Endothelin Receptors and Coupled GTP-Binding Proteins in Glomerular Mesangial Cells
Endothelins (ETs) are a family of vasoactive peptides with profound biological actions in diverse cell systems. Among its varied actions, ET stimulates phospholipase C (PLC) in cultured mesangial cells. We investigated the presence of specific ET receptors in rat mesangial cells in culture, and stud...
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| Veröffentlicht in: | Journal of cardiovascular pharmacology 1991, Vol.17 Suppl 7, p.S79-S79 |
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| creator | Thomas, Christie P Baldi, Elisabetta Simonson, Michael S Kester, Mark Dunn, Michael J |
| description | Endothelins (ETs) are a family of vasoactive peptides with profound biological actions in diverse cell systems. Among its varied actions, ET stimulates phospholipase C (PLC) in cultured mesangial cells. We investigated the presence of specific ET receptors in rat mesangial cells in culture, and studied the role of GTP-binding proteins (G proteins) in coupling PLC to the endothelin receptor. [I]ET binding was time- and temperature-dependent, and Scatchard analysis of saturation data showed a single class of high-affinity binding sites. Heterologous displacement with two related peptides, ET-3 and sarafotoxin (SFTX), revealed the presence of two binding sites for these isopeptides. Preincubation of cells with ET-1 reduced the receptor number without affecting K, and this effect was not prevented by protein kinase C inhibition or downregulation. We confirmed the presence of a 41− to 43-kDa pertussis toxin substrate in rat mesangial cell membranes in an ADP ribosylation assay. ET-1 inhibits and GDPβS enhances toxin-catalyzed transfer of ADP-ribose to this substrate. ET-1 potentiated GTPγS-induced phosphatidylinositol (PI) hydrolysis in a concentration-dependent manner. In addition, pertussis toxin partially inhibited ET-stimulated PI hydrolysis in intact mesangial cells. Pertussis toxin also reduced the magnitude of ET-stimulated intracellular free calcium [(Ca )]. Thus, ET-1 binds to specific receptors on rat mesangial cells and activates PLC, in part, through a pertussis toxin-sensitive G-protein. |
| doi_str_mv | 10.1097/00005344-199100177-00022 |
| format | Article |
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Among its varied actions, ET stimulates phospholipase C (PLC) in cultured mesangial cells. We investigated the presence of specific ET receptors in rat mesangial cells in culture, and studied the role of GTP-binding proteins (G proteins) in coupling PLC to the endothelin receptor. [I]ET binding was time- and temperature-dependent, and Scatchard analysis of saturation data showed a single class of high-affinity binding sites. Heterologous displacement with two related peptides, ET-3 and sarafotoxin (SFTX), revealed the presence of two binding sites for these isopeptides. Preincubation of cells with ET-1 reduced the receptor number without affecting K, and this effect was not prevented by protein kinase C inhibition or downregulation. We confirmed the presence of a 41− to 43-kDa pertussis toxin substrate in rat mesangial cell membranes in an ADP ribosylation assay. ET-1 inhibits and GDPβS enhances toxin-catalyzed transfer of ADP-ribose to this substrate. ET-1 potentiated GTPγS-induced phosphatidylinositol (PI) hydrolysis in a concentration-dependent manner. In addition, pertussis toxin partially inhibited ET-stimulated PI hydrolysis in intact mesangial cells. Pertussis toxin also reduced the magnitude of ET-stimulated intracellular free calcium [(Ca )]. Thus, ET-1 binds to specific receptors on rat mesangial cells and activates PLC, in part, through a pertussis toxin-sensitive G-protein.</description><identifier>ISSN: 0160-2446</identifier><identifier>EISSN: 1533-4023</identifier><identifier>DOI: 10.1097/00005344-199100177-00022</identifier><identifier>PMID: 1725439</identifier><identifier>CODEN: JCPCDT</identifier><language>eng</language><publisher>Philadelphia, PA: Lippincott-Raven Publishers</publisher><subject>Adenosine Diphosphate Ribose - metabolism ; Animals ; Biological and medical sciences ; Endothelins - metabolism ; Endothelins - pharmacology ; Enzyme Activation - physiology ; Fundamental and applied biological sciences. Psychology ; Fura-2 ; Glomerular Mesangium - enzymology ; Glomerular Mesangium - metabolism ; GTP-Binding Proteins - metabolism ; Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology ; In Vitro Techniques ; Kinetics ; Pertussis Toxin ; Rats ; Rats, Inbred Strains ; Receptors, Cell Surface - metabolism ; Receptors, Endothelin ; Temperature ; Type C Phospholipases - antagonists & inhibitors ; Type C Phospholipases - metabolism ; Vertebrates: urinary system ; Virulence Factors, Bordetella - pharmacology</subject><ispartof>Journal of cardiovascular pharmacology, 1991, Vol.17 Suppl 7, p.S79-S79</ispartof><rights>Lippincott-Raven Publishers.