Identification of an EDG7 Variant, HOFNH30, a G-Protein-Coupled Receptor for Lysophosphatidic Acid
We have identified a cDNA, designated HOFNH30, which encodes a 354 amino acid G-protein-coupled receptor (GPCR). This receptor has 96% amino acid identity to the Jurkat-T cell-derived EDG7 and could be a splice variant. RT-PCR analysis demonstrated that HOFNH30 mRNA is expressed in placenta whereas...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2000-07, Vol.273 (3), p.805-810 |
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| creator | Fitzgerald, Laura Rydelek Dytko, George M. Sarau, Henry M. Mannan, Ishrat Jahan Ellis, Catherine Lane, Pamela A. Tan, Kong B. Murdock, Paul R. Wilson, Shelagh Bergsma, Derk J. Ames, Robert S. Foley, James J. Campbell, David A. McMillan, Lynnette Evans, Nicholas Elshourbagy, Nabil A. Minehart, Heather Tsui, Ping |
| description | We have identified a cDNA, designated HOFNH30, which encodes a 354 amino acid G-protein-coupled receptor (GPCR). This receptor has 96% amino acid identity to the Jurkat-T cell-derived EDG7 and could be a splice variant. RT-PCR analysis demonstrated that HOFNH30 mRNA is expressed in placenta whereas EDG7 mRNA shows highest expression in prostate. The HOFNH30 gene is localized to human chromosome 1p22.3-1p31.1. When HOFNH30 was expressed in RBL-2H3 cells, LPA and phosphatidic acid (PA) induced a calcium mobilization response with EC50 values of 13 nM and 3 μM, respectively. LPA also induced phosphorylation of mitogen-activated protein kinase (p42MAPK and p44MAPK) in HOFNH30-transfected but not vector-transfected RBL-2H3 cells. In the present study, we have identified a novel variant from the EDG receptor family, a GPCR for which LPA is a high-affinity endogenous ligand. |
| doi_str_mv | 10.1006/bbrc.2000.2943 |
| format | Article |
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This receptor has 96% amino acid identity to the Jurkat-T cell-derived EDG7 and could be a splice variant. RT-PCR analysis demonstrated that HOFNH30 mRNA is expressed in placenta whereas EDG7 mRNA shows highest expression in prostate. The HOFNH30 gene is localized to human chromosome 1p22.3-1p31.1. When HOFNH30 was expressed in RBL-2H3 cells, LPA and phosphatidic acid (PA) induced a calcium mobilization response with EC50 values of 13 nM and 3 μM, respectively. LPA also induced phosphorylation of mitogen-activated protein kinase (p42MAPK and p44MAPK) in HOFNH30-transfected but not vector-transfected RBL-2H3 cells. In the present study, we have identified a novel variant from the EDG receptor family, a GPCR for which LPA is a high-affinity endogenous ligand.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.2000.2943</identifier><identifier>PMID: 10891327</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Base Sequence ; Calcium - metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 1 ; Cloning, Molecular ; Enzyme Activation ; FLIPR ; GTP-Binding Proteins - metabolism ; Humans ; Jurkat Cells ; Lysophospholipids - metabolism ; Mitogen-Activated Protein Kinase 1 - metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases - metabolism ; Molecular Sequence Data ; phospholipid ; Phosphorylation ; Receptors, Cell Surface - chemistry ; Receptors, Cell Surface - genetics ; Receptors, Cell Surface - metabolism ; Receptors, G-Protein-Coupled ; Receptors, Lysophosphatidic Acid ; Sequence Homology, Amino Acid ; seven-transmembrane ; Tumor Cells, Cultured</subject><ispartof>Biochemical and biophysical research communications, 2000-07, Vol.273 (3), p.805-810</ispartof><rights>2000 Academic Press</rights><rights>Copyright 2000 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c435t-128832ab9cd3cfe4ff3b88776ffe16877b58ae183a56f7e0373625f32fdcef933</citedby><cites>FETCH-LOGICAL-c435t-128832ab9cd3cfe4ff3b88776ffe16877b58ae183a56f7e0373625f32fdcef933</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.2000.2943$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10891327$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fitzgerald, Laura Rydelek</creatorcontrib><creatorcontrib>Dytko, George M.</creatorcontrib><creatorcontrib>Sarau, Henry M.</creatorcontrib><creatorcontrib>Mannan, Ishrat Jahan</creatorcontrib><creatorcontrib>Ellis, Catherine</creatorcontrib><creatorcontrib>Lane, Pamela A.</creatorcontrib><creatorcontrib>Tan, Kong B.</creatorcontrib><creatorcontrib>Murdock, Paul R.</creatorcontrib><creatorcontrib>Wilson, Shelagh</creatorcontrib><creatorcontrib>Bergsma, Derk J.