ADP-ribosylation of brain synaptosomal proteins correlates with adenylate cyclase activation
ADP-ribosylation of the adenylate cyclase G F regulatory subunit by cholera toxin is a major tool for the study of this enzyme. Investigation of the brain enzyme has been hampered up to now by the failure to demonstrate cholera toxin-dependent ADP-ribosylation of membrane-bound proteins. Synaptosome...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1982-11, Vol.109 (2), p.297-304 |
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| creator | Berthillier, Gisèle d'Alayer, Jacque Monneron, Ariane |
| description | ADP-ribosylation of the adenylate cyclase
G
F
regulatory subunit by cholera toxin is a major tool for the study of this enzyme. Investigation of the brain enzyme has been hampered up to now by the failure to demonstrate cholera toxin-dependent ADP-ribosylation of membrane-bound proteins. Synaptosomes prepared by flotation from fresh brains homogenized in the presence of protease inhibitors yielded membranes of which several proteins could be ADP-ribosylated by the toxin. The same membranes subjected to mild proteolysis could not be ADP-ribosylated. Adenylate cyclase activation and ADP-ribosylation were simultaneous processes. The major labeled species was of 47,000 M
r. It was solubilized by Lubrol-PX, together with other labeled polypeptides. As analyzed on sucrose gradients, the 47,000 M
r protein was found both in the 3S region, and in the adenylate cyclase containing fraction (9.1S). |
| doi_str_mv | 10.1016/0006-291X(82)91720-X |
| format | Article |
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G
F
regulatory subunit by cholera toxin is a major tool for the study of this enzyme. Investigation of the brain enzyme has been hampered up to now by the failure to demonstrate cholera toxin-dependent ADP-ribosylation of membrane-bound proteins. Synaptosomes prepared by flotation from fresh brains homogenized in the presence of protease inhibitors yielded membranes of which several proteins could be ADP-ribosylated by the toxin. The same membranes subjected to mild proteolysis could not be ADP-ribosylated. Adenylate cyclase activation and ADP-ribosylation were simultaneous processes. The major labeled species was of 47,000 M
r. It was solubilized by Lubrol-PX, together with other labeled polypeptides. As analyzed on sucrose gradients, the 47,000 M
r protein was found both in the 3S region, and in the adenylate cyclase containing fraction (9.1S).</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(82)91720-X</identifier><identifier>PMID: 6817756</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Diphosphate Ribose - metabolism ; Adenosine Triphosphate - metabolism ; adenylate cyclase ; Adenylyl Cyclases - metabolism ; ADP-ribosylation ; Animals ; brain ; Brain - metabolism ; Cholera Toxin - pharmacology ; Egtazic Acid - pharmacology ; Enzyme Activation ; Guanosine Triphosphate - metabolism ; Membrane Proteins - metabolism ; Molecular Weight ; NAD - metabolism ; Nerve Tissue Proteins - metabolism ; Nucleoside Diphosphate Sugars - metabolism ; Rats ; synaptosomes ; Synaptosomes - metabolism</subject><ispartof>Biochemical and biophysical research communications, 1982-11, Vol.109 (2), p.297-304</ispartof><rights>1982</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-f517d361150207bf6b998831c96d8981306744353df9e989d8ad486cc9ccbc8e3</citedby><cites>FETCH-LOGICAL-c388t-f517d361150207bf6b998831c96d8981306744353df9e989d8ad486cc9ccbc8e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X8291720X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6817756$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Berthillier, Gisèle</creatorcontrib><creatorcontrib>d'Alayer, Jacque</creatorcontrib><creatorcontrib>Monneron, Ariane</creatorcontrib><title>ADP-ribosylation of brain synaptosomal proteins correlates with adenylate cyclase activation</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>ADP-ribosylation of the adenylate cyclase
G
F
regulatory subunit by cholera toxin is a major tool for the study of this enzyme. Investigation of the brain enzyme has been hampered up to now by the failure to demonstrate cholera toxin-dependent ADP-ribosylation of membrane-bound proteins. Synaptosomes prepared by flotation from fresh brains homogenized in the presence of protease inhibitors yielded membranes of which several proteins could be ADP-ribosylated by the toxin. The same membranes subjected to mild proteolysis could not be ADP-ribosylated. Adenylate cyclase activation and ADP-ribosylation were simultaneous processes. The major labeled species was of 47,000 M
r. It was solubilized by Lubrol-PX, together with other labeled polypeptides. As analyzed on sucrose gradients, the 47,000 M