</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5002-9b9369ad72cb5ea128fa505a59aa7b534aa39aa4a618cd190fa6fd2be3af6ed53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf><![CDATA[$$Uhttp://ovidsp.ovid.com/ovidweb.cgi?T=JS&CSC=Y&NEWS=N&PAGE=fulltext&PDF=y&D=ovft&AN=00005344-199100177-00022$$EPDF$$P50$$Gwolterskluwer$$H]]></linktopdf><linktohtml>$$Uhttp://ovidsp.ovid.com/ovidweb.cgi?T=JS&NEWS=n&CSC=Y&PAGE=fulltext&D=ovft&AN=00005344-199100177-00022$$EHTML$$P50$$Gwolterskluwer$$H</linktohtml><link.rule.ids>309,310,314,780,784,789,790,4024,4050,4051,4609,23930,23931,25140,27923,27924,27925,64666,65461</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5532795$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1725439$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Thomas, Christie P</creatorcontrib><creatorcontrib>Baldi, Elisabetta</creatorcontrib><creatorcontrib>Simonson, Michael S</creatorcontrib><creatorcontrib>Kester, Mark</creatorcontrib><creatorcontrib>Dunn, Michael J</creatorcontrib><title>Endothelin Receptors and Coupled GTP-Binding Proteins in Glomerular Mesangial Cells</title><title>Journal of cardiovascular pharmacology</title><addtitle>J Cardiovasc Pharmacol</addtitle><description>Endothelins (ETs) are a family of vasoactive peptides with profound biological actions in diverse cell systems. Among its varied actions, ET stimulates phospholipase C (PLC) in cultured mesangial cells. We investigated the presence of specific ET receptors in rat mesangial cells in culture, and studied the role of GTP-binding proteins (G proteins) in coupling PLC to the endothelin receptor. [I]ET binding was time- and temperature-dependent, and Scatchard analysis of saturation data showed a single class of high-affinity binding sites. Heterologous displacement with two related peptides, ET-3 and sarafotoxin (SFTX), revealed the presence of two binding sites for these isopeptides. Preincubation of cells with ET-1 reduced the receptor number without affecting K, and this effect was not prevented by protein kinase C inhibition or downregulation. We confirmed the presence of a 41− to 43-kDa pertussis toxin substrate in rat mesangial cell membranes in an ADP ribosylation assay. ET-1 inhibits and GDPβS enhances toxin-catalyzed transfer of ADP-ribose to this substrate. ET-1 potentiated GTPγS-induced phosphatidylinositol (PI) hydrolysis in a concentration-dependent manner. In addition, pertussis toxin partially inhibited ET-stimulated PI hydrolysis in intact mesangial cells. Pertussis toxin also reduced the magnitude of ET-stimulated intracellular free calcium [(Ca )]. Thus, ET-1 binds to specific receptors on rat mesangial cells and activates PLC, in part, through a pertussis toxin-sensitive G-protein.</description><subject>Adenosine Diphosphate Ribose - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Endothelins - metabolism</subject><subject>Endothelins - pharmacology</subject><subject>Enzyme Activation - physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fura-2</subject><subject>Glomerular Mesangium - enzymology</subject><subject>Glomerular Mesangium - metabolism</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>Pertussis Toxin</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Endothelin</subject><subject>Temperature</subject><subject>Type C Phospholipases - antagonists & inhibitors</subject><subject>Type C Phospholipases - metabolism</subject><subject>Vertebrates: urinary system</subject><subject>Virulence Factors, Bordetella - pharmacology</subject><issn>0160-2446</issn><issn>1533-4023</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kV1vFCEUhonR1LX6E0y4MN6N8s1yqZt2Namx0XpNzgxnuqMsrDCTxn8vddd6JTcQznPg5YEQytkbzpx9y9rQUqmOO8cZ49Z2bUeIR2TFtZSdYkI-JivGDeuEUuYpeVbr9wYqbc0ZOeNWaCXdiny9SCHPO4xTol9wwMOcS6WQAt3k5RAx0O3Ndfd-SmFKt_S65BmnVGmjtzHvsSwRCv2EFdLtBJFuMMb6nDwZIVZ8cZrPybfLi5vNh-7q8_bj5t1VN-iWtXO9k8ZBsGLoNQIX6xE006AdgO3b6wBkWyowfD0E7tgIZgyiRwmjwaDlOXl9PPdQ8s8F6-z3Ux1aAkiYl-qtMM5Yphq4PoJDybUWHP2hTHsovzxn_t6n_-vTP_j0f3y21penO5Z-j-Ff41Fgq7861aEOEMcCaZjqA6a1FNbdR1VH7C7HGUv9EZc7LH6HEOed_99vyt-HA4zt</recordid><startdate>1991</startdate><enddate>1991</enddate><creator>Thomas, Christie P</creator><creator>Baldi, Elisabetta</creator><creator>Simonson, Michael S</creator><creator>Kester, Mark</creator><creator>Dunn, Michael J</creator><general>Lippincott-Raven Publishers</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>1991</creationdate><title>Endothelin Receptors and Coupled GTP-Binding Proteins in Glomerular Mesangial Cells</title><author>Thomas, Christie P ; Baldi, Elisabetta ; Simonson, Michael S ; Kester, Mark ; Dunn, Michael