CD38 controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins

Journal of Immunology

Volumn 174, Issue 6, 2005, Pages 3298-3305

  Krebs, Christian ^a,b   Adriouch, Sahil ^a,c   Braasch, Fenja ^a   Koestner, Wolfgang ^a   Leiter, Edward H ^b   Seman, Michel ^c   Lund, Frances E ^d   Oppenheimer, Norman ^e   Haag, Friedrich ^a   Koch Nolte, Friedrich ^a  

^a UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

^b JACKSON LABORATORY   (United States)

^c UNIVERSITÉ PARIS DESCARTES   (France)

^d TRUDEAU INSTITUTE   (United States)

^e UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD38 ANTIGEN; CELL SURFACE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PADGEM PROTEIN; PHOSPHATIDYLSERINE; PURINE P2X7 RECEPTOR;

ADENOSINE DIPHOSPHATE RIBOSYLATION; ANIMAL CELL; ANTIGEN EXPRESSION; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; MOUSE; NONHUMAN; PRIORITY JOURNAL; SPLEEN CELL; T LYMPHOCYTE ACTIVATION;

EID: 20144379146     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.174.6.3298     Document Type: Article

References (47)

1. Corda, D., and M. Di Girolamo. 2003. Functional aspects of protein mono-ADP-ribosylation. EMBO J. 22:1953.
2. Seman, M., S. Adriouch, F. Haag, and F. Koch-Nolte. 2004. Ecto-ADP-ribosyltransferases (ARTs): emerging actors in cell communication and signaling. Curr. Med. Chem. 11:857.
3. Aktories, K., and I. Just. 2000. Bacterial Protein Toxins. Springer, Berlin.
4. Okazaki, I. J., H. J. Kim, N. G. McElvaney, E. Lesma, and J. Moss. 1996. Molecular characterization of a glycosylphosphatidylinositol-linked ADP-ribosyltransferase from lymphocytes. Blood 88:915.
5. Glowacki, G., R. Braren, K. Firner, M. Nissen, M. Kuhl, P. Reche, F. Bazan, M. Cetkovic-Cvrlje, E. Leiter, F. Haag, and F. Koch-Nolte. 2002. The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse. Protein Sci. 11:1657.
6. Okamoto, S., O. Azhipa, Y. Yu, E. Russo, and G. Dennert. 1998. Expression of ADP-ribosyltransferase on normal T lymphocytes and effects of nicotinamide adenine dinucleotide on their function. J. Immunol. 160:4190.
7. Seman, M., S. Adriouch, F. Scheuplein, C. Krebs, D. Freese, G. Glowacki, P. Deterre, F. Haag, and F. Koch-Nolte. 2003. NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor. Immunity 19:571.
8. Adriouch, S., W. Ohlrogge, F. Haag, F. Koch-Nolte, and M. Seman. 2001. Rapid induction of naive T cell apoptosis by ecto-nicotinamide adenine dinucleotide: requirement for mono(ADP-ribosyl)transferase 2 and a downstream effector. J. Immunol. 167:196.
9. Liu, Z. X., O. Azhipa, S. Okamoto, S. Govindarajan, and G. Dennert. 2001. Extracellular nicotinamide adenine dinucleotide induces T cell apoptosis in vivo and in vitro. J. Immunol. 167:4942.
10. Bortell, R., J. Moss, R. C. McKenna, M. R. Rigby, D. Niedzwiecki, L. A. Stevens, W. A. Patton, J. P. Mordes, D. L. Greiner, and A. A. Rossini. 2001. Nicotinamide adenine dinucleotide (NAD) and its metabolites inhibit T lymphocyte proliferation: role of cell surface NAD glycohydrolase and pyrophosphatase activities. J. Immunol. 167:2049.
11. Di Virgilio, F., P. Chiozzi, D. Ferrari, S. Falzoni, J. M. Sanz, A. Morelli, M. Torboli, G. Bolognesi, and O. R. Baricordi. 2001. Nucleotide receptors: an emerging family of regulatory molecules in blood cells. Blood 97:587.
12. North, R. A. 2002. Molecular physiology of P2X receptors. Physiol. Rev. 82:1013.
