메뉴 건너뛰기




Volumn 7, Issue , 2016, Pages

Neutrophil P2X7 receptors mediate NLRP3 inflammasome-dependent IL-1β secretion in response to ATP

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM; CRYOPYRIN; INFLAMMASOME; INTERLEUKIN 1BETA; POTASSIUM; PURINERGIC P2X7 RECEPTOR; CARRIER PROTEIN; IL1B PROTEIN, HUMAN; IL1B PROTEIN, MOUSE; NLRP3 PROTEIN, HUMAN; NLRP3 PROTEIN, MOUSE; PURINERGIC P2X RECEPTOR ANTAGONIST;

EID: 84958230881     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10555     Document Type: Article
Times cited : (334)

References (62)
  • 1
    • 46349089573 scopus 로고    scopus 로고
    • Regulation of cellular ATP release
    • Fitz, J. G. Regulation of cellular ATP release. Trans. Am. Clin. Climatol. Assoc. 118, 199-208 (2007).
    • (2007) Trans. Am. Clin. Climatol. Assoc. , vol.118 , pp. 199-208
    • Fitz, J.G.1
  • 2
    • 79952192382 scopus 로고    scopus 로고
    • Immune cell regulation by autocrine purinergic signalling
    • Junger, W. G. Immune cell regulation by autocrine purinergic signalling. Nat. Rev. Immunol. 11, 201-212 (2011).
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 201-212
    • Junger, W.G.1
  • 3
    • 62349114041 scopus 로고    scopus 로고
    • Extracellular ATP in the immune system: More than just a "danger signal"
    • Trautmann, A. Extracellular ATP in the immune system: more than just a "danger signal". Sci. Signal. 2, pe6 (2009).
    • (2009) Sci. Signal , vol.2 , pp. pe6
    • Trautmann, A.1
  • 5
    • 77957101431 scopus 로고    scopus 로고
    • Extracellular ATP is a danger signal activating P2X7 receptor in lung inflammation and fibrosis
    • Riteau, N. et al. Extracellular ATP is a danger signal activating P2X7 receptor in lung inflammation and fibrosis. Am. J. Respir. Crit. Care Med. 182, 774-783 (2010).
    • (2010) Am. J. Respir. Crit. Care Med. , vol.182 , pp. 774-783
    • Riteau, N.1
  • 6
    • 84892618602 scopus 로고    scopus 로고
    • Extracellular ATP mediates the late phase of neutrophil recruitment to the lung in murine models of acute lung injury
    • Shah, D., Romero, F., Stafstrom, W., Duong, M. & Summer, R. Extracellular ATP mediates the late phase of neutrophil recruitment to the lung in murine models of acute lung injury. Am. J. Physiol. Lung Cell Mol. Physiol. 306, L152-L161 (2014).
    • (2014) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.306 , pp. L152-L161
    • Shah, D.1    Romero, F.2    Stafstrom, W.3    Duong, M.4    Summer, R.5
  • 7
    • 84874280249 scopus 로고    scopus 로고
    • ATP release and purinergic signaling in NLRP3 inflammasome activation
    • Gombault, A., Baron, L. & Couillin, I. ATP release and purinergic signaling in NLRP3 inflammasome activation. Front. Immunol. 3, 414 (2012).
    • (2012) Front. Immunol. , vol.3 , pp. 414
    • Gombault, A.1    Baron, L.2    Couillin, I.3
  • 8
    • 9144269934 scopus 로고    scopus 로고
    • Cellular distribution and functions of P2 receptor subtypes in different systems
    • Burnstock, G. & Knight, G. E. Cellular distribution and functions of P2 receptor subtypes in different systems. Int. Rev. Cytol. 240, 31-304 (2004).
    • (2004) Int. Rev. Cytol. , vol.240 , pp. 31-304
    • Burnstock, G.1    Knight, G.E.2
  • 9
    • 0035338445 scopus 로고    scopus 로고
    • P2X7 nucleotide receptor mediation of membrane pore formation and superoxide generation in human promyelocytes and neutrophils
    • Suh, B. C., Kim, J. S., Namgung, U., Ha, H. & Kim, K. T. P2X7 nucleotide receptor mediation of membrane pore formation and superoxide generation in human promyelocytes and neutrophils. J. Immunol. 166, 6754-6763 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 6754-6763
    • Suh, B.C.1    Kim, J.S.2    Namgung, U.3    Ha, H.4    Kim, K.T.5
  • 10
    • 3042781027 scopus 로고    scopus 로고
    • A putative osmoreceptor system that controls neutrophil function through the release of ATP, its conversion to adenosine, and activation of A2 adenosine and P2 receptors
    • Chen, Y., Shukla, A., Namiki, S., Insel, P. A. & Junger, W. G. A putative osmoreceptor system that controls neutrophil function through the release of ATP, its conversion to adenosine, and activation of A2 adenosine and P2 receptors. J. Leukoc. Biol. 76, 245-253 (2004).
