Cloning and Expression of a Human Endothelin Receptor: Subtype A
The polymerase chain reaction, employing degenerate primers specific for the intramembrane domains III and VI of G-coupled receptors, was used to generate partial clones encoding those receptors carried by cultured rat aorta smooth muscle cells. One clone, spanning the intramembrane domains IV–VI of...
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Veröffentlicht in: | The American journal of the medical sciences 1992-10, Vol.304 (4), p.231-238 |
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description | The polymerase chain reaction, employing degenerate primers specific for the intramembrane domains III and VI of G-coupled receptors, was used to generate partial clones encoding those receptors carried by cultured rat aorta smooth muscle cells. One clone, spanning the intramembrane domains IV–VI of a receptor specific for endothelin-1 (ET-R[A]), was used as a probe to screen a human placental cDNA library. The clone pL4-3, encoding a selective type of human endothelin receptor (ET-R[A]), has an open reading frame encoding a protein 427 amino acids in length, with a relative molecular weight of 48, 625 daltons. The sequence analysis suggests the presence of a signal peptide, two potential sites for glycosylation in the N terminal extracellular domain, the seven transmembrane domains typical of G-protein receptors, and several potential sites for phosphorylation in the C terminal cytoplasmic domain. At the amino acid level, the human ET-R(A) shows 91% and 94% identity with the rat and bovine ET-R(A)s, respectively, and 59% similarity with the human ET-R(B). Xenopus laevis oocytes injected with the cloned cDNA express binding sites specific for endothelin-1. Expression of the message in COS 7 cells gave a membrane-bound product to which binding of the [125I]-ET-1 was inhibited by peptide analogues specific for ET-R(A). |
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One clone, spanning the intramembrane domains IV–VI of a receptor specific for endothelin-1 (ET-R[A]), was used as a probe to screen a human placental cDNA library. The clone pL4-3, encoding a selective type of human endothelin receptor (ET-R[A]), has an open reading frame encoding a protein 427 amino acids in length, with a relative molecular weight of 48, 625 daltons. The sequence analysis suggests the presence of a signal peptide, two potential sites for glycosylation in the N terminal extracellular domain, the seven transmembrane domains typical of G-protein receptors, and several potential sites for phosphorylation in the C terminal cytoplasmic domain. At the amino acid level, the human ET-R(A) shows 91% and 94% identity with the rat and bovine ET-R(A)s, respectively, and 59% similarity with the human ET-R(B). Xenopus laevis oocytes injected with the cloned cDNA express binding sites specific for endothelin-1. Expression of the message in COS 7 cells gave a membrane-bound product to which binding of the [125I]-ET-1 was inhibited by peptide analogues specific for ET-R(A).</description><identifier>ISSN: 0002-9629</identifier><identifier>EISSN: 1538-2990</identifier><identifier>DOI: 10.1097/00000441-199210000-00002</identifier><identifier>PMID: 1415318</identifier><identifier>CODEN: AJMSA9</identifier><language>eng</language><publisher>Hagerstown, MD: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Aorta - physiology ; Base Sequence ; Biological and medical sciences ; Blood vessels and receptors ; Cattle ; Cell Line ; Cell Membrane - metabolism ; Cells, Cultured ; Cloning ; Cloning, Molecular ; Endothelin receptor ; Endothelins - metabolism ; Expression ; Female ; Fundamental and applied biological sciences. Psychology ; Gene Library ; Humans ; Kinetics ; Ligand binding ; Molecular Sequence Data ; Muscle, Smooth, Vascular - physiology ; Oligodeoxyribonucleotides ; Placenta - physiology ; Polymerase Chain Reaction ; Pregnancy ; Rats ; Receptors, Endothelin - classification ; Receptors, Endothelin - genetics ; Receptors, Endothelin - metabolism ; Sequence Homology, Amino Acid ; Sequence Homology, Nucleic Acid ; Transfection ; Vertebrates: cardiovascular system</subject><ispartof>The American journal of the medical sciences, 1992-10, Vol.304 (4), p.231-238</ispartof><rights>1992 Southern Society for Clinical Investigation</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c398t-d5e0b05d3326df10740538ff9a200e141ddde666d7555891f5bf44a979563b1e3</citedby><cites>FETCH-LOGICAL-c398t-d5e0b05d3326df10740538ff9a200e141ddde666d7555891f5bf44a979563b1e3</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=3953195$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1415318$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hayzer, David J.