13. Surprenant, A., F. Rassendren, E. Kawashima, R. A. North, and G. Buell. 1996. The cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7). Science 272:735.
14. Zanovello, P., V. Bronte, A. Rosato, P. Pizzo, and F. Di Virgilio. 1990. Responses of mouse lymphocytes to extracellular ATP. II. Extracellular ATP causes cell type-dependent lysis and DNA fragmentation. J. Immunol. 145:1545.
15. Jamieson, G. P., M. B. Snook, P. J. Thurlow, and J. S. Wiley. 1996. Extracellular ATP causes of loss of L-selectin from human lymphocytes via occupancy of P2Z purinocepters. J. Cell. Physiol. 166:637.
16. Ohlrogge, W., F. Haag, J. Lohler, M. Seman, D. R. Littman, N. Killeen, and F. Koch-Nolte. 2002. Generation and characterization of ecto-ADP- ribosyltransferase ART2.1/ART2.2-deficient mice. Mol. Cell. Biol. 22:7535.
17. Adriouch, S., C. Dox, V. Welge, M. Seman, F. Koch-Nolte, and F. Haag. 2002. Cutting edge: a natural P451L mutation in the cytoplasmic domain impairs the function of the mouse P2X7 receptor. J. Immunol. 169:4108.
18. Ferrero, E., and F. Malavasi. 1999. The metamorphosis of a molecule: from soluble enzyme to the leukocyte receptor CD38. J. Leukocyte Biol. 65:151.
19. Schuber, F., and F. E. Lund. 2004. Structure and enzymology of ADP-ribosyl cyclases: conserved enzymes that produce multiple calcium mobilizing metabolites. Curr. Mol. Med. 4:249.
20. Cockayne, D. A., T. Muchamuel, J. C. Grimaldi, H. Muller-Steffner, T. D. Randall, F. E. Lund, R. Murray, F. Schuber, and M. C. Howard. 1998. Mice deficient for the ecto-nicotinamide adenine dinucleotide glycohydrolase CD38 exhibit altered humoral immune responses. Blood 92:1324.
21. Partida-Sanchez, S., D. A. Cockayne, S. Monard, E. L. Jacobson, N. Oppenheimer, B. Garvy, K. Kusser, S. Goodrich, M. Howard, A. Harmsen, et al. 2001. Cyclic ADP-ribose production by CD38 regulates intracellular calcium release, extracellular calcium influx and chemotaxis in neutrophils and is required for bacterial clearance in vivo. Nat. Med. 7:1209.
22. Partida-Sanchez, S., S. Goodrich, K. Kusser, N. Oppenheimer, T. D. Randall, and F. E. Lund. 2004. Regulation of dendritic cell trafficking by the ADP-ribosyl cyclase CD38: impact on the development of humoral immunity. Immunity 20:279.
23. Ziegler, M. 2000. New functions of a long-known molecule: emerging roles of NAD in cellular signaling. Eur. J. Biochem. 267:1550.
24. la Sala, A., D. Ferrari, F. Di Virgilio, M. Idzko, J. Norgauer, and G. Girolomoni. 2003. Alerting and tuning the immune response by extracellular nucleotides. J. Leukocyte Biol. 73:339.
25. Berger, F., M. H. Ramirez-Hernandez, and M. Ziegler. 2004. The new life of a centenarian: signalling functions of NAD(P). Trends Biochem. Sci. 29:111.
26. + fluxes in intact cells. FASEB J. 15:10.
27. Lazarowski, E. R., R. C. Boucher, and T. K. Harden. 2003. Mechanisms of release of nucleotides and integration of their action as P2X- and P2Y-receptor activating molecules. Mol. Pharmacol. 64:785.
28. Zimmermann, H., and N. Braun. 1999. Ecto-nucleotidases: molecular structures, catalytic properties, and functional roles in the nervous system. Prog. Brain Res. 120:371.
29. Sneddon, P., T. D. Westfall, L. D. Todorov, S. Mihaylova-Todorova, D. P. Westfall, and C. Kennedy. 1999. Modulation of purinergic neurotransmission. Prog. Brain Res. 120:11.
30. Krebs, C., W. Koestner, M. Nissen, V. Welge, I. Parusel, F. Malavasi, E. H. Leiter, R. M. Santella, F. Haag, and F. Koch-Nolte. 2003. Flow cytometric and immunoblot assays for cell surface ADP-ribosylation using a monoclonal antibody specific for ethenoadenosine. Anal. Biochem. 314:108.
