IDENTIFICATION AND CHARACTERIZATION OF THE MOUSE AND RAT RELAXIN RECEPTORS AS THE NOVEL ORTHOLOGUES OF HUMAN LEUCINE-RICH REPEAT-CONTAINING G-PROTEIN-COUPLED RECEPTOR 7
SUMMARY 1. Relaxin is an extracellular matrix (ECM)‐remodelling hormone that is functionally important in reproductive tissues, brain, lung and heart. 2. Recently, the human relaxin receptor was identified as leucine‐rich repeat‐containing G‐protein‐coupled receptor 7 (LGR7). 3. Using human LGR7 as...
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| Veröffentlicht in: | Clinical and experimental pharmacology & physiology 2004-11, Vol.31 (11), p.828-832 |
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| creator | Scott, DJ Layfield, S Riesewijk, A Morita, H Tregear, GW Bathgate, RAD |
| description | SUMMARY
1. Relaxin is an extracellular matrix (ECM)‐remodelling hormone that is functionally important in reproductive tissues, brain, lung and heart.
2. Recently, the human relaxin receptor was identified as leucine‐rich repeat‐containing G‐protein‐coupled receptor 7 (LGR7).
3. Using human LGR7 as a template, we identified mouse and rat LGR7 orthologues in the Celera and National Centre for Biotechnology Information databases.
4. At the protein level, mouse and rat LGR7 share 85.2 and 85.7% identity with human LGR7, respectively.
5. Mouse LGR7 mRNA was detected in all tissues where relaxin binding is observed.
6. Mouse and rat LGR7 bound [33P]‐relaxin with high affinity and, upon relaxin treatment, both receptors stimulated cAMP production in transfected HEK 293T cells.
7. These results indicate that mouse and rat LGR7 are the relaxin receptors in these species.
8. The actions of relaxin in rodents are well characterized, providing an established platform for research into the molecular pharmacology of the highly conserved relaxin receptor. |
| doi_str_mv | 10.1111/j.1440-1681.2004.04075.x |
| format | Article |
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1. Relaxin is an extracellular matrix (ECM)‐remodelling hormone that is functionally important in reproductive tissues, brain, lung and heart.
2. Recently, the human relaxin receptor was identified as leucine‐rich repeat‐containing G‐protein‐coupled receptor 7 (LGR7).
3. Using human LGR7 as a template, we identified mouse and rat LGR7 orthologues in the Celera and National Centre for Biotechnology Information databases.
4. At the protein level, mouse and rat LGR7 share 85.2 and 85.7% identity with human LGR7, respectively.
5. Mouse LGR7 mRNA was detected in all tissues where relaxin binding is observed.
6. Mouse and rat LGR7 bound [33P]‐relaxin with high affinity and, upon relaxin treatment, both receptors stimulated cAMP production in transfected HEK 293T cells.
7. These results indicate that mouse and rat LGR7 are the relaxin receptors in these species.
8. The actions of relaxin in rodents are well characterized, providing an established platform for research into the molecular pharmacology of the highly conserved relaxin receptor.</description><identifier>ISSN: 0305-1870</identifier><identifier>EISSN: 1440-1681</identifier><identifier>DOI: 10.1111/j.1440-1681.2004.04075.x</identifier><identifier>PMID: 15566402</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Pty</publisher><subject>Amino Acid Sequence ; Animals ; Blotting, Northern ; Computational Biology ; Cyclic AMP - biosynthesis ; extracellular matrix ; Humans ; insulin-like peptide 3 (INSL3) ; insulin-like peptides ; leucine-rich repeat-containing G-protein-coupled receptor 7 (LGR7) ; Ligands ; Membrane Proteins - drug effects ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mice ; pregnancy ; Rats ; Receptors, G-Protein-Coupled - drug effects ; Receptors, G-Protein-Coupled - genetics ; Receptors, G-Protein-Coupled - metabolism ; Receptors, Peptide - drug effects ; Receptors, Peptide - genetics ; Receptors, Peptide - metabolism ; relaxin ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - biosynthesis ; RNA, Messenger - chemistry ; RNA, Messenger - genetics ; Signal Transduction - drug effects ; Species Specificity ; Tissue Distribution</subject><ispartof>Clinical and experimental pharmacology & physiology, 2004-11, Vol.31 (11), p.828-832</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4035-3f558214b56659b1474b3e186fc8ea73a36c96e3187b02f88801fad4841699b53</citedby><cites>FETCH-LOGICAL-c4035-3f558214b56659b1474b3e186fc8ea73a36c96e3187b02f88801fad4841699b53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1440-1681.2004.04075.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1440-1681.2004.04075.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15566402$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Scott, DJ</creatorcontrib><creatorcontrib>Layfield, S</creatorcontrib><creatorcontrib>Riesewijk, A</creatorcontrib><creatorcontrib>Morita, H</creatorcontrib><creatorcontrib>Tregear, GW</creatorcontrib><creatorcontrib>Bathgate, RAD</creatorcontrib><title>IDENTIFICATION AND CHARACTERIZATION OF THE MOUSE AND RAT RELAXIN RECEPTORS AS THE NOVEL ORTHOLOGUES OF HUMAN LEUCINE-RICH REPEAT-CONTAINING G-PROTEIN-COUPLED RECEPTOR 7</title><title>Clinical and experimental pharmacology & physiology</title><addtitle>Clin Exp Pharmacol Physiol</addtitle><description>SUMMARY
1. Relaxin is an extracellular matrix (ECM)‐remodelling hormone that is functionally important in reproductive tissues, brain, lung and heart.