</creatorcontrib><creatorcontrib>Rose, Patricia M.</creatorcontrib><creatorcontrib>Lynch, Jean S.</creatorcontrib><creatorcontrib>Webb, Maria L.</creatorcontrib><creatorcontrib>Kienzle, Bernadette K.</creatorcontrib><creatorcontrib>Liu, Edward C.-K.</creatorcontrib><creatorcontrib>Bogosian, Elizabeth A.</creatorcontrib><creatorcontrib>Brinson, Eleanor</creatorcontrib><creatorcontrib>Runge, Marschall S.</creatorcontrib><title>Cloning and Expression of a Human Endothelin Receptor: Subtype A</title><title>The American journal of the medical sciences</title><addtitle>Am J Med Sci</addtitle><description>The polymerase chain reaction, employing degenerate primers specific for the intramembrane domains III and VI of G-coupled receptors, was used to generate partial clones encoding those receptors carried by cultured rat aorta smooth muscle cells. One clone, spanning the intramembrane domains IV–VI of a receptor specific for endothelin-1 (ET-R[A]), was used as a probe to screen a human placental cDNA library. The clone pL4-3, encoding a selective type of human endothelin receptor (ET-R[A]), has an open reading frame encoding a protein 427 amino acids in length, with a relative molecular weight of 48, 625 daltons. The sequence analysis suggests the presence of a signal peptide, two potential sites for glycosylation in the N terminal extracellular domain, the seven transmembrane domains typical of G-protein receptors, and several potential sites for phosphorylation in the C terminal cytoplasmic domain. At the amino acid level, the human ET-R(A) shows 91% and 94% identity with the rat and bovine ET-R(A)s, respectively, and 59% similarity with the human ET-R(B). Xenopus laevis oocytes injected with the cloned cDNA express binding sites specific for endothelin-1. Expression of the message in COS 7 cells gave a membrane-bound product to which binding of the [125I]-ET-1 was inhibited by peptide analogues specific for ET-R(A).</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Aorta - physiology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blood vessels and receptors</subject><subject>Cattle</subject><subject>Cell Line</subject><subject>Cell Membrane - metabolism</subject><subject>Cells, Cultured</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>Endothelin receptor</subject><subject>Endothelins - metabolism</subject><subject>Expression</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Library</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Ligand binding</subject><subject>Molecular Sequence Data</subject><subject>Muscle, Smooth, Vascular - physiology</subject><subject>Oligodeoxyribonucleotides</subject><subject>Placenta - physiology</subject><subject>Polymerase Chain Reaction</subject><subject>Pregnancy</subject><subject>Rats</subject><subject>Receptors, Endothelin - classification</subject><subject>Receptors, Endothelin - genetics</subject><subject>Receptors, Endothelin - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Transfection</subject><subject>Vertebrates: cardiovascular system</subject><issn>0002-9629</issn><issn>1538-2990</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1PGzEQhi0ESkPoT0DyoeK2rT_2yz0VohSQkJBoOVtee9y62thbexfBv8fbpOGIJXvkmWdmXr0IYUo-UyKaL2Q-ZUkLKgSj86eYH3aElrTibcGEIMdoOacKUTPxAZ2m9IcQylrKF2hBy4zRdom-rfvgnf-FlTd48zxESMkFj4PFCt9MW-Xxxpsw_obeefwAGoYxxK_4x9SNLwPgyzN0YlWf4OM-rtDj983P9U1xd399u768KzQX7ViYCkhHKsM5q42lpClJ1mmtUIwQyHKMMVDXtWmqqmoFtVVny1KJRlQ17yjwFbrYzR1i-DtBGuXWJQ19rzyEKcmGs1K0TZ3BdgfqGFKKYOUQ3VbFF0mJnM2T_82TB_P-pVhuPd_vmLotmLfGnVu5_mlfV0mr3kbltUsHjItM5btCVzsMsh9PDqJM2oHXYFwEPUoT3PtaXgEBn4iR</recordid><startdate>19921001</startdate><enddate>19921001</enddate><creator>Hayzer, David J.</creator><creator>Rose, Patricia M.</creator><creator>Lynch, Jean S.</creator><creator>Webb, Maria L.</creator><creator>Kienzle, Bernadette K.</creator><creator>Liu, Edward C.-K.</creator><creator>Bogosian, Elizabeth A.</creator><creator>Brinson, Eleanor</creator><creator>Runge, Marschall S.</creator><general>Elsevier Inc</general><general>Lippincott</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>7X8</scope></search><sort><creationdate>19921001</creationdate><title>Cloning and Expression of a Human Endothelin Receptor: Subtype A</title><author>Hayzer, David J. ; Rose, Patricia M. ; Lynch, Jean S. ; Webb, Maria L. ; Kienzle, Bernadette K. ; Liu, Edward C.