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
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 tr...
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| Veröffentlicht in: | Endocrinology (Philadelphia) 2003-08, Vol.144 (8), p.3532-3540 |
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| creator | Biener, Eva Martin, Cyril Daniel, Nathalie Frank, Stuart J Centonze, Victoria E Herman, Brian Djiane, Jean Gertler, Arieh |
| description | 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. |
| doi_str_mv | 10.1210/en.2003-0096 |
| format | Article |
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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.</description><identifier>ISSN: 0013-7227</identifier><identifier>EISSN: 1945-7170</identifier><identifier>DOI: 10.1210/en.2003-0096</identifier><identifier>PMID: 12865335</identifier><identifier>CODEN: ENDOAO</identifier><language>eng</language><publisher>Bethesda, MD: Endocrine Society</publisher><subject>Animals ; Bacterial Proteins - genetics ; Biological and medical sciences ; Cell Line ; CHO Cells ; Colony-stimulating factor ; Cricetinae ; Dimerization ; DNA-Binding Proteins - metabolism ; Embryo, Mammalian ; Energy transfer ; Fluorescence ; Fluorescence Resonance Energy Transfer ; Fundamental and applied biological sciences. Psychology ; Granulocyte-macrophage colony-stimulating factor ; Green Fluorescent Proteins ; Growth hormones ; Humans ; Janus kinase ; Janus kinase 2 ; Kidney ; Kinases ; Kinetics ; Luminescent Proteins - genetics ; MAP kinase ; Microscopy ; Microscopy, Fluorescence ; Milk Proteins ; Mitogen-Activated Protein Kinases - metabolism ; Phosphorylation ; Placenta ; Placental Lactogen - pharmacology ; Prolactin ; Prolactin receptors ; Proteins ; Receptors ; Receptors, Prolactin - chemistry ; Receptors, Prolactin - genetics ; Receptors, Somatotropin - chemistry ; Receptors, Somatotropin - genetics ; Recombinant Proteins ; Resonance ; Sheep ; Stat1 protein ; STAT1 Transcription Factor ; Stat3 protein ; STAT3 Transcription Factor ; Stat5 protein ; STAT5 Transcription Factor ; Trans-Activators - metabolism ; Transcription activation ; Transducers ; Transfection</subject><ispartof>Endocrinology (Philadelphia), 2003-08, Vol.144 (8), p.3532-3540</ispartof><rights>Copyright © 2003 by The Endocrine Society 2003</rights><rights>2003 INIST-CNRS</rights><rights>Copyright © 2003 by The Endocrine Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3746-26572bc6351a1a91ed69d841354bfca44e712bed9efd41f5e5480671fa42e0153</citedby><cites>FETCH-LOGICAL-c3746-26572bc6351a1a91ed69d841354bfca44e712bed9efd41f5e5480671fa42e0153</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14980567$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12865335$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Biener, Eva</creatorcontrib><creatorcontrib>Martin, Cyril</creatorcontrib><creatorcontrib>Daniel, Nathalie</creatorcontrib><creatorcontrib>Frank, Stuart J</creatorcontrib><creatorcontrib>Centonze, Victoria E</creatorcontrib><creatorcontrib>Herman, Brian</creatorcontrib><creatorcontrib>Djiane, Jean</creatorcontrib><creatorcontrib>Gertler, Arieh</creatorcontrib><title>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</title><title>Endocrinology (Philadelphia)</title><addtitle>Endocrinology</addtitle><description>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.