DOI: 10.4049/jimmunol.174.6.3298. CD38 Controls ADP-Ribosyltransferase-2-Catalyzed ADP-Ribosylation of T Cell Surface Proteins

CD38 Controls ADP-Ribosyltransferase-2-Catalyzed ADP-Ribosylation of T Cell Surface Proteins

10.4049/jimmunol.174.6.3298

Crossref journal-article

Oxford University Press (OUP)

The Journal of Immunology (286)

Abstract

AbstractADP-ribosyltransferase-2 (ART2), a GPI-anchored, toxin-related ADP-ribosylating ectoenzyme, is prominently expressed by murine T cells but not by B cells. Upon exposure of T cells to NAD, the substrate for ADP-ribosylation, ART2 catalyzes ADP-ribosylation of the P2X7 purinoceptor and other functionally important cell surface proteins. This in turn activates P2X7 and induces exposure of phosphatidylserine and shedding of CD62L. CD38, a potent ecto-NAD-glycohydrolase, is strongly expressed by most B cells but only weakly by T cells. Following incubation with NAD, CD38-deficient splenocytes exhibited lower NAD-glycohydrolase activity and stronger ADP-ribosylation of cell surface proteins than their wild-type counterparts. Depletion of CD38high cells from wild-type splenocytes resulted in stronger ADP-ribosylation on the remaining cells. Similarly, treatment of total splenocytes with the CD38 inhibitor nicotinamide 2′-deoxy-2′-fluoroarabinoside adenine dinucleotide increased the level of cell surface ADP-ribosylation. Furthermore, the majority of T cells isolated from CD38-deficient mice “spontaneously” exposed phosphatidylserine and lacked CD62L, most likely reflecting previous encounter with ecto-NAD. Our findings support the notion that ecto-NAD functions as a signaling molecule following its release from cells by lytic or nonlytic mechanisms. ART2 can sense and translate the local concentration of ecto-NAD into corresponding levels of ADP-ribosylated cell surface proteins, whereas CD38 controls the level of cell surface protein ADP-ribosylation by limiting the substrate availability for ART2.

Bibliography

Krebs, C., Adriouch, S., Braasch, F., Koestner, W., Leiter, E. H., Seman, M., Lund, F. E., Oppenheimer, N., Haag, F., & Koch-Nolte, F. (2005). CD38 Controls ADP-Ribosyltransferase-2-Catalyzed ADP-Ribosylation of T Cell Surface Proteins. The Journal of Immunology, 174(6), 3298â3305.

Authors 10

Christian Krebs (first)
Sahil Adriouch (additional)
Fenja Braasch (additional)
Wolfgang Koestner (additional)
Edward H. Leiter (additional)
Michel Seman (additional)
Frances E. Lund (additional)
Norman Oppenheimer (additional)
Friedrich Haag (additional)
Friedrich Koch-Nolte (additional)

References 47 Referenced 75

Dates

Type	When
Created	11 years, 4 months ago (April 21, 2014, 10:13 p.m.)
Deposited	7 months, 4 weeks ago (Jan. 2, 2025, 1:03 p.m.)
Indexed	3 months, 2 weeks ago (May 16, 2025, 1:25 p.m.)
Issued	20 years, 5 months ago (March 15, 2005)
Published	20 years, 5 months ago (March 15, 2005)
Published Print	20 years, 5 months ago (March 15, 2005)

Funders 0

None

BibTeX

@article{Krebs_2005, title={CD38 Controls ADP-Ribosyltransferase-2-Catalyzed ADP-Ribosylation of T Cell Surface Proteins}, volume={174}, ISSN={1550-6606}, url={http://dx.doi.org/10.4049/jimmunol.174.6.3298}, DOI={10.4049/jimmunol.174.6.3298}, number={6}, journal={The Journal of Immunology}, publisher={Oxford University Press (OUP)}, author={Krebs, Christian and Adriouch, Sahil and Braasch, Fenja and Koestner, Wolfgang and Leiter, Edward H. and Seman, Michel and Lund, Frances E. and Oppenheimer, Norman and Haag, Friedrich and Koch-Nolte, Friedrich}, year={2005}, month=mar, pages={3298–3305} }

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  "abstract": "<jats:title>Abstract</jats:title><jats:p>ADP-ribosyltransferase-2 (ART2), a GPI-anchored, toxin-related ADP-ribosylating ectoenzyme, is prominently expressed by murine T cells but not by B cells. Upon exposure of T cells to NAD, the substrate for ADP-ribosylation, ART2 catalyzes ADP-ribosylation of the P2X7 purinoceptor and other functionally important cell surface proteins. This in turn activates P2X7 and induces exposure of phosphatidylserine and shedding of CD62L. CD38, a potent ecto-NAD-glycohydrolase, is strongly expressed by most B cells but only weakly by T cells. Following incubation with NAD, CD38-deficient splenocytes exhibited lower NAD-glycohydrolase activity and stronger ADP-ribosylation of cell surface proteins than their wild-type counterparts. Depletion of CD38high cells from wild-type splenocytes resulted in stronger ADP-ribosylation on the remaining cells. Similarly, treatment of total splenocytes with the CD38 inhibitor nicotinamide 2\u2032-deoxy-2\u2032-fluoroarabinoside adenine dinucleotide increased the level of cell surface ADP-ribosylation. Furthermore, the majority of T cells isolated from CD38-deficient mice \u201cspontaneously\u201d exposed phosphatidylserine and lacked CD62L, most likely reflecting previous encounter with ecto-NAD. Our findings support the notion that ecto-NAD functions as a signaling molecule following its release from cells by lytic or nonlytic mechanisms. ART2 can sense and translate the local concentration of ecto-NAD into corresponding levels of ADP-ribosylated cell surface proteins, whereas CD38 controls the level of cell surface protein ADP-ribosylation by limiting the substrate availability for ART2.</jats:p>",
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