lactogène placentaire 0303 health sciences Janus kinase 2 biology Milk Proteins Recombinant Proteins DNA-Binding Proteins STAT1 Transcription Factor Mitogen-Activated Protein Kinases récepteur Dimerization STAT3 Transcription Factor medicine.medical_specialty Receptors Prolactin Green Fluorescent Proteins 030209 endocrinology & metabolism CHO Cells Transfection hormone de croissance Cell Line 03 medical and health sciences Bacterial Proteins Internal medicine medicine Animals Humans [INFO]Computer Science [cs] 030304 developmental biology Sheep Prolactin receptor Receptors Somatotropin Embryo Mammalian Placental Lactogen Molecular biology Kinetics Luminescent Proteins Microscopy Fluorescence STAT protein biology.protein Trans-Activators prolactine |
| Zdroj: | Endocrinology Endocrinology, Endocrine Society, 2003, 144 (8), pp.3532-3540. ⟨10.1210/en.2003-0096#sthash.x2nvVx34.dpuf⟩ Endocrinology 8 (144), 3532-3540. (2003) |
| ISSN: | 0013-7227 |
| DOI: | 10.1210/en.2003-0096#sthash.x2nvVx34.dpuf⟩ |
| Popis: | HEK-293T cells transiently transfected with ovine (o) GH receptor (GHR) and prolactin receptor (PRLR) constructs respectively tagged downstream with cyan or yellow fluorescent proteins were used to study ovine placental lactogen (oPL)-stimulated heterodimerization by fluorescence resonance energy transfer (FRET) microscopy. The oPL-stimulated transient heterodimerization of GHR and PRLR had a peak occurring 2.5–3 min after oPL application, whereas oGH or oPRL had no effect at all. The results indicate none or only little dimerization occurring before the hormonal stimulation. The effect of heterodimerization was studied by comparing activation of Janus kinase 2, signal transducer and activator of transcription (STAT)1, STAT3, STAT5, and MAPK in Chinese hamster ovary cells stably transfected with chimeric genes encoding receptors consisting of cytosolic and transmembrane parts of oGHR and oPRLR, extracellular domains of human granulocyte and macrophage colony-stimulating factor (hGM-CSF) receptor α or β, and cells transfected with the two forms (α or β) of PRLR and GHR. Functionality of those proteins was verified by hGM-CSF-induced phosphorylation of both intracellular PRLR and GHR domains and hGM-CSF-induced heterodimerization was documented by chimeric receptor coimmunoprecipitation. Homodimerization or heterodimerization of PRLRs and GHRs had no differential effect on activation of STAT5 and MAPK. However, heterodimerization resulted in a prolonged phosphorylation of STAT1 and in particular STAT3, suggesting that the heterodimerization of α-oGHR and β-oPRLR is able to transduce a signal, which is distinct from that occurring on homodimeric associations. |
| Databáze: | OpenAIRE |
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