Regulation of cytotoxic T cell functions by a GPI-anchored ecto-ADP-ribosyltransferase

Advances in Experimental Medicine and Biology
J WangG Dennert

Abstract

Protein mono-(ADP-ribosyl)transferases (ADPRTs) catalyze transfer of the ADP-ribose moiety from nicotinamide adenine dinucleotide (NAD) to specific amino acids. We recently described presence of an enzyme with this activity on cytotoxic T cells (CTL). Incubation of CTL with micromolar concentrations of NAD causes inhibition of cell proliferation and cytolytic activity. ADPRT can be released by bacterial phosphoinosital specific phospholipase C, indicating that it is a glycosylphosphatidylinositol (GPI) anchored exo-enzyme. Enzymatic release of ADPRT results in inability of NAD to modulate CTL function. Expression of ADPRT was found to be regulated, in quiescent CTL ADPRT is expressed at significant levels, however, upon TCR crosslinking it is rapidly released by an anchor hydrolyzing mechanism. This results in relative insensitivity to the inhibitory action of NAD. The question how ADPRT regulates T cell functions was investigated by incubating CTL with radioactively labeled NAD which causes modification of several proteins, pointing to potential candidates in these regulatory processes. We found that the protein tyrosine kinase p56lck but not p59fyn exists in a digitonin resistant complex with a 40 kD protein, which in its ADP...Continue Reading

Citations

Feb 3, 2006·Journal of Cellular Biochemistry·Xuexiu ZhengRita Bortell
Oct 18, 2000·The Journal of Immunology : Official Journal of the American Association of Immunologists·S KahlF Koch-Nolte
Aug 8, 2001·The Journal of Immunology : Official Journal of the American Association of Immunologists·R BortellA A Rossini

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