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Mouse RT6 locus 1 and rat RT6.2 are NAD+. Arginine ADP-ribosyltransferases with auto-ADP-ribosylation activity

dc.contributor.authorBortell, Rita
dc.contributor.authorRigby, Mark R.
dc.contributor.authorStevens, Linda A.
dc.contributor.authorMoss, Joel
dc.contributor.authorKanaitsuka, Toshihiro
dc.contributor.authorMordes, John P.
dc.contributor.authorGreiner, Dale L.
dc.contributor.authorRossini, Aldo A.
dc.date2022-08-11T08:08:48.000
dc.date.accessioned2022-08-23T16:08:55Z
dc.date.available2022-08-23T16:08:55Z
dc.date.issued1997-01-01
dc.date.submitted2008-08-05
dc.identifier.citationAdv Exp Med Biol. 1997;419:169-73.
dc.identifier.issn0065-2598 (Print)
dc.identifier.pmid9193650
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32566
dc.description.abstractWe report that rat RT6.2 and recombinant mouse Rt6 locus 1 proteins possess auto-ADP-ribosyltransferase activity and that Rt6, but not RT6, catalyzes the ADP-ribosylation of exogenous histones. Based on NH2OH sensitivity, it appeared that the ADP-ribose was attached to arginine residues on proteins. We also observed that the NAD+ concentration in culture medium correlates inversely with the proliferation of rat RT6+ T cells. The data suggest that lymphocyte surface ADP-ribosyltransferases could be involved in signaling and immunoregulatory processes.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9193650&dopt=Abstract ">Link to article in PubMed</a>
dc.relation.urlhttp://www.jimmunol.org/content/156/11/4259
dc.titleMouse RT6 locus 1 and rat RT6.2 are NAD+. Arginine ADP-ribosyltransferases with auto-ADP-ribosylation activity
dc.typeJournal Article
dc.source.journaltitleAdvances in experimental medicine and biology
dc.source.volume419
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/113
dc.identifier.contextkey566367
html.description.abstract<p>We report that rat RT6.2 and recombinant mouse Rt6 locus 1 proteins possess auto-ADP-ribosyltransferase activity and that Rt6, but not RT6, catalyzes the ADP-ribosylation of exogenous histones. Based on NH2OH sensitivity, it appeared that the ADP-ribose was attached to arginine residues on proteins. We also observed that the NAD+ concentration in culture medium correlates inversely with the proliferation of rat RT6+ T cells. The data suggest that lymphocyte surface ADP-ribosyltransferases could be involved in signaling and immunoregulatory processes.</p>
dc.identifier.submissionpathgsbs_sp/113
dc.contributor.departmentDepartment of Medicine, Division of Endocrinology and Metabolism
dc.contributor.departmentDepartment of Medicine, Diabetes Division
dc.contributor.departmentMorningside Graduate School of Biomedical Sciences
dc.source.pages169-73


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