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 245-253
    • Chen, Y.1    Shukla, A.2    Namiki, S.3    Insel, P.A.4    Junger, W.G.5
  • 11
    • 0033711728 scopus 로고    scopus 로고
    • Expression of P2X(7) purinoceptors on human lymphocytes and monocytes: Evidence for nonfunctional P2X(7) receptors
    • Gu, B. J. et al. Expression of P2X(7) purinoceptors on human lymphocytes and monocytes: evidence for nonfunctional P2X(7) receptors. Am. J. Physiol. Cell Physiol. 279, C1189-C1197 (2000).
    • (2000) Am. J. Physiol. Cell Physiol. , vol.279 , pp. C1189-C1197
    • Gu, B.J.1
  • 12
    • 77957296804 scopus 로고    scopus 로고
    • Human neutrophils do not express purinergic P2X7 receptors
    • Martel-Gallegos, G. et al. Human neutrophils do not express purinergic P2X7 receptors. Purinergic Signal. 6, 297-306 (2010).
    • (2010) Purinergic Signal , vol.6 , pp. 297-306
    • Martel-Gallegos, G.1
  • 13
    • 40049087904 scopus 로고    scopus 로고
    • Inhibition of neutrophil apoptosis by ATP is mediated by the P2Y11 receptor
    • Vaughan, K. R. et al. Inhibition of neutrophil apoptosis by ATP is mediated by the P2Y11 receptor. J. Immunol. 179, 8544-8553 (2007).
    • (2007) J. Immunol. , vol.179 , pp. 8544-8553
    • Vaughan, K.R.1
  • 14
    • 0035013306 scopus 로고    scopus 로고
    • Effects of purine and pyrimidine nucleotides on intracellular Ca2+ in human eosinophils: Activation of purinergic P2Y receptors
    • Mohanty, J. G., Raible, D. G., McDermott, L. J., Pelleg, A. & Schulman, E. S. Effects of purine and pyrimidine nucleotides on intracellular Ca2+ in human eosinophils: activation of purinergic P2Y receptors. J. Allergy Clin. Immunol. 107, 849-855 (2001).
    • (2001) J. Allergy Clin. Immunol. , vol.107 , pp. 849-855
    • Mohanty, J.G.1    Raible, D.G.2    McDermott, L.J.3    Pelleg, A.4    Schulman, E.S.5
  • 15
    • 84859492693 scopus 로고    scopus 로고
    • The NLRP3/ASC/Caspase-1 axis regulates IL-1beta processing in neutrophils
    • Mankan, A. K., Dau, T., Jenne, D. & Hornung, V. The NLRP3/ASC/Caspase-1 axis regulates IL-1beta processing in neutrophils. Eur. J. Immunol. 42, 710-715 (2012).
    • (2012) Eur. J. Immunol. , vol.42 , pp. 710-715
    • Mankan, A.K.1    Dau, T.2    Jenne, D.3    Hornung, V.4
  • 16
    • 67649639047 scopus 로고    scopus 로고
    • Signaling at purinergic P2X receptors
    • Surprenant, A. & North, R. A. Signaling at purinergic P2X receptors. Annu. Rev. Physiol. 71, 333-359 (2009).
    • (2009) Annu. Rev. Physiol. , vol.71 , pp. 333-359
    • Surprenant, A.1    North, R.A.2
  • 17
    • 70350339068 scopus 로고    scopus 로고
    • Mammalian P2X7 receptor pharmacology: Comparison of recombinant mouse, rat and human P2X7 receptors
    • Donnelly-Roberts, D. L., Namovic, M. T., Han, P. & Jarvis, M. F. Mammalian P2X7 receptor pharmacology: comparison of recombinant mouse, rat and human P2X7 receptors. Br. J. Pharmacol. 157, 1203-1214 (2009).
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 1203-1214
    • Donnelly-Roberts, D.L.1    Namovic, M.T.2    Han, P.3    Jarvis, M.F.4
  • 18
    • 80052179138 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptotic cell death
    • Miao, E. A., Rajan, J. V. & Aderem, A. Caspase-1-induced pyroptotic cell death. Immunol. Rev. 243, 206-214 (2011).