2. Recently, the human relaxin receptor was identified as leucine‐rich repeat‐containing G‐protein‐coupled receptor 7 (LGR7).
3. Using human LGR7 as a template, we identified mouse and rat LGR7 orthologues in the Celera and National Centre for Biotechnology Information databases.
4. At the protein level, mouse and rat LGR7 share 85.2 and 85.7% identity with human LGR7, respectively.
5. Mouse LGR7 mRNA was detected in all tissues where relaxin binding is observed.
6. Mouse and rat LGR7 bound [33P]‐relaxin with high affinity and, upon relaxin treatment, both receptors stimulated cAMP production in transfected HEK 293T cells.
7. These results indicate that mouse and rat LGR7 are the relaxin receptors in these species.
8. The actions of relaxin in rodents are well characterized, providing an established platform for research into the molecular pharmacology of the highly conserved relaxin receptor.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Blotting, Northern</subject><subject>Computational Biology</subject><subject>Cyclic AMP - biosynthesis</subject><subject>extracellular matrix</subject><subject>Humans</subject><subject>insulin-like peptide 3 (INSL3)</subject><subject>insulin-like peptides</subject><subject>leucine-rich repeat-containing G-protein-coupled receptor 7 (LGR7)</subject><subject>Ligands</subject><subject>Membrane Proteins - drug effects</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>pregnancy</subject><subject>Rats</subject><subject>Receptors, G-Protein-Coupled - drug effects</subject><subject>Receptors, G-Protein-Coupled - genetics</subject><subject>Receptors, G-Protein-Coupled - metabolism</subject><subject>Receptors, Peptide - drug effects</subject><subject>Receptors, Peptide - genetics</subject><subject>Receptors, Peptide - metabolism</subject><subject>relaxin</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - biosynthesis</subject><subject>RNA, Messenger - chemistry</subject><subject>RNA, Messenger - genetics</subject><subject>Signal Transduction - drug effects</subject><subject>Species Specificity</subject><subject>Tissue Distribution</subject><issn>0305-1870</issn><issn>1440-1681</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcGO0zAQhiMEYsvCKyCfuCXYseO4Bw5W6jaWsk43cWDFxUqyjtTS0iXZiu4b8Zg4TVWu-DLW-P9mxvN7HkAwQO583gaIEOgjylAQQkgCSGAcBadX3uz68NqbQQwjH7EY3njvhmELIYwgxW-9GxRFlBIYzrw_ciGUlkuZcC1zBbhagCTlBU-0KOT3KZkvgU4FuMurUpwVBdegEBl_kMrFRKx1XpSAl2eZyr-KDOSFTvMsX1WiHPm0uuMKZKJKpBJ-IZPUgWvBtZ_kSnOppFqBlb8uci2kcslqnYnFtTiI33tvuno32A-XeOtVS6GT1Hc93PCZ3xKIIx93UcRCRBr3wWjeIBKTBlvEaNcyW8e4xrSdU4vdVhoYdowxiLr6kTCC6HzeRPjW-zTVfeoPv452eDb7zdDa3a7-aQ_HwdAYQcIwdUI2Cdv-MAy97cxTv9nX_YtB0Iwuma0ZzTCjGWZ0yZxdMieHfrz0ODZ7-_gPvNjiBF8mwe_Nzr78d2HjljXeHO9P_GZ4tqcrX_c_3PzYSb-plVmU98V9_JCYEP8FcVihBA</recordid><startdate>200411</startdate><enddate>200411</enddate><creator>Scott, DJ</creator><creator>Layfield, S</creator><creator>Riesewijk, A</creator><creator>Morita, H</creator><creator>Tregear, GW</creator><creator>Bathgate, RAD</creator><general>Blackwell Science Pty</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>200411</creationdate><title>IDENTIFICATION AND CHARACTERIZATION OF THE MOUSE AND RAT RELAXIN RECEPTORS AS THE NOVEL ORTHOLOGUES OF HUMAN LEUCINE-RICH REPEAT-CONTAINING G-PROTEIN-COUPLED RECEPTOR 7</title><author>Scott, DJ ; Layfield, S ; Riesewijk, A ; Morita, H ; Tregear, GW ; Bathgate, RAD</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4035-3f558214b56659b1474b3e186fc8ea73a36c96e3187b02f88801fad4841699b53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Blotting, Northern</topic><topic>Computational Biology</topic><topic>Cyclic AMP - biosynthesis</topic><topic>extracellular matrix</topic><topic>Humans</topic><topic>insulin-like peptide 3 (INSL3)</topic><topic>insulin-like peptides</topic><topic>leucine-rich repeat-containing G-protein-coupled receptor 7 (LGR7)</topic><topic>Ligands</topic><topic>Membrane Proteins - drug effects</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>pregnancy</topic><topic>Rats</topic><topic>Receptors, G-Protein-Coupled - drug