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NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor

Standard

NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor. / Seman, Michel; Adriouch, Sahil; Scheuplein, Felix; Krebs, Christian; Freese, Dunja; Glowacki, Gustavo; Deterre, Phillipe; Haag, Friedrich; Koch-Nolte, Friedrich.

in: IMMUNITY, Jahrgang 19, Nr. 4, 10.2003, S. 571-82.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Seman, M, Adriouch, S, Scheuplein, F, Krebs, C, Freese, D, Glowacki, G, Deterre, P, Haag, F & Koch-Nolte, F 2003, 'NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor', IMMUNITY, Jg. 19, Nr. 4, S. 571-82.

APA

Seman, M., Adriouch, S., Scheuplein, F., Krebs, C., Freese, D., Glowacki, G., Deterre, P., Haag, F., & Koch-Nolte, F. (2003). NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor. IMMUNITY, 19(4), 571-82.

Vancouver

Seman M, Adriouch S, Scheuplein F, Krebs C, Freese D, Glowacki G et al. NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor. IMMUNITY. 2003 Okt;19(4):571-82.

Bibtex

@article{97661b941706471288ea0359bfae1b6f,
title = "NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor",
abstract = "T cells express a toxin-related ADP-ribosylating ectoenzyme, ART2. Exposure of mature T cells to NAD, the substrate for ADP-ribosylation, induces cell death. ART2-catalyzed ADP-ribosylation activates the cytolytic P2X7 purinoceptor, causing calcium flux, pore formation, phosphatidylserine exposure, shedding of CD62L, cell shrinkage, and propidium iodide uptake. Interestingly, much lower NAD than ATP concentrations are required to activate P2X7. NAD-induced cell death (NICD) operates with endogenous sources of NAD released upon cell lysis. These findings identify P2X7 as a key effector of NICD and demonstrate that P2X7 can be activated by an endogenous ligand other than ATP. Our results delineate an alternative mechanism for inducing T cell death and set an interesting precedent for immunoregulation via crosstalk between NAD-dependent ADP-ribosyltransferases and purinoceptors.",
keywords = "ADP Ribose Transferases, Animals, Apoptosis, Calcium, GPI-Linked Proteins, L-Selectin, Membrane Proteins, Mice, NAD, Receptors, Purinergic P2, Receptors, Purinergic P2X7, T-Lymphocytes, Journal Article, Research Support, Non-U.S. Gov't",
author = "Michel Seman and Sahil Adriouch and Felix Scheuplein and Christian Krebs and Dunja Freese and Gustavo Glowacki and Phillipe Deterre and Friedrich Haag and Friedrich Koch-Nolte",
year = "2003",
month = oct,
language = "English",
volume = "19",
pages = "571--82",
journal = "IMMUNITY",
issn = "1074-7613",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - NAD-induced T cell death: ADP-ribosylation of cell surface proteins by ART2 activates the cytolytic P2X7 purinoceptor

AU - Seman, Michel

AU - Adriouch, Sahil

AU - Scheuplein, Felix

AU - Krebs, Christian

AU - Freese, Dunja

AU - Glowacki, Gustavo

AU - Deterre, Phillipe

AU - Haag, Friedrich

AU - Koch-Nolte, Friedrich

PY - 2003/10

Y1 - 2003/10

N2 - T cells express a toxin-related ADP-ribosylating ectoenzyme, ART2. Exposure of mature T cells to NAD, the substrate for ADP-ribosylation, induces cell death. ART2-catalyzed ADP-ribosylation activates the cytolytic P2X7 purinoceptor, causing calcium flux, pore formation, phosphatidylserine exposure, shedding of CD62L, cell shrinkage, and propidium iodide uptake. Interestingly, much lower NAD than ATP concentrations are required to activate P2X7. NAD-induced cell death (NICD) operates with endogenous sources of NAD released upon cell lysis. These findings identify P2X7 as a key effector of NICD and demonstrate that P2X7 can be activated by an endogenous ligand other than ATP. Our results delineate an alternative mechanism for inducing T cell death and set an interesting precedent for immunoregulation via crosstalk between NAD-dependent ADP-ribosyltransferases and purinoceptors.

AB - T cells express a toxin-related ADP-ribosylating ectoenzyme, ART2. Exposure of mature T cells to NAD, the substrate for ADP-ribosylation, induces cell death. ART2-catalyzed ADP-ribosylation activates the cytolytic P2X7 purinoceptor, causing calcium flux, pore formation, phosphatidylserine exposure, shedding of CD62L, cell shrinkage, and propidium iodide uptake. Interestingly, much lower NAD than ATP concentrations are required to activate P2X7. NAD-induced cell death (NICD) operates with endogenous sources of NAD released upon cell lysis. These findings identify P2X7 as a key effector of NICD and demonstrate that P2X7 can be activated by an endogenous ligand other than ATP. Our results delineate an alternative mechanism for inducing T cell death and set an interesting precedent for immunoregulation via crosstalk between NAD-dependent ADP-ribosyltransferases and purinoceptors.

KW - ADP Ribose Transferases

KW - Animals

KW - Apoptosis

KW - Calcium

KW - GPI-Linked Proteins

KW - L-Selectin

KW - Membrane Proteins

KW - Mice

KW - NAD

KW - Receptors, Purinergic P2

KW - Receptors, Purinergic P2X7

KW - T-Lymphocytes

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

M3 - SCORING: Journal article

C2 - 14563321

VL - 19

SP - 571

EP - 582

JO - IMMUNITY

JF - IMMUNITY

SN - 1074-7613

IS - 4

ER -