P2X7 receptor-dependent and -independent T cell death is induced by nicotinamide adenine dinucleotide

Journal of Immunology

Volumn 174, Issue 4, 2005, Pages 1971-1979

  Kawamura, Hiroki ^a   Aswad, Fred ^a   Minagawa, Masahiro ^a   Malone, Karen ^a   Kaslow, Harvey ^a   Koch Nolte, Friederich ^b   Schott, William H ^c   Leiter, Edward H ^c   Dennert, Gunther ^a,d  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^b UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

^c JACKSON LABORATORY   (United States)

^d UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; CASPASE INHIBITOR; CELL SURFACE PROTEIN; DNA FRAGMENT; LIGAND; LIPOCORTIN 5; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PURINE P2X7 RECEPTOR; PURINE RECEPTOR;

APOPTOSIS; ARTICLE; CELL DEATH; CELL PROLIFERATION; CHANNEL GATING; FLOW CYTOMETRY; HYDROLYSIS; MOUSE; NONHUMAN; PRIORITY JOURNAL; T LYMPHOCYTE; WESTERN BLOTTING;

EID: 13544258083     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.174.4.1971     Document Type: Article

References (37)

1. Wang, J., E. Nemoto, A. Y. Kots, H. R. Kaslow, and G. Dennert. 1994. Regulation of cytotoxic T cells by ecto-nicotinamide adenine dinucleotide (NAD) correlates with cell surface GPI-anchored/arginine ADP-ribosyltransferase. J. Immunol. 153:4048.
2. 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.
3. Han, M. K., Y. S. Cho, Y. S. Kim, C. Y. Yim, and U. H. Kim. 2000. Interaction of two classes of ADP-ribose transfer reactions in immune signaling. J. Biol. Chem. 275:20799.
4. 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.
5. Nemoto, E., Y. Yu, and G. Dennert. 1996. Cell surface ADP-ribosyltransferase regulates lymphocyte function-associated molecule-1 (LFA-1) function in T cells. J. Immunol. 157:3341.
6. 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.
7. 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.
8. Liu, Z. X., Y. Yu, and G. Dennert. 1999. A cell surface ADP-ribosyltransferase modulates T cell receptor association and signaling. J. Biol. Chem. 274:17399.
9. 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.
10. 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.
11. 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.
12. Solle, M., J. Labasi, D. G. Perregaux, E. Stam, N. Petrushova, B. H. Koller, R. J. Griffiths, and C. A. Gabel. 2001. Altered cytokine production in mice lacking P2X(7) receptors. J. Biol. Chem. 276:125.
13. 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.
14. Matsuoka, S., H. Tsurui, M. Abe, K. Terashima, K. Nakamura, Y. Hamano, M. Ohtsuji, N. Honma, I. Serizawa, Y. Ishii, et al. 2003. A monoclonal antibody to the α2 domain of murine major histocompatibility complex class I that specifically kills activated lymphocytes and blocks liver damage in the concanavalin A hepatitis model. J. Exp. Med. 198:497.
15. Humphreys, B. D., C. Virginio, A. Surprenant, J. Rice, and G. R. Dubyak. 1998. Isoquinolines as antagonists of the P2X7 nucleotide receptor: high selectivity for the human versus rat receptor homologues. Mol. Pharmacol. 54:22.
16. Howard, M., J. C. Grimaldi, J. F. Bazan, F. E. Lund, L. Santos-Argumedo, R. M. Parkhouse, T. F. Walseth, and H. C. Lee. 1993. Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38. Science 262:1056.
17. Mutini, C., S. Falzoni, D. Ferrari, P. Chiozzi, A. Morelli, O. R. Baricordi, G. Collo, P. Ricciardi-Castagnoli, and F. Di Virgilio. 1999. Mouse dendritic cells express the P2X7 purinergic receptor: characterization and possible participation in antigen presentation. J. Immunol. 163:1958.
18. Collo, G., S. Neidhart, E. Kawashima, M. Kosco-Vilbois, R. A. North, and G. Buell. 1997. Tissue distribution of the P2X7 receptor. Neuropharmacology 36:1277.
19. Mehta, V. B., J. Hart, and M. D. Wewers. 2001. ATP-stimulated release of interleukin (IL)-1β and IL-18 requires priming by lipopolysaccharide and is independent of caspase-1 cleavage. J. Biol. Chem. 276:3820.
20. 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.
21. Chakfe, Y., R. Seguin, J. P. Antel, C. Morissette, D. Malo, D. Henderson, and P. Seguela. 2002. ADP and AMP induce interleukin-1β release from microglial cells through activation of ATP-primed P2X7 receptor channels. J. Neurosci. 22:3061.
22. Gargett, C. E., and J. S. Wiley. 1997. The isoquinoline derivative KN-62 a potent antagonist of the P2Z-receptor of human lymphocytes. Br. J. Pharmacol. 120:1483.
23. Jacobson, E. L., and M. K. Jacobson. 1997. Tissue NAD as a biochemical measure of niacin status in humans. Methods Enzymol. 280:221.
24. Kim, U. H., M. K. Kim, J. S. Kim, M. K. Han, B. H. Park, and H. R. Kim. 1993. Purification and characterization of NAD glycohydrolase from rabbit erythrocytes. Arch. Biochem. Biophys. 305:147.
25. Aleo, M. F., M. L. Giudici, S. Sestini, P. Danesi, G. Pompucci, and A. Preti. 2001. Metabolic fate of extracellular NAD in human skin fibroblasts. J. Cell. Biochem. 80:360.
26. 2A adenosine receptor as a physiological immunosuppressor and to engineer inflammation in vivo. Biochem. Pharmacol. 65:493.
27. Haag, F., V. Andresen, S. Karsten, F. Koch-Nolte, and H. Thiele. 1995. Both allelic forms of the rat T cell differentiation marker RT6 display nicotinamide adenine dinucleotide (NAD)-glycohydrolase activity, yet only RT6.2 is capable of automodification upon incubation with NAD. Eur. J. Immunol. 25:2355.
28. +: arginine ADP ribosyltransferases with auto-ADP ribosylation activity. J. Immunol. 156:4259.
29. + regulates intracellular free calcium concentration in human monocytes. Biochem. J. 382:849.
30. Verhoef, P. A., M. Estacion, W. Schilling, and G. R. Dubyak. 2003. P2X7 receptor-dependent blebbing and the activation of Rho-effector kinases, caspases, and IL-1β release. J. Immunol. 170:5728.
31. Ferrari, D., M. Los, M. K. Bauer, P. Vandenabeele, S. Wesselborg, and K. Schulze-Osthoff. 1999. P2Z purinoreceptor ligation induces activation of caspases with distinct roles in apoptotic and necrotic alterations of cell death. FEBS Lett. 447:71.
32. North, R. A., and A. Surprenant. 2000. Pharmacology of cloned P2X receptors. Annu. Rev. Pharmacol. Toxicol. 40:563.
33. Traut, T. W. 1994. Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 140:1.
34. + T lymphocytes induces diabetes in resistant biobreeding/Worcester (BB/W) rats. J. Exp. Med. 166:461.
35. 1 mice. Int. Immunol. 7:883.
36. Prochazka, M., D. V. Serreze, S. M. Worthen, and E. H. Leiter. 1989. Genetic control of diabetogenesis in NOD/Lt mice: development and analysis of congenic stocks. Diabetes 38:1446.
37. Elliott, J. I., and C. F. Higgins. 2004. Major histocompatibility complex class I shedding and programmed cell death stimulated through the proinflammatory P2X7 receptor: a candidate susceptibility gene for NOD diabetes. Diabetes 53:2012.