r protein was found both in the 3S region, and in the adenylate cyclase containing fraction (9.1S).</description><subject>Adenosine Diphosphate Ribose - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>adenylate cyclase</subject><subject>Adenylyl Cyclases - metabolism</subject><subject>ADP-ribosylation</subject><subject>Animals</subject><subject>brain</subject><subject>Brain - metabolism</subject><subject>Cholera Toxin - pharmacology</subject><subject>Egtazic Acid - pharmacology</subject><subject>Enzyme Activation</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Weight</subject><subject>NAD - metabolism</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Nucleoside Diphosphate Sugars - metabolism</subject><subject>Rats</subject><subject>synaptosomes</subject><subject>Synaptosomes - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKLDEQhoMonvHyBh7I6qCL1qq-pJPNAfEOgi4UZiGEdFKNkZ7OmPQo8_b2OINLV7X4L1X1MXaEcIqA4gwARJYrnB7L_ERhnUM23WITBAVZjlBus8mP5Q_bS-kNALEUapftCol1XYkJezm_fMyib0Jadmbwoeeh5U00vudp2Zv5EFKYmY7PYxjI94nbECONVkr80w-v3DjqV1Hidmk7k4gbO_iP764DttOaLtHhZu6z5-urp4vb7P7h5u7i_D6zhZRD1lZYu0IgVpBD3bSiUUrKAq0STiqJBYi6LIuqcK0iJZWTxpVSWKusbaykYp_9W_eOV74vKA165pOlrjM9hUXSWFUlgoDRWK6NNoaUIrV6Hv3MxKVG0CuoekVMr4hpmetvqHo6xv5u-hfNjNxPaENx1P-vdRqf_PAUdbKeekvOR7KDdsH_vuAL80OH5Q</recordid><startdate>19821130</startdate><enddate>19821130</enddate><creator>Berthillier, Gisèle</creator><creator>d'Alayer, Jacque</creator><creator>Monneron, Ariane</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>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope></search><sort><creationdate>19821130</creationdate><title>ADP-ribosylation of brain synaptosomal proteins correlates with adenylate cyclase activation</title><author>Berthillier, Gisèle ; d'Alayer, Jacque ; Monneron, Ariane</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-f517d361150207bf6b998831c96d8981306744353df9e989d8ad486cc9ccbc8e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Adenosine Diphosphate Ribose - metabolism</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>adenylate cyclase</topic><topic>Adenylyl Cyclases - metabolism</topic><topic>ADP-ribosylation</topic><topic>Animals</topic><topic>brain</topic><topic>Brain - metabolism</topic><topic>Cholera Toxin - pharmacology</topic><topic>Egtazic Acid - pharmacology</topic><topic>Enzyme Activation</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Weight</topic><topic>NAD - metabolism</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Nucleoside Diphosphate Sugars - metabolism</topic><topic>Rats</topic><topic>synaptosomes</topic><topic>Synaptosomes - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Berthillier, Gisèle</creatorcontrib><creatorcontrib>d'Alayer, Jacque</creatorcontrib><creatorcontrib>Monneron, Ariane</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Berthillier, Gisèle</au><au>d'Alayer, Jacque</au><au>Monneron, Ariane</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ADP-ribosylation of brain synaptosomal proteins correlates with adenylate cyclase activation</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1982-11-30</date><risdate>1982</risdate><volume>109</volume><issue>2</issue><spage>297</spage><epage>304</epage><pages>297-304</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>ADP-ribosylation of the adenylate cyclase
G
F
regulatory subunit by cholera toxin is a major tool for the study of this enzyme. Investigation of the brain enzyme has been hampered up to now by the failure to demonstrate cholera toxin-dependent ADP-ribosylation of membrane-bound proteins. Synaptosomes prepared by flotation from fresh brains homogenized in the presence of protease inhibitors yielded membranes of which several proteins could be ADP-ribosylated by the toxin. The same membranes subjected to mild proteolysis could not be ADP-ribosylated. Adenylate cyclase activation and ADP-ribosylation were simultaneous processes. The major labeled species was of 47,000 M
r. It was solubilized by Lubrol-PX, together with other labeled polypeptides. As analyzed on sucrose gradients, the 47,000 M
r protein was found both in the 3S region, and in the adenylate cyclase containing fraction (9.1S).</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6817756</pmid><doi>10.1016/0006-291X(82)91720-X</doi><tpages>8</tpages></addata></record> |
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| language | eng |
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| subjects | Adenosine Diphosphate Ribose - metabolism Adenosine Triphosphate - metabolism adenylate cyclase Adenylyl Cyclases - metabolism ADP-ribosylation Animals brain Brain - metabolism Cholera Toxin - pharmacology Egtazic Acid - pharmacology Enzyme Activation Guanosine Triphosphate - metabolism Membrane Proteins - metabolism Molecular Weight NAD - metabolism Nerve Tissue Proteins - metabolism Nucleoside Diphosphate Sugars - metabolism Rats synaptosomes Synaptosomes - metabolism |
| title | ADP-ribosylation of brain synaptosomal proteins correlates with adenylate cyclase activation |
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