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dc.contributor.authorRigby, Mark R.
dc.contributor.authorBortell, Rita
dc.contributor.authorStevens, Linda A.
dc.contributor.authorMoss, Joel
dc.contributor.authorKanaitsuka, Toshihiro
dc.contributor.authorShigeta, Hirofumi
dc.contributor.authorMordes, John P.
dc.contributor.authorGreiner, Dale L.
dc.contributor.authorRossini, Aldo A.
dc.date2022-08-11T08:08:47.000
dc.date.accessioned2022-08-23T16:08:33Z
dc.date.available2022-08-23T16:08:33Z
dc.date.issued1996-06-01
dc.date.submitted2008-12-08
dc.identifier.citation<p>J Immunol. 1996 Jun 1;156(11):4259-65.</p>
dc.identifier.issn0022-1767 (Print)
dc.identifier.pmid8666796
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32477
dc.description.abstractRT6 is a glycosylphosphatidylinositol-linked protein found on the surface of mature rat T lymphocytes. Cells that express RT6 have an immunoregulatory function and modulate the expression of autoimmune diabetes mellitus in the BioBreeding rat. A homologue of the rat RT6 gene, designated Rt6, has been identified in the mouse, but expression of mouse Rt6 protein has not been documented. Rat RT6 is known to be a nicotinamide adenine dinucleotide (NAD+) glycohydrolase. We now report that rat RT6.2 and recombinant mouse Rt6 locus 1 proteins possess auto-ADP ribosylation activity. In addition, mouse Rt6 but not rat RT6, catalyzes the ADP ribosylation of exogenous acceptors such as histones. The ADP-ribosyl-protein bonds in auto-ADP-ribosylated rat RT6.2, auto-ADP-ribosylated mouse Rt6, and ADP-ribosylhistone synthesized by Rt6 were stable to HgCl2 and HCl, but labile to NH2OH, consistent with ADP ribosylarginine linkages. To determine if these enzymatic activities could affect the function of rat T cells, the effect of substrate availability on lymphocyte proliferation was examined. An inverse correlation was observed between NAD+ concentration in the medium and the ability of rat T cells to respond to anti-CD3, ConA, and PMA plus ionomycin. The data suggest that lymphocyte surface ADP ribosyltransferases could be involved in signaling and immunoregulatory processes.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=8666796&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttp://www.jimmunol.org/cgi/content/abstract/156/11/4259
dc.subjectADP Ribose Transferases; Adenosine Diphosphate Ribose; Animals; Antigens, Differentiation, T-Lymphocyte; Base Sequence; Cross-Linking Reagents; DNA Primers; Female; Histocompatibility Antigens; Lymphocyte Activation; Male; *Membrane Glycoproteins; Mice; Molecular Sequence Data; NAD; Rats; Rats, Inbred BB; Rats, Inbred WF; Recombinant Proteins; T-Lymphocytes
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleRat RT6.2 and mouse Rt6 locus 1 are NAD+: arginine ADP ribosyltransferases with auto-ADP ribosylation activity
dc.typeJournal Article
dc.source.journaltitleJournal of immunology (Baltimore, Md. : 1950)
dc.source.volume156
dc.source.issue11
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1046
dc.identifier.contextkey677766
html.description.abstract<p>RT6 is a glycosylphosphatidylinositol-linked protein found on the surface of mature rat T lymphocytes. Cells that express RT6 have an immunoregulatory function and modulate the expression of autoimmune diabetes mellitus in the BioBreeding rat. A homologue of the rat RT6 gene, designated Rt6, has been identified in the mouse, but expression of mouse Rt6 protein has not been documented. Rat RT6 is known to be a nicotinamide adenine dinucleotide (NAD+) glycohydrolase. We now report that rat RT6.2 and recombinant mouse Rt6 locus 1 proteins possess auto-ADP ribosylation activity. In addition, mouse Rt6 but not rat RT6, catalyzes the ADP ribosylation of exogenous acceptors such as histones. The ADP-ribosyl-protein bonds in auto-ADP-ribosylated rat RT6.2, auto-ADP-ribosylated mouse Rt6, and ADP-ribosylhistone synthesized by Rt6 were stable to HgCl2 and HCl, but labile to NH2OH, consistent with ADP ribosylarginine linkages. To determine if these enzymatic activities could affect the function of rat T cells, the effect of substrate availability on lymphocyte proliferation was examined. An inverse correlation was observed between NAD+ concentration in the medium and the ability of rat T cells to respond to anti-CD3, ConA, and PMA plus ionomycin. The data suggest that lymphocyte surface ADP ribosyltransferases could be involved in signaling and immunoregulatory processes.</p>
dc.identifier.submissionpathgsbs_sp/1046
dc.contributor.departmentDepartment of Medicine, Diabetes Division
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages4259-65


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