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

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    Authors
    Bortell, Rita
    Rigby, Mark R.
    Stevens, Linda A.
    Moss, Joel
    Kanaitsuka, Toshihiro
    Mordes, John P.
    Greiner, Dale L.
    Rossini, Aldo A.
    UMass Chan Affiliations
    Department of Medicine, Division of Endocrinology and Metabolism
    Department of Medicine, Diabetes Division
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    1997-01-01
    Keywords
    ADP Ribose Transferases; Adenosine Diphosphate Ribose; Animals; Antigens, Differentiation, T-Lymphocyte; Catalysis; Cell Division; Cell Line; Histocompatibility Antigens; Linkage (Genetics); *Membrane Glycoproteins; Mice; NAD; Precipitin Tests; Rats; Recombinant Fusion Proteins; Spodoptera; T-Lymphocytes
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://www.jimmunol.org/content/156/11/4259
    Abstract
    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.
    Source
    Adv Exp Med Biol. 1997;419:169-73.
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32566
    PubMed ID
    9193650
    Related Resources
    Link to article in PubMed
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    Morningside GSBS Scholarly Publications

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