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Molecular characterization of a glycosylphosphatidylinositol-linked ADP-
ribosyltransferase from lymphocytes
IJ Okazaki, HJ Kim, NG McElvaney, E Lesma and J Moss
Pulmonary-Critical Care Medicine Branch, National Heart, Lung, and Blood
Institute, National Institutes of Health, Bethesda, MD 20892- 1434, USA.
Mono ADP-ribosyltransferases catalyze the transfer of the ADP-ribose moiety
of nicotinamide adenine dinucleotide (NAD) to proteins. It was reported by
Wang et al (J Immunol 153:4048, 1994) that incubation of mouse cytotoxic T
lymphocytes (CTL) with NAD resulted in the ADP- ribosylation of membrane
proteins and inhibition of cell proliferation and cytotoxicity. Treatment
of CTL with phosphatidylinositol-specific phospholipase C (PI-PLC) before
incubation with NAD prevented the inhibitory effects of NAD on the cells,
consistent with the removal of a glycosylphosphatidylinositol
(GPI)-anchored ADP-ribosyltransferase on the lymphocyte surface. We have
identified and cloned a GPI-linked ADP- ribosyltransferase from Yac-1 mouse
T-cell lymphoma cells. The deduced amino acid sequence of the Yac-1
transferase was 70% and 41% identical to those of the rabbit skeletal
muscle and chicken heterophil, respectively. It contained three
noncontiguous sequences similar to those found in several of the bacterial
toxin and vertebrate ADP- ribosyltransferases. Based on crystallography of
the bacterial toxins, these regions are believed to form, in part, the
catalytic site consistent with a common mechanism for the ADP-ribose
transfer reaction. In rat mammary adenocarcinoma (NMU) cells transformed
with the Yac-1 transferase cDNA, transferase activity was present on the
cell surface and was released into the medium by treatment of cells with
PI-PLC. Thus, we have cloned a novel gene that has properties identical to
the transferase detected in CTL, and may be involved in the NAD-dependent
regulation of proliferation and cytotoxicity.
Volume 88,
Issue 3,
pp. 915-921,
08/01/1996
Copyright © 1996 by The American Society of Hematology
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S. Kahl, M. Nissen, R. Girisch, T. Duffy, E. H. Leiter, F. Haag, and F. Koch-Nolte
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A New Monoclonal Antibody Detects a Developmentally Regulated Mouse Ecto-ADP-Ribosyltransferase on T Cells: Subset Distribution, Inbred Strain Variation, and Modulation Upon T Cell Activation
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December 1, 1999;
163(11):
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B. Weng, W. C. Thompson, H.-J. Kim, R. L. Levine, and J. Moss
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Selective Expression of RT6 Superfamily in Human Bronchial Epithelial Cells
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September 1, 1999;
21(3):
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I. J. Okazaki and J. Moss
Glycosylphosphatidylinositol-anchored and Secretory Isoforms of Mono-ADP-ribosyltransferases
J. Biol. Chem.,
September 11, 1998;
273(37):
23617 - 23620.
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J. Biol. Chem.,
April 4, 1997;
272(14):
8918 - 8923.
[Abstract]
[Full Text]
[PDF]
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J. Moss, L. A. Stevens, E. Cavanaugh, I. J. Okazaki, R. Bortell, T. Kanaitsuka, J. P. Mordes, D. L. Greiner, and A. A. Rossini
Characterization of Mouse Rt6.1 NAD:Arginine ADP-ribosyltransferase
J. Biol. Chem.,
February 14, 1997;
272(7):
4342 - 4346.
[Abstract]
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