G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides
The neuropeptide substance P, the venom peptide mastoparan and the synthetic polyamine compound 48/80 activate rat peritoneal mast cells, leading to rapid histamine release by exocytosis. Although these effects are inhibited by pertussis toxin and involve a transient increase in IP3, no selective me...
Gespeichert in:
| Veröffentlicht in: | Trends in pharmacological sciences (Regular ed.) 1990-09, Vol.11 (9), p.358-362 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 362 |
|---|---|
| container_issue | 9 |
| container_start_page | 358 |
| container_title | Trends in pharmacological sciences (Regular ed.) |
| container_volume | 11 |
| creator | Mousli, Mouaiak Bueb, Jean-Luc Bronner, Christian Rouot, Bruno Landry, Yves |
| description | The neuropeptide substance P, the venom peptide mastoparan and the synthetic polyamine compound 48/80 activate rat peritoneal mast cells, leading to rapid histamine release by exocytosis. Although these effects are inhibited by pertussis toxin and involve a transient increase in IP3, no selective membrane receptors have been identified. However, it has recently been shown that these compounds activate G proteins in vitro.
Here Yves Landry and colleagues
discuss the proposal that direct activation of G protein is the physiological mechanism of action of substance P on rat peritoneal mast cells, this mechanism being mimicked by mastoparan and 48/80, and possibly by other cationic amphiphilic peptides such as kinins. These compounds might be of help m defining the interaction between membrane receptors and G proteins. |
| doi_str_mv | 10.1016/0165-6147(90)90179-C |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80111289</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>016561479090179C</els_id><sourcerecordid>80111289</sourcerecordid><originalsourceid>FETCH-LOGICAL-c439t-f2339886429c4779d592ec5c96e16d8c293b6de1216535d147d436a3cc82dd2a3</originalsourceid><addsrcrecordid>eNqFUctKAzEUDaLUWv0DhaxEF6N5zCsuBClahYIbXYc0uYORTjImMwX_3vRhlwpJbsg954ZzDkLnlNxQQsvbtIuspHl1Jci1ILQS2fQAjWld8YxXvDhE4z3kGJ3E-EkI4ZzRERoxylhR8jEaZrgLvgfrsNK9XaneeneHFQ6goet9yKwz0EE6XI9bbwD7ZgP1Djc-YL1hWI1V233YtJbp7mAIvkt8ayBi5QxegfMt_n06RUeNWkY429UJen96fJs-Z_PX2cv0YZ7pnIs-axjnoq7LnAmdV5UwhWCgCy1KoKWpNRN8URqgLMnkhUk6Tc5LxbWumTFM8Qm63M5NGr8GiL1sbdSwXCoHfoiyJpRSVot_gbSoOKtynoD5FqiDjzFAI7tgWxW-JSVyHYtcey7XnktB5CYWOU20i938YdGC2ZN2OaT-_bYPyY2VhSCjtuA0GJuC6KXx9u8PfgCGBZ1G</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15732743</pqid></control><display><type>article</type><title>G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Mousli, Mouaiak ; Bueb, Jean-Luc ; Bronner, Christian ; Rouot, Bruno ; Landry, Yves</creator><creatorcontrib>Mousli, Mouaiak ; Bueb, Jean-Luc ; Bronner, Christian ; Rouot, Bruno ; Landry, Yves</creatorcontrib><description>The neuropeptide substance P, the venom peptide mastoparan and the synthetic polyamine compound 48/80 activate rat peritoneal mast cells, leading to rapid histamine release by exocytosis. Although these effects are inhibited by pertussis toxin and involve a transient increase in IP3, no selective membrane receptors have been identified. However, it has recently been shown that these compounds activate G proteins in vitro.
Here Yves Landry and colleagues
discuss the proposal that direct activation of G protein is the physiological mechanism of action of substance P on rat peritoneal mast cells, this mechanism being mimicked by mastoparan and 48/80, and possibly by other cationic amphiphilic peptides such as kinins. These compounds might be of help m defining the interaction between membrane receptors and G proteins.</description><identifier>ISSN: 0165-6147</identifier><identifier>EISSN: 1873-3735</identifier><identifier>DOI: 10.1016/0165-6147(90)90179-C</identifier><identifier>PMID: 2122563</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Biotransformation ; GTP-Binding Proteins - metabolism ; Humans ; mast cells ; Molecular Sequence Data ; Neuropeptides - chemistry ; Neuropeptides - pharmacology ; Peptides ; substance P ; Wasp Venoms - chemistry ; Wasp Venoms - pharmacology</subject><ispartof>Trends in pharmacological sciences (Regular ed.), 1990-09, Vol.11 (9), p.358-362</ispartof><rights>1990</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-f2339886429c4779d592ec5c96e16d8c293b6de1216535d147d436a3cc82dd2a3</citedby><cites>FETCH-LOGICAL-c439t-f2339886429c4779d592ec5c96e16d8c293b6de1216535d147d436a3cc82dd2a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0165-6147(90)90179-C$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2122563$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mousli, Mouaiak</creatorcontrib><creatorcontrib>Bueb, Jean-Luc</creatorcontrib><creatorcontrib>Bronner, Christian</creatorcontrib><creatorcontrib>Rouot, Bruno</creatorcontrib><creatorcontrib>Landry, Yves</creatorcontrib><title>G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides</title><title>Trends in pharmacological sciences (Regular ed.)</title><addtitle>Trends Pharmacol Sci</addtitle><description>The neuropeptide substance P, the venom peptide mastoparan and the synthetic polyamine compound 48/80 activate rat peritoneal mast cells, leading to rapid histamine release by exocytosis. Although these effects are inhibited by pertussis toxin and involve a transient increase in IP3, no selective membrane receptors have been identified. However, it has recently been shown that these compounds activate G proteins in vitro.