-K. ; Bogosian, Elizabeth A. ; Brinson, Eleanor ; Runge, Marschall S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c398t-d5e0b05d3326df10740538ff9a200e141ddde666d7555891f5bf44a979563b1e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Aorta - physiology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Blood vessels and receptors</topic><topic>Cattle</topic><topic>Cell Line</topic><topic>Cell Membrane - metabolism</topic><topic>Cells, Cultured</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>Endothelin receptor</topic><topic>Endothelins - metabolism</topic><topic>Expression</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Library</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Ligand binding</topic><topic>Molecular Sequence Data</topic><topic>Muscle, Smooth, Vascular - physiology</topic><topic>Oligodeoxyribonucleotides</topic><topic>Placenta - physiology</topic><topic>Polymerase Chain Reaction</topic><topic>Pregnancy</topic><topic>Rats</topic><topic>Receptors, Endothelin - classification</topic><topic>Receptors, Endothelin - genetics</topic><topic>Receptors, Endothelin - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Transfection</topic><topic>Vertebrates: cardiovascular system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hayzer, David J.</creatorcontrib><creatorcontrib>Rose, Patricia M.</creatorcontrib><creatorcontrib>Lynch, Jean S.</creatorcontrib><creatorcontrib>Webb, Maria L.</creatorcontrib><creatorcontrib>Kienzle, Bernadette K.</creatorcontrib><creatorcontrib>Liu, Edward C.-K.</creatorcontrib><creatorcontrib>Bogosian, Elizabeth A.</creatorcontrib><creatorcontrib>Brinson, Eleanor</creatorcontrib><creatorcontrib>Runge, Marschall S.</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>MEDLINE - Academic</collection><jtitle>The American journal of the medical sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hayzer, David J.</au><au>Rose, Patricia M.</au><au>Lynch, Jean S.</au><au>Webb, Maria L.</au><au>Kienzle, Bernadette K.</au><au>Liu, Edward C.-K.</au><au>Bogosian, Elizabeth A.</au><au>Brinson, Eleanor</au><au>Runge, Marschall S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and Expression of a Human Endothelin Receptor: Subtype A</atitle><jtitle>The American journal of the medical sciences</jtitle><addtitle>Am J Med Sci</addtitle><date>1992-10-01</date><risdate>1992</risdate><volume>304</volume><issue>4</issue><spage>231</spage><epage>238</epage><pages>231-238</pages><issn>0002-9629</issn><eissn>1538-2990</eissn><coden>AJMSA9</coden><abstract>The polymerase chain reaction, employing degenerate primers specific for the intramembrane domains III and VI of G-coupled receptors, was used to generate partial clones encoding those receptors carried by cultured rat aorta smooth muscle cells. One clone, spanning the intramembrane domains IV–VI of a receptor specific for endothelin-1 (ET-R[A]), was used as a probe to screen a human placental cDNA library. The clone pL4-3, encoding a selective type of human endothelin receptor (ET-R[A]), has an open reading frame encoding a protein 427 amino acids in length, with a relative molecular weight of 48, 625 daltons. The sequence analysis suggests the presence of a signal peptide, two potential sites for glycosylation in the N terminal extracellular domain, the seven transmembrane domains typical of G-protein receptors, and several potential sites for phosphorylation in the C terminal cytoplasmic domain. At the amino acid level, the human ET-R(A) shows 91% and 94% identity with the rat and bovine ET-R(A)s, respectively, and 59% similarity with the human ET-R(B). Xenopus laevis oocytes injected with the cloned cDNA express binding sites specific for endothelin-1. Expression of the message in COS 7 cells gave a membrane-bound product to which binding of the [125I]-ET-1 was inhibited by peptide analogues specific for ET-R(A).</abstract><cop>Hagerstown, MD</cop><pub>Elsevier Inc</pub><pmid>1415318</pmid><doi>10.1097/00000441-199210000-00002</doi><tpages>8</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Aorta - physiology Base Sequence Biological and medical sciences Blood vessels and receptors Cattle Cell Line Cell Membrane - metabolism Cells, Cultured Cloning Cloning, Molecular Endothelin receptor Endothelins - metabolism Expression Female Fundamental and applied biological sciences. Psychology Gene Library Humans Kinetics Ligand binding Molecular Sequence Data Muscle, Smooth, Vascular - physiology Oligodeoxyribonucleotides Placenta - physiology Polymerase Chain Reaction Pregnancy Rats Receptors, Endothelin - classification Receptors, Endothelin - genetics Receptors, Endothelin - metabolism Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid Transfection Vertebrates: cardiovascular system |
title | Cloning and Expression of a Human Endothelin Receptor: Subtype A |
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