J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5002-9b9369ad72cb5ea128fa505a59aa7b534aa39aa4a618cd190fa6fd2be3af6ed53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Adenosine Diphosphate Ribose - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Endothelins - metabolism</topic><topic>Endothelins - pharmacology</topic><topic>Enzyme Activation - physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fura-2</topic><topic>Glomerular Mesangium - enzymology</topic><topic>Glomerular Mesangium - metabolism</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology</topic><topic>In Vitro Techniques</topic><topic>Kinetics</topic><topic>Pertussis Toxin</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Endothelin</topic><topic>Temperature</topic><topic>Type C Phospholipases - antagonists & inhibitors</topic><topic>Type C Phospholipases - metabolism</topic><topic>Vertebrates: urinary system</topic><topic>Virulence Factors, Bordetella - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Thomas, Christie P</creatorcontrib><creatorcontrib>Baldi, Elisabetta</creatorcontrib><creatorcontrib>Simonson, Michael S</creatorcontrib><creatorcontrib>Kester, Mark</creatorcontrib><creatorcontrib>Dunn, Michael J</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>Journal of cardiovascular pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Thomas, Christie P</au><au>Baldi, Elisabetta</au><au>Simonson, Michael S</au><au>Kester, Mark</au><au>Dunn, Michael J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endothelin Receptors and Coupled GTP-Binding Proteins in Glomerular Mesangial Cells</atitle><jtitle>Journal of cardiovascular pharmacology</jtitle><addtitle>J Cardiovasc Pharmacol</addtitle><date>1991</date><risdate>1991</risdate><volume>17 Suppl 7</volume><spage>S79</spage><epage>S79</epage><pages>S79-S79</pages><issn>0160-2446</issn><eissn>1533-4023</eissn><coden>JCPCDT</coden><abstract>Endothelins (ETs) are a family of vasoactive peptides with profound biological actions in diverse cell systems. Among its varied actions, ET stimulates phospholipase C (PLC) in cultured mesangial cells. We investigated the presence of specific ET receptors in rat mesangial cells in culture, and studied the role of GTP-binding proteins (G proteins) in coupling PLC to the endothelin receptor. [I]ET binding was time- and temperature-dependent, and Scatchard analysis of saturation data showed a single class of high-affinity binding sites. Heterologous displacement with two related peptides, ET-3 and sarafotoxin (SFTX), revealed the presence of two binding sites for these isopeptides. Preincubation of cells with ET-1 reduced the receptor number without affecting K, and this effect was not prevented by protein kinase C inhibition or downregulation. We confirmed the presence of a 41− to 43-kDa pertussis toxin substrate in rat mesangial cell membranes in an ADP ribosylation assay. ET-1 inhibits and GDPβS enhances toxin-catalyzed transfer of ADP-ribose to this substrate. ET-1 potentiated GTPγS-induced phosphatidylinositol (PI) hydrolysis in a concentration-dependent manner. In addition, pertussis toxin partially inhibited ET-stimulated PI hydrolysis in intact mesangial cells. Pertussis toxin also reduced the magnitude of ET-stimulated intracellular free calcium [(Ca )]. Thus, ET-1 binds to specific receptors on rat mesangial cells and activates PLC, in part, through a pertussis toxin-sensitive G-protein.</abstract><cop>Philadelphia, PA</cop><cop>Hagerstown, MD</cop><pub>Lippincott-Raven Publishers</pub><pmid>1725439</pmid><doi>10.1097/00005344-199100177-00022</doi><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of cardiovascular pharmacology, 1991, Vol.17 Suppl 7, p.S79-S79 |
| issn | 0160-2446 1533-4023 |
| language | eng |
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| source | MEDLINE; Journals@Ovid LWW Legacy Archive; Journals@Ovid Complete; EZB-FREE-00999 freely available EZB journals |
| subjects | Adenosine Diphosphate Ribose - metabolism Animals Biological and medical sciences Endothelins - metabolism Endothelins - pharmacology Enzyme Activation - physiology Fundamental and applied biological sciences. Psychology Fura-2 Glomerular Mesangium - enzymology Glomerular Mesangium - metabolism GTP-Binding Proteins - metabolism Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology In Vitro Techniques Kinetics Pertussis Toxin Rats Rats, Inbred Strains Receptors, Cell Surface - metabolism Receptors, Endothelin Temperature Type C Phospholipases - antagonists & inhibitors Type C Phospholipases - metabolism Vertebrates: urinary system Virulence Factors, Bordetella - pharmacology |
| title | Endothelin Receptors and Coupled GTP-Binding Proteins in Glomerular Mesangial Cells |
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