effects</topic><topic>Receptors, G-Protein-Coupled - genetics</topic><topic>Receptors, G-Protein-Coupled - metabolism</topic><topic>Receptors, Peptide - drug effects</topic><topic>Receptors, Peptide - genetics</topic><topic>Receptors, Peptide - metabolism</topic><topic>relaxin</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - biosynthesis</topic><topic>RNA, Messenger - chemistry</topic><topic>RNA, Messenger - genetics</topic><topic>Signal Transduction - drug effects</topic><topic>Species Specificity</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Scott, DJ</creatorcontrib><creatorcontrib>Layfield, S</creatorcontrib><creatorcontrib>Riesewijk, A</creatorcontrib><creatorcontrib>Morita, H</creatorcontrib><creatorcontrib>Tregear, GW</creatorcontrib><creatorcontrib>Bathgate, RAD</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Clinical and experimental pharmacology & physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Scott, DJ</au><au>Layfield, S</au><au>Riesewijk, A</au><au>Morita, H</au><au>Tregear, GW</au><au>Bathgate, RAD</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>IDENTIFICATION AND CHARACTERIZATION OF THE MOUSE AND RAT RELAXIN RECEPTORS AS THE NOVEL ORTHOLOGUES OF HUMAN LEUCINE-RICH REPEAT-CONTAINING G-PROTEIN-COUPLED RECEPTOR 7</atitle><jtitle>Clinical and experimental pharmacology & physiology</jtitle><addtitle>Clin Exp Pharmacol Physiol</addtitle><date>2004-11</date><risdate>2004</risdate><volume>31</volume><issue>11</issue><spage>828</spage><epage>832</epage><pages>828-832</pages><issn>0305-1870</issn><eissn>1440-1681</eissn><abstract>SUMMARY
1. Relaxin is an extracellular matrix (ECM)‐remodelling hormone that is functionally important in reproductive tissues, brain, lung and heart.
2. Recently, the human relaxin receptor was identified as leucine‐rich repeat‐containing G‐protein‐coupled receptor 7 (LGR7).
3. Using human LGR7 as a template, we identified mouse and rat LGR7 orthologues in the Celera and National Centre for Biotechnology Information databases.
4. At the protein level, mouse and rat LGR7 share 85.2 and 85.7% identity with human LGR7, respectively.
5. Mouse LGR7 mRNA was detected in all tissues where relaxin binding is observed.
6. Mouse and rat LGR7 bound [33P]‐relaxin with high affinity and, upon relaxin treatment, both receptors stimulated cAMP production in transfected HEK 293T cells.
7. These results indicate that mouse and rat LGR7 are the relaxin receptors in these species.
8. The actions of relaxin in rodents are well characterized, providing an established platform for research into the molecular pharmacology of the highly conserved relaxin receptor.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Pty</pub><pmid>15566402</pmid><doi>10.1111/j.1440-1681.2004.04075.x</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Clinical and experimental pharmacology & physiology, 2004-11, Vol.31 (11), p.828-832 |
| issn | 0305-1870 1440-1681 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67104836 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Amino Acid Sequence Animals Blotting, Northern Computational Biology Cyclic AMP - biosynthesis extracellular matrix Humans insulin-like peptide 3 (INSL3) insulin-like peptides leucine-rich repeat-containing G-protein-coupled receptor 7 (LGR7) Ligands Membrane Proteins - drug effects Membrane Proteins - genetics Membrane Proteins - metabolism Mice pregnancy Rats Receptors, G-Protein-Coupled - drug effects Receptors, G-Protein-Coupled - genetics Receptors, G-Protein-Coupled - metabolism Receptors, Peptide - drug effects Receptors, Peptide - genetics Receptors, Peptide - metabolism relaxin Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - biosynthesis RNA, Messenger - chemistry RNA, Messenger - genetics Signal Transduction - drug effects Species Specificity Tissue Distribution |
| title | IDENTIFICATION AND CHARACTERIZATION OF THE MOUSE AND RAT RELAXIN RECEPTORS AS THE NOVEL ORTHOLOGUES OF HUMAN LEUCINE-RICH REPEAT-CONTAINING G-PROTEIN-COUPLED RECEPTOR 7 |
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