GSBS Student Publications
Title
Mouse RT6 locus 1 and rat RT6.2 are NAD+. Arginine ADP-ribosyltransferases with auto-ADP-ribosylation activity
GSBS Program
Biochemistry & Molecular Pharmacology
UMMS Affiliation
Graduate School of Biomedical Sciences; Department of Medicine, Diabetes Division; Department of Medicine, Division of Endocrinology and Metabolism
Date
1-1-1997
Document Type
Article
Medical Subject Headings
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
Disciplines
Life Sciences | Medicine and Health Sciences
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.
Rights and Permissions
Citation: Adv Exp Med Biol. 1997;419:169-73.
Related Resources
Journal Title
Advances in experimental medicine and biology
PubMed ID
9193650
Repository Citation
Bortell, Rita; Rigby, Mark R.; Stevens, Linda A.; Moss, Joel; Kanaitsuka, Toshihiro; Mordes, John P.; Greiner, Dale L.; and Rossini, Aldo A., "Mouse RT6 locus 1 and rat RT6.2 are NAD+. Arginine ADP-ribosyltransferases with auto-ADP-ribosylation activity" (1997). GSBS Student Publications. 113.
https://escholarship.umassmed.edu/gsbs_sp/113