    • (2011) Immunol. Rev. , vol.243 , pp. 206-214
    • Miao, E.A.1    Rajan, J.V.2    Aderem, A.3
  • 19
    • 0029665112 scopus 로고    scopus 로고
    • The cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7)
    • Surprenant, A., Rassendren, F., Kawashima, E., North, R. A. & Buell, G. The cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7). Science 272, 735-738 (1996).
    • (1996) Science , vol.272 , pp. 735-738
    • Surprenant, A.1    Rassendren, F.2    Kawashima, E.3    North, R.A.4    Buell, G.5
  • 20
    • 84863011694 scopus 로고    scopus 로고
    • Expression, assembly and function of novel C-terminal truncated variants of the mouse P2X7 receptor: Re-evaluation of P2X7 knockouts
    • Masin, M. et al. Expression, assembly and function of novel C-terminal truncated variants of the mouse P2X7 receptor: re-evaluation of P2X7 knockouts. Br. J. Pharmacol. 165, 978-993 (2012).
    • (2012) Br. J. Pharmacol. , vol.165 , pp. 978-993
    • Masin, M.1
  • 21
    • 34548614009 scopus 로고    scopus 로고
    • Nonclassical IL-1 beta secretion stimulated by P2X7 receptors is dependent on inflammasome activation and correlated with exosome release in murine macrophages
    • Qu, Y., Franchi, L., Nunez, G. & Dubyak, G. R. Nonclassical IL-1 beta secretion stimulated by P2X7 receptors is dependent on inflammasome activation and correlated with exosome release in murine macrophages. J. Immunol. 179, 1913-1925 (2007).
    • (2007) J. Immunol. , vol.179 , pp. 1913-1925
    • Qu, Y.1    Franchi, L.2    Nunez, G.3    Dubyak, G.R.4
  • 22
    • 20144375454 scopus 로고    scopus 로고
    • Disruption of the P2X7 purinoceptor gene abolishes chronic inflammatory and neuropathic pain
    • Chessell, I. P. et al. Disruption of the P2X7 purinoceptor gene abolishes chronic inflammatory and neuropathic pain. Pain 114, 386-396 (2005).
    • (2005) Pain , vol.114 , pp. 386-396
    • Chessell, I.P.1
  • 23
    • 67149096558 scopus 로고    scopus 로고
    • Lymphocytes from P2X7-deficient mice exhibit enhanced P2X7 responses
    • Taylor, S. R. et al. Lymphocytes from P2X7-deficient mice exhibit enhanced P2X7 responses. J. Leukoc. Biol. 85, 978-986 (2009).
    • (2009) J. Leukoc. Biol. , vol.85 , pp. 978-986
    • Taylor, S.R.1
  • 24
    • 70350012258 scopus 로고    scopus 로고
    • A functional P2X7 splice variant with an alternative transmembrane domain 1 escapes gene inactivation in P2X7 knock-out mice
    • Nicke, A. et al. A functional P2X7 splice variant with an alternative transmembrane domain 1 escapes gene inactivation in P2X7 knock-out mice. J. Biol. Chem. 284, 25813-25822 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 25813-25822
    • Nicke, A.1
  • 25
    • 0037108511 scopus 로고    scopus 로고
    • Cutting edge: A natural P451L mutation in the cytoplasmic domain impairs the function of the mouse P2X7 receptor
    • Adriouch, S. et al. Cutting edge: a natural P451L mutation in the cytoplasmic domain impairs the function of the mouse P2X7 receptor. J. Immunol. 169, 4108-4112 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 4108-4112
    • Adriouch, S.1
  • 26
    • 84879596906 scopus 로고    scopus 로고
    • K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter
    • Munoz-Planillo, R. et al. K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity 38, 1142-1153 (2013).
    • (2013) Immunity , vol.38 , pp. 1142-1153
    • Munoz-Planillo, R.1
  • 27
    • 84927669849 scopus 로고    scopus 로고
    • K+ efflux agonists induce NLRP3 inflammasome activation independently of Ca2+ signaling
    • Katsnelson, M. A., Rucker, L. G., Russo, H. M. & Dubyak, G. R. K+ efflux agonists induce NLRP3 inflammasome activation independently of Ca2+ signaling. J. Immunol. 194, 3937-3952 (2015).
    • (2015) J. Immunol. , vol.194 , pp. 3937-3952
    • Katsnelson, M.A.1    Rucker, L.G.2    Russo, H.M.3    Dubyak, G.R.4
  • 28
    • 84922553500 scopus 로고    scopus 로고
    • Neutrophil IL-1beta processing induced by pneumolysin is mediated by the NLRP3/ASC inflammasome and caspase-1 activation and is dependent on K+ efflux
    • Karmakar, M. et al. Neutrophil IL-1beta processing induced by pneumolysin is mediated by the NLRP3/ASC inflammasome and caspase-1 activation and is dependent on K+ efflux. J. Immunol. 194, 1763-1775 (2015).