</description><subject>Animals</subject><subject>Bacterial Proteins - genetics</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>CHO Cells</subject><subject>Colony-stimulating factor</subject><subject>Cricetinae</subject><subject>Dimerization</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Embryo, Mammalian</subject><subject>Energy transfer</subject><subject>Fluorescence</subject><subject>Fluorescence Resonance Energy Transfer</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Granulocyte-macrophage colony-stimulating factor</subject><subject>Green Fluorescent Proteins</subject><subject>Growth hormones</subject><subject>Humans</subject><subject>Janus kinase</subject><subject>Janus kinase 2</subject><subject>Kidney</subject><subject>Kinases</subject><subject>Kinetics</subject><subject>Luminescent Proteins - genetics</subject><subject>MAP kinase</subject><subject>Microscopy</subject><subject>Microscopy, Fluorescence</subject><subject>Milk Proteins</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Phosphorylation</subject><subject>Placenta</subject><subject>Placental Lactogen - pharmacology</subject><subject>Prolactin</subject><subject>Prolactin receptors</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Receptors, Prolactin - chemistry</subject><subject>Receptors, Prolactin - genetics</subject><subject>Receptors, Somatotropin - chemistry</subject><subject>Receptors, Somatotropin - genetics</subject><subject>Recombinant Proteins</subject><subject>Resonance</subject><subject>Sheep</subject><subject>Stat1 protein</subject><subject>STAT1 Transcription Factor</subject><subject>Stat3 protein</subject><subject>STAT3 Transcription Factor</subject><subject>Stat5 protein</subject><subject>STAT5 Transcription Factor</subject><subject>Trans-Activators - metabolism</subject><subject>Transcription activation</subject><subject>Transducers</subject><subject>Transfection</subject><issn>0013-7227</issn><issn>1945-7170</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kt9v0zAQxwMCsTJ44xlZmsYPiQw7tpPmsSrbWqloFSvPketcWk-pHexkqPz1XNKKSgie4lM-3_t-73RR9IbRK5Yw-hnsVUIpjynN06fRiOVCxhnL6LNoRCnjcZYk2Vn0MoQHLIUQ_EV0xpJxKjmXoyeXd4_GAlnWSoNtVU0WSrduAzae27LTUJIZtOBdaXbgzS_VGmeJq8hBduvdz3ZLZs7vHJbKlmTpHfZqjSXfQEPTOh8IFguDgg2ZQl0HMg_kC6AitF61aLHek5u6cx4ChtCAyuCs6l_XFvxmT1Ze2VCBJ1-N9i5o1-wHswWoMpDWDa7ObrDXcutCs3V-X__Jem82FicbmvQz-UE7wZCPCvP1yPBPe9MMmg_3q8nqIxuw_slfRc8rVQd4ffyeR99vrlfTWby4u51PJ4tY80ykcZLKLFnrlEummMoZlGlejgXjUqwrrYSAjCVrKHOoSsEqCVKMaZqxSokEKJP8PHp36Nt496OD0BY7gzupa2XBdaHIuEgFlQzBi7_AB9d5nDIUnHEq00yME6Q-Hah-acFDVTTe7JTfF4wW_fEUYIv-eIr-eBB_e2zarXdQnuDjtSBweQRU0KqucGnahBMn8nFvjdz7A-e65n-W8dGSH0iwpcP9W2jwCsJpmn8G_Q1MH-3e</recordid><startdate>20030801</startdate><enddate>20030801</enddate><creator>Biener, Eva</creator><creator>Martin, Cyril</creator><creator>Daniel, Nathalie</creator><creator>Frank, Stuart J</creator><creator>Centonze, Victoria E</creator><creator>Herman, Brian</creator><creator>Djiane, Jean</creator><creator>Gertler, Arieh</creator><general>Endocrine Society</general><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20030801</creationdate><title>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</title><author>Biener, Eva ; Martin, Cyril ; Daniel, Nathalie ; Frank, Stuart J ; Centonze, Victoria E ; Herman, Brian ; Djiane, Jean ; Gertler, Arieh</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3746-26572bc6351a1a91ed69d841354bfca44e712bed9efd41f5e5480671fa42e0153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Bacterial Proteins - genetics</topic><topic>Biological and medical sciences</topic><topic>Cell Line</topic><topic>CHO Cells</topic><topic>Colony-stimulating factor</topic><topic>Cricetinae</topic><topic>Dimerization</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Embryo, Mammalian</topic><topic>Energy transfer</topic><topic>Fluorescence</topic><topic>Fluorescence Resonance Energy Transfer</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Granulocyte-macrophage colony-stimulating factor</topic><topic>Green Fluorescent