31. + glycohydrolase by arabino analogues of β-NAD. J. Biol. Chem. 267:9606.
32. Koch-Nolte, F., T. Duffy, M. Nissen, S. Kahl, N. Killeen, V. Ablamunits, F. Haag, and E. H. Leiter. 1999. 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. J. Immunol. 163:6014.
33. Kahl, S., M. Nissen, R. Girisch, T. Duffy, E. H. Leiter, F. Haag, and F. Koch-Nolte. 2000. Metalloprotease-mediated shedding of enzymatically active mouse ecto-ADP-ribosyltransferase ART2.2 upon T cell activation. J. Immunol. 165:4463.
34. Moreno-Garcia, M. E., S. Partida-Sanchez, J. Primack, A. Sumoza-Toledo, H. Muller-Steffner, F. Schuber, N. Oppenheimer, F. E. Lund, and L. Santos-Argumedo. 2004. CD38 is expressed as noncovalently associated homodimers on the surface of murine B lymphocytes. Eur. J. Biochem. 271:1025.
35. Schweitzer, K., G. W. Mayr, and A. H. Guse. 2001. Assay for ADP-ribosyl cyclase by reverse-phase high-performance liquid chromatography. Anal. Biochem. 299:218.
36. Koch-Nolte, F., D. Petersen, S. Balasubramanian, F. Haag, D. Kahlke, T. Willer, R. Kastelein, F. Bazan, and H. G. Thiele. 1996. Mouse T cell membrane proteins Rt6-1 and Rt6-2 are arginine/protein mono(ADPribosyl)transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins. J. Biol. Chem. 271:7686.
37. Deterre, P., L. Gelman, H. Gary-Gouy, C. Arrieumerlou, V. Berthelier, J. M. Tixier, S. Ktorza, J. Coding, C. Schmitt, and G. Bismuth. 1996. Coordinated regulation in human T cells of nucleotide-hydrolyzing ecto-enzymatic activities, including CD38 and PC-1: possible role in the recycling of nicotinamide adenine dinucleotide metabolites. J. Immunol. 157:1381.
38. Goding, J. W., and M. C. Howard. 1998. Ecto-enzymes of lymphoid cells. Immunol. Rev. 161:5.
39. Partida-Sanchez, S., P. Iribarren, M. E. Moreno-Garcia, J. L. Gao, P. M. Murphy, N. Oppenheimer, J. M. Wang, and F. E. Lund. 2004. Chemotaxis and calcium responses of phagocytes to formyl peptide receptor ligands is differentially regulated by cyclic ADP ribose. J. Immunol. 172:1896.
40. Mitsui-Saito, M., I. Kato, S. Takasawa, H. Okamoto, and T. Yanagisawa. 2003. CD38 gene disruption inhibits the contraction induced by α-adrenoceptor stimulation in mouse aorta. J. Vet. Med. Sci. 65:1325.
41. i, and insulin secretion. J. Biol. Chem. 274:1869.
42. 2+ signaling using CD38 knockout mice. J. Biol. Chem. 276:649.
43. Jacobson, E. L., and M. K. Jacobson. 1997. Tissue NAD as a biochemical measure of niacin status in humans. Methods Enzymol. 280:221.
44. Reidl, J., S. Schlor, A. Kraiss, J. Schmidt-Brauns, G. Kemmer, and E. Soleva. 2000. NADP and NAD utilization in Haemophilus influence. Mol. Microbiol. 35:1573.
45. King, C., A. Ilic, K. Koelsch, and N. Sarvetnick. 2004. Homeostatic expansion of T cells during immune insufficiency generates autoimmunity. Cell 117:265.
46. Takahashi, J., Y. Kagaya, I. Kato, J. Ohta, S. Isoyama, M. Miura, Y. Sugai, M. Hirose, Y. Wakayama, M. Ninomiya, et al. 2003. Deficit of CD38/cyclic ADP-ribose is differentially compensated in hearts by gender. Biochem. Biophys. Res. Commun. 312:434.
47. Zielinska, W., H. Barata, and E. N. Chini. 2004. Metabolism of cyclic ADP-ribose: zinc is an endogenous modulator of the cyclase/NAD glycohydrolase ratio of a CD38-like enzyme from human seminal fluid. Life Sci. 74:1781.