    • (2015) J. Immunol. , vol.194 , pp. 1763-1775
    • Karmakar, M.1
  • 29
    • 33947498152 scopus 로고    scopus 로고
    • Bacterial infections of the cornea (Pseudomonas aeruginosa)
    • Hazlett, L. D. Bacterial infections of the cornea (Pseudomonas aeruginosa). Chem. Immunol. Allergy. 92, 185-194 (2007).
    • (2007) Chem. Immunol. Allergy , vol.92 , pp. 185-194
    • Hazlett, L.D.1
  • 30
    • 84867903731 scopus 로고    scopus 로고
    • Cutting edge: IL-1beta processing during Pseudomonas aeruginosa infection is mediated by neutrophil serine proteases and is independent of NLRC4 and caspase-1
    • Karmakar, M., Sun, Y., Hise, A. G., Rietsch, A. & Pearlman, E. Cutting edge: IL-1beta processing during Pseudomonas aeruginosa infection is mediated by neutrophil serine proteases and is independent of NLRC4 and caspase-1. J. Immunol. 189, 4231-4235 (2012).
    • (2012) J. Immunol. , vol.189 , pp. 4231-4235
    • Karmakar, M.1    Sun, Y.2    Hise, A.G.3    Rietsch, A.4    Pearlman, E.5
  • 31
    • 84863558332 scopus 로고    scopus 로고
    • Fungal antioxidant pathways promote survival against neutrophils during infection
    • Leal, Jr. S. M. et al. Fungal antioxidant pathways promote survival against neutrophils during infection. J. Clin. Invest. 122, 2482-2498 (2012).
    • (2012) J. Clin. Invest. , vol.122 , pp. 2482-2498
    • Leal, S.M.1
  • 32
    • 84892827750 scopus 로고    scopus 로고
    • Activation of neutrophils by autocrine IL-17 A-IL-17RC interactions during fungal infection is regulated by IL-6, IL-23, RORgammat and dectin-2
    • Taylor, P. R. et al. Activation of neutrophils by autocrine IL-17 A-IL-17RC interactions during fungal infection is regulated by IL-6, IL-23, RORgammat and dectin-2. Nat. Immunol. 15, 143-151 (2014).
    • (2014) Nat. Immunol. , vol.15 , pp. 143-151
    • Taylor, P.R.1
  • 33
    • 0027257221 scopus 로고
    • Gene targeting yields a CD18-mutant mouse for study of inflammation
    • Wilson, R. W. et al. Gene targeting yields a CD18-mutant mouse for study of inflammation. J. Immunol. 151, 1571-1578 (1993).
    • (1993) J. Immunol. , vol.151 , pp. 1571-1578
    • Wilson, R.W.1
  • 34
    • 84904792729 scopus 로고    scopus 로고
    • The neutrophil NLRC4 inflammasome selectively promotes IL-1beta maturation without pyroptosis during acute Salmonella challenge
    • Chen, K. W. et al. The neutrophil NLRC4 inflammasome selectively promotes IL-1beta maturation without pyroptosis during acute Salmonella challenge. Cell Rep. 8, 570-582 (2014).
    • (2014) Cell Rep. , vol.8 , pp. 570-582
    • Chen, K.W.1
  • 35
    • 73249139175 scopus 로고    scopus 로고
    • Caspase 1-independent activation of interleukin-1beta in neutrophil-predominant inflammation
    • Guma, M. et al. Caspase 1-independent activation of interleukin-1beta in neutrophil-predominant inflammation. Arthritis Rheum. 60, 3642-3650 (2009).
    • (2009) Arthritis Rheum. , vol.60 , pp. 3642-3650
    • Guma, M.1
  • 36
    • 84922008927 scopus 로고    scopus 로고
    • Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation
    • Romberg, N. et al. Mutation of NLRC4 causes a syndrome of enterocolitis and autoinflammation. Nat. Genet. 46, 1135-1139 (2014).
    • (2014) Nat. Genet. , vol.46 , pp. 1135-1139
    • Romberg, N.1
  • 37
    • 84878237993 scopus 로고    scopus 로고
    • Activation and regulation of the inflammasomes
    • Latz, E., Xiao, T. S. & Stutz, A. Activation and regulation of the inflammasomes. Nat. Rev. Immunol. 13, 397-411 (2013).
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 397-411
    • Latz, E.1    Xiao, T.S.2    Stutz, A.3
  • 38
    • 0032923377 scopus 로고    scopus 로고
    • The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles
    • Andrei, C. et al. The secretory route of the leaderless protein interleukin 1beta involves exocytosis of endolysosome-related vesicles. Mol. Biol. Cell 10, 1463-1475 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1463-1475
    • Andrei, C.1
  • 39
    • 3042800587 scopus 로고    scopus 로고
    • Phospholipases C and A2 control lysosome-mediated IL-1 beta secretion: Implications for inflammatory processes
    • Andrei, C. et al. Phospholipases C and A2 control lysosome-mediated IL-1 beta secretion: Implications for inflammatory processes. Proc. Natl Acad. Sci. USA 101, 9745-9750 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9745-9750
    • Andrei, C.1
  • 40
    • 0035655395 scopus 로고    scopus 로고
    • Rapid secretion of interleukin-1beta by microvesicle shedding
    • MacKenzie, A. et al. Rapid secretion of interleukin-1beta by microvesicle shedding. Immunity 15, 825-835 (2001).
    • (2001) Immunity , vol.15 , pp. 825-835
    • MacKenzie, A.1
  • 41
    • 34247353273 scopus 로고    scopus 로고
    • Stimulation of P2 receptors causes release of IL-1 beta-loaded microvesicles from human dendritic cells
    • Pizzirani, C. et al. Stimulation of P2 receptors causes release of IL-1 beta-loaded microvesicles from human dendritic cells. Blood 109, 3856-3864 (2007).
    • (2007) Blood , vol.109 , pp. 3856-3864
    • Pizzirani, C.1
  • 42
    • 34548444551 scopus 로고    scopus 로고
    • Liaisons dangereuses: P2X(7) and the inflammasome
    • Di Virgilio, F. Liaisons dangereuses: P2X(7) and the inflammasome. Trends Pharmacol. Sci. 28, 465-472 (2007).
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 465-472
    • Di Virgilio, F.1
  • 43
    • 0034192082 scopus 로고    scopus 로고
    • Kinetics and mechanism of ATP-dependent IL-1 beta release from microglial cells
    • Sanz, J. M. & Di Virgilio, F. Kinetics and mechanism of ATP-dependent IL-1 beta release from microglial cells. J. Immunol. 164, 4893-4898 (2000).
    • (2000) J. Immunol. , vol.164 , pp. 4893-4898
    • Sanz, J.M.1    Di Virgilio, F.2
  • 44
    • 84896733932 scopus 로고    scopus 로고
    • Localization and functionality of the inflammasome in neutrophils
    • Bakele, M. et al. Localization and functionality of the inflammasome in neutrophils. J. Biol. Chem. 289, 5320-5329 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 5320-5329
    • Bakele, M.1
  • 45
    • 84894583793 scopus 로고    scopus 로고
    • NADPH oxidase derived reactive oxygen species are involved in human neutrophil IL-1beta secretion but not in inflammasome activation
    • Gabelloni, M. L. et al. NADPH oxidase derived reactive oxygen species are involved in human neutrophil IL-1beta secretion but not in inflammasome activation. Eur. J. Immunol. 43, 3324-3335 (2013).
    • (2013) Eur. J. Immunol. , vol.43 , pp. 3324-3335
    • Gabelloni, M.L.1
  • 46
    • 67349167990 scopus 로고    scopus 로고
    • The P2X(7) receptor and intracellular pathogens: A continuing struggle
    • Coutinho-Silva, R., Correa, G., Sater, A. A. & Ojcius, D. M. The P2X(7) receptor and intracellular pathogens: a continuing struggle. Purinergic Signal. 5, 197-204 (2009).
    • (2009) Purinergic Signal , vol.5 , pp. 197-204
    • Coutinho-Silva, R.1    Correa, G.2    Sater, A.A.3    Ojcius, D.M.4
  • 47
    • 0023802930 scopus 로고
    • Stimulation of human neutrophil adhesive properties by adenine nucleotides
    • Freyer, D. R., Boxer, L. A., Axtell, R. A. & Todd, 3rd R. F. Stimulation of human neutrophil adhesive properties by adenine nucleotides. J. Immunol. 141, 580-586 (1988).
    • (1988) J. Immunol. , vol.141 , pp. 580-586
    • Freyer, D.R.1    Boxer, L.A.2    Axtell, R.A.3    Todd, R.F.4
  • 48
    • 0035830853 scopus 로고    scopus 로고
    • ATP-stimulated release of interleukin (IL)-1beta and IL-18 requires priming by lipopolysaccharide and is independent of caspase-1 cleavage
    • Mehta, V. B., Hart, J. & Wewers, M. D