</creatorcontrib><creatorcontrib>Ames, Robert S.</creatorcontrib><creatorcontrib>Foley, James J.</creatorcontrib><creatorcontrib>Campbell, David A.</creatorcontrib><creatorcontrib>McMillan, Lynnette</creatorcontrib><creatorcontrib>Evans, Nicholas</creatorcontrib><creatorcontrib>Elshourbagy, Nabil A.</creatorcontrib><creatorcontrib>Minehart, Heather</creatorcontrib><creatorcontrib>Tsui, Ping</creatorcontrib><title>Identification of an EDG7 Variant, HOFNH30, a G-Protein-Coupled Receptor for Lysophosphatidic Acid</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>We have identified a cDNA, designated HOFNH30, which encodes a 354 amino acid G-protein-coupled receptor (GPCR). This receptor has 96% amino acid identity to the Jurkat-T cell-derived EDG7 and could be a splice variant. RT-PCR analysis demonstrated that HOFNH30 mRNA is expressed in placenta whereas EDG7 mRNA shows highest expression in prostate. The HOFNH30 gene is localized to human chromosome 1p22.3-1p31.1. When HOFNH30 was expressed in RBL-2H3 cells, LPA and phosphatidic acid (PA) induced a calcium mobilization response with EC50 values of 13 nM and 3 μM, respectively. LPA also induced phosphorylation of mitogen-activated protein kinase (p42MAPK and p44MAPK) in HOFNH30-transfected but not vector-transfected RBL-2H3 cells. In the present study, we have identified a novel variant from the EDG receptor family, a GPCR for which LPA is a high-affinity endogenous ligand.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Calcium - metabolism</subject><subject>Chromosome Mapping</subject><subject>Chromosomes, Human, Pair 1</subject><subject>Cloning, Molecular</subject><subject>Enzyme Activation</subject><subject>FLIPR</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Humans</subject><subject>Jurkat Cells</subject><subject>Lysophospholipids - metabolism</subject><subject>Mitogen-Activated Protein Kinase 1 - metabolism</subject><subject>Mitogen-Activated Protein Kinase 3</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Molecular Sequence Data</subject><subject>phospholipid</subject><subject>Phosphorylation</subject><subject>Receptors, Cell Surface - chemistry</subject><subject>Receptors, Cell Surface - genetics</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, G-Protein-Coupled</subject><subject>Receptors, Lysophosphatidic Acid</subject><subject>Sequence Homology, Amino Acid</subject><subject>seven-transmembrane</subject><subject>Tumor Cells, Cultured</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMtLAzEQh4MotlavHiUnT901j30epfYFxYqoeAvZZEIj7WZNdoX-925pD148DDMM3_xgPoRuKYkpIdlDVXkVM0JIzMqEn6EhJSWJGCXJORr26yxiJf0coKsQvgihNMnKSzSgpCgpZ_kQVUsNdWuNVbK1rsbOYFnj6dM8xx_SW1m3Y7xYz54XnIyxxPPoxbsWbB1NXNdsQeNXUNC0zmPT12ofXLNxodn0adoq_KisvkYXRm4D3Jz6CL3Ppm-TRbRaz5eTx1WkEp62EWVFwZmsSqW5MpAYw6uiyPPMGKBZP1RpIYEWXKaZyYHwnGcsNZwZrcCUnI_Q_TG38e67g9CKnQ0KtltZg-uCyCljNEvyHoyPoPIuBA9GNN7upN8LSsTBqjhYFQer4mC1P7g7JXfVDvQf_KixB4ojAP1_Pxa8CMpCrUBbD6oV2tn_sn8BOlWE2Q</recordid><startdate>20000714</startdate><enddate>20000714</enddate><creator>Fitzgerald, Laura Rydelek</creator><creator>Dytko, George M.</creator><creator>Sarau, Henry M.</creator><creator>Mannan, Ishrat Jahan</creator><creator>Ellis, Catherine</creator><creator>Lane, Pamela A.</creator><creator>Tan, Kong B.</creator><creator>Murdock, Paul R.</creator><creator>Wilson, Shelagh</creator><creator>Bergsma, Derk J.</creator><creator>Ames, Robert S.</creator><creator>Foley, James J.</creator><creator>Campbell, David A.</creator><creator>McMillan, Lynnette</creator><creator>Evans, Nicholas</creator><creator>Elshourbagy, Nabil A.</creator><creator>Minehart, Heather</creator><creator>Tsui, Ping</creator><general>Elsevier Inc</general><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>20000714</creationdate><title>Identification of an EDG7 Variant, HOFNH30, a G-Protein-Coupled Receptor for Lysophosphatidic Acid</title><author>Fitzgerald, Laura Rydelek ; Dytko, George M. ; Sarau, Henry M. ; Mannan, Ishrat Jahan ; Ellis, Catherine ; Lane, Pamela A. ; Tan, Kong B. ; Murdock, Paul R. ; Wilson, Shelagh ; Bergsma, Derk J. ; Ames, Robert S. ; Foley, James J. ; Campbell, David A. ; McMillan, Lynnette ; Evans, Nicholas ; Elshourbagy, Nabil A. ; Minehart, Heather ; Tsui, Ping</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c435t-128832ab9cd3cfe4ff3b88776ffe16877b58ae183a56f7e0373625f32fdcef933</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Calcium - metabolism</topic><topic>Chromosome Mapping</topic><topic>Chromosomes, Human, Pair 1</topic><topic>Cloning, Molecular</topic><topic>Enzyme Activation</topic><topic>FLIPR</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>Humans</topic><topic>Jurkat Cells</topic><topic>Lysophospholipids - metabolism</topic><topic>Mitogen-Activated Protein Kinase 1 - metabolism</topic><topic>Mitogen-Activated Protein Kinase 3</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Molecular Sequence Data</topic><topic>phospholipid</topic><topic>Phosphorylation</topic><topic>Receptors, Cell Surface - chemistry</topic><topic>Receptors, Cell Surface - genetics</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, G-Protein-Coupled</topic><topic>Receptors, Lysophosphatidic Acid</topic><topic>Sequence Homology, Amino Acid</topic><topic>seven-transmembrane</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fitzgerald, Laura Rydelek</creatorcontrib><creatorcontrib>Dytko, George M.</creatorcontrib><creatorcontrib>Sarau, Henry M.</creatorcontrib><creatorcontrib>Mannan, Ishrat Jahan</creatorcontrib><creatorcontrib>Ellis, Catherine</creatorcontrib><creatorcontrib>Lane, Pamela A.</creatorcontrib><creatorcontrib>Tan, Kong B.</creatorcontrib><creatorcontrib>Murdock, Paul R.</creatorcontrib><creatorcontrib>Wilson, Shelagh</creatorcontrib><creatorcontrib>Bergsma, Derk J.</creatorcontrib><creatorcontrib>Ames, Robert S.</creatorcontrib><creatorcontrib>Foley, James J.</creatorcontrib><creatorcontrib>Campbell, David A.</creatorcontrib><creatorcontrib>McMillan, Lynnette</creatorcontrib><creatorcontrib>Evans, Nicholas</creatorcontrib><creatorcontrib>Elshourbagy, Nabil A.</creatorcontrib><creatorcontrib>Minehart, Heather</creatorcontrib><creatorcontrib>Tsui, Ping</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fitzgerald, Laura Rydelek</au><au>Dytko, George M.</au><au>Sarau, Henry M.</au><au>Mannan, Ishrat Jahan</au><au>Ellis, Catherine</au><au>Lane, Pamela A.</au><au>Tan, Kong B.</au><au>Murdock, Paul R.</au><au>Wilson, Shelagh</au><au>Bergsma, Derk J.</au><au>Ames, Robert S.</au><au>Foley, James J.</au><au>Campbell, David A.</au><au>McMillan, Lynnette</au><au>Evans, Nicholas</au><au>Elshourbagy, Nabil A.</au><au>Minehart, Heather</au><au>Tsui, Ping</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of an EDG7 Variant, HOFNH30, a G-Protein-Coupled Receptor for Lysophosphatidic Acid</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2000-07-14</date><risdate>2000</risdate><volume>273</volume><issue>3</issue><spage>805</spage><epage>810</epage><pages>805-810</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>We have identified a cDNA, designated HOFNH30, which encodes a 354 amino acid G-protein-coupled receptor (GPCR). This receptor has 96% amino acid identity to the Jurkat-T cell-derived EDG7 and could be a splice variant. RT-PCR analysis demonstrated that HOFNH30 mRNA is expressed in placenta whereas EDG7 mRNA shows highest expression in prostate. The HOFNH30 gene is localized to human chromosome 1p22.3-1p31.1. When HOFNH30 was expressed in RBL-2H3 cells, LPA and phosphatidic acid (PA) induced a calcium mobilization response with EC50 values of 13 nM and 3 μM, respectively. LPA also induced phosphorylation of mitogen-activated protein kinase (p42MAPK and p44MAPK) in HOFNH30-transfected but not vector-transfected RBL-2H3 cells. In the present study, we have identified a novel variant from the EDG receptor family, a GPCR for which LPA is a high-affinity endogenous ligand.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10891327</pmid><doi>10.1006/bbrc.2000.2943</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 2000-07, Vol.273 (3), p.805-810 |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Base Sequence Calcium - metabolism Chromosome Mapping Chromosomes, Human, Pair 1 Cloning, Molecular Enzyme Activation FLIPR GTP-Binding Proteins - metabolism Humans Jurkat Cells Lysophospholipids - metabolism Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases - metabolism Molecular Sequence Data phospholipid Phosphorylation Receptors, Cell Surface - chemistry Receptors, Cell Surface - genetics Receptors, Cell Surface - metabolism Receptors, G-Protein-Coupled Receptors, Lysophosphatidic Acid Sequence Homology, Amino Acid seven-transmembrane Tumor Cells, Cultured |
| title | Identification of an EDG7 Variant, HOFNH30, a G-Protein-Coupled Receptor for Lysophosphatidic Acid |
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