Proteins</topic><topic>Growth hormones</topic><topic>Humans</topic><topic>Janus kinase</topic><topic>Janus kinase 2</topic><topic>Kidney</topic><topic>Kinases</topic><topic>Kinetics</topic><topic>Luminescent Proteins - genetics</topic><topic>MAP kinase</topic><topic>Microscopy</topic><topic>Microscopy, Fluorescence</topic><topic>Milk Proteins</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Phosphorylation</topic><topic>Placenta</topic><topic>Placental Lactogen - pharmacology</topic><topic>Prolactin</topic><topic>Prolactin receptors</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Receptors, Prolactin - chemistry</topic><topic>Receptors, Prolactin - genetics</topic><topic>Receptors, Somatotropin - chemistry</topic><topic>Receptors, Somatotropin - genetics</topic><topic>Recombinant Proteins</topic><topic>Resonance</topic><topic>Sheep</topic><topic>Stat1 protein</topic><topic>STAT1 Transcription Factor</topic><topic>Stat3 protein</topic><topic>STAT3 Transcription Factor</topic><topic>Stat5 protein</topic><topic>STAT5 Transcription Factor</topic><topic>Trans-Activators - metabolism</topic><topic>Transcription activation</topic><topic>Transducers</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Biener, Eva</creatorcontrib><creatorcontrib>Martin, Cyril</creatorcontrib><creatorcontrib>Daniel, Nathalie</creatorcontrib><creatorcontrib>Frank, Stuart J</creatorcontrib><creatorcontrib>Centonze, Victoria E</creatorcontrib><creatorcontrib>Herman, Brian</creatorcontrib><creatorcontrib>Djiane, Jean</creatorcontrib><creatorcontrib>Gertler, Arieh</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Endocrinology (Philadelphia)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Biener, Eva</au><au>Martin, Cyril</au><au>Daniel, Nathalie</au><au>Frank, Stuart J</au><au>Centonze, Victoria E</au><au>Herman, Brian</au><au>Djiane, Jean</au><au>Gertler, Arieh</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>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</atitle><jtitle>Endocrinology (Philadelphia)</jtitle><addtitle>Endocrinology</addtitle><date>2003-08-01</date><risdate>2003</risdate><volume>144</volume><issue>8</issue><spage>3532</spage><epage>3540</epage><pages>3532-3540</pages><issn>0013-7227</issn><eissn>1945-7170</eissn><coden>ENDOAO</coden><abstract>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.</abstract><cop>Bethesda, MD</cop><pub>Endocrine Society</pub><pmid>12865335</pmid><doi>10.1210/en.2003-0096</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Bacterial Proteins - genetics Biological and medical sciences Cell Line CHO Cells Colony-stimulating factor Cricetinae Dimerization DNA-Binding Proteins - metabolism Embryo, Mammalian Energy transfer Fluorescence Fluorescence Resonance Energy Transfer Fundamental and applied biological sciences. Psychology Granulocyte-macrophage colony-stimulating factor Green Fluorescent Proteins Growth hormones Humans Janus kinase Janus kinase 2 Kidney Kinases Kinetics Luminescent Proteins - genetics MAP kinase Microscopy Microscopy, Fluorescence Milk Proteins Mitogen-Activated Protein Kinases - metabolism Phosphorylation Placenta Placental Lactogen - pharmacology Prolactin Prolactin receptors Proteins Receptors Receptors, Prolactin - chemistry Receptors, Prolactin - genetics Receptors, Somatotropin - chemistry Receptors, Somatotropin - genetics Recombinant Proteins Resonance Sheep Stat1 protein STAT1 Transcription Factor Stat3 protein STAT3 Transcription Factor Stat5 protein STAT5 Transcription Factor Trans-Activators - metabolism Transcription activation Transducers Transfection |
| title | 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 |
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