Here Yves Landry and colleagues
discuss the proposal that direct activation of G protein is the physiological mechanism of action of substance P on rat peritoneal mast cells, this mechanism being mimicked by mastoparan and 48/80, and possibly by other cationic amphiphilic peptides such as kinins. These compounds might be of help m defining the interaction between membrane receptors and G proteins.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biotransformation</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Humans</subject><subject>mast cells</subject><subject>Molecular Sequence Data</subject><subject>Neuropeptides - chemistry</subject><subject>Neuropeptides - pharmacology</subject><subject>Peptides</subject><subject>substance P</subject><subject>Wasp Venoms - chemistry</subject><subject>Wasp Venoms - pharmacology</subject><issn>0165-6147</issn><issn>1873-3735</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUctKAzEUDaLUWv0DhaxEF6N5zCsuBClahYIbXYc0uYORTjImMwX_3vRhlwpJbsg954ZzDkLnlNxQQsvbtIuspHl1Jci1ILQS2fQAjWld8YxXvDhE4z3kGJ3E-EkI4ZzRERoxylhR8jEaZrgLvgfrsNK9XaneeneHFQ6goet9yKwz0EE6XI9bbwD7ZgP1Djc-YL1hWI1V233YtJbp7mAIvkt8ayBi5QxegfMt_n06RUeNWkY429UJen96fJs-Z_PX2cv0YZ7pnIs-axjnoq7LnAmdV5UwhWCgCy1KoKWpNRN8URqgLMnkhUk6Tc5LxbWumTFM8Qm63M5NGr8GiL1sbdSwXCoHfoiyJpRSVot_gbSoOKtynoD5FqiDjzFAI7tgWxW-JSVyHYtcey7XnktB5CYWOU20i938YdGC2ZN2OaT-_bYPyY2VhSCjtuA0GJuC6KXx9u8PfgCGBZ1G</recordid><startdate>19900901</startdate><enddate>19900901</enddate><creator>Mousli, Mouaiak</creator><creator>Bueb, Jean-Luc</creator><creator>Bronner, Christian</creator><creator>Rouot, Bruno</creator><creator>Landry, Yves</creator><general>Elsevier Ltd</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19900901</creationdate><title>G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides</title><author>Mousli, Mouaiak ; Bueb, Jean-Luc ; Bronner, Christian ; Rouot, Bruno ; Landry, Yves</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-f2339886429c4779d592ec5c96e16d8c293b6de1216535d147d436a3cc82dd2a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biotransformation</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>Humans</topic><topic>mast cells</topic><topic>Molecular Sequence Data</topic><topic>Neuropeptides - chemistry</topic><topic>Neuropeptides - pharmacology</topic><topic>Peptides</topic><topic>substance P</topic><topic>Wasp Venoms - chemistry</topic><topic>Wasp Venoms - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mousli, Mouaiak</creatorcontrib><creatorcontrib>Bueb, Jean-Luc</creatorcontrib><creatorcontrib>Bronner, Christian</creatorcontrib><creatorcontrib>Rouot, Bruno</creatorcontrib><creatorcontrib>Landry, Yves</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Trends in pharmacological sciences (Regular ed.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mousli, Mouaiak</au><au>Bueb, Jean-Luc</au><au>Bronner, Christian</au><au>Rouot, Bruno</au><au>Landry, Yves</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides</atitle><jtitle>Trends in pharmacological sciences (Regular ed.)</jtitle><addtitle>Trends Pharmacol Sci</addtitle><date>1990-09-01</date><risdate>1990</risdate><volume>11</volume><issue>9</issue><spage>358</spage><epage>362</epage><pages>358-362</pages><issn>0165-6147</issn><eissn>1873-3735</eissn><abstract>The neuropeptide substance P, the venom peptide mastoparan and the synthetic polyamine compound 48/80 activate rat peritoneal mast cells, leading to rapid histamine release by exocytosis. Although these effects are inhibited by pertussis toxin and involve a transient increase in IP3, no selective membrane receptors have been identified. However, it has recently been shown that these compounds activate G proteins in vitro.
Here Yves Landry and colleagues
discuss the proposal that direct activation of G protein is the physiological mechanism of action of substance P on rat peritoneal mast cells, this mechanism being mimicked by mastoparan and 48/80, and possibly by other cationic amphiphilic peptides such as kinins. These compounds might be of help m defining the interaction between membrane receptors and G proteins.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>2122563</pmid><doi>10.1016/0165-6147(90)90179-C</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0165-6147 |
| ispartof | Trends in pharmacological sciences (Regular ed.), 1990-09, Vol.11 (9), p.358-362 |
| issn | 0165-6147 1873-3735 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80111289 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amino Acid Sequence Animals Biotransformation GTP-Binding Proteins - metabolism Humans mast cells Molecular Sequence Data Neuropeptides - chemistry Neuropeptides - pharmacology Peptides substance P Wasp Venoms - chemistry Wasp Venoms - pharmacology |
| title | G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T15%3A58%3A16IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=G%20protein%20activation:%20a%20receptor-independent%20mode%20of%20action%20for%20cationic%20amphiphilic%20neuropeptides%20and%20venom%20peptides&rft.jtitle=Trends%20in%20pharmacological%20sciences%20(Regular%20ed.)&rft.au=Mousli,%20Mouaiak&rft.date=1990-09-01&rft.volume=11&rft.issue=9&rft.spage=358&rft.epage=362&rft.pages=358-362&rft.issn=0165-6147&rft.eissn=1873-3735&rft_id=info:doi/10.1016/0165-6147(90)90179-C&rft_dat=%3Cproquest_cross%3E80111289%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15732743&rft_id=info:pmid/2122563&rft_els_id=016561479090179C&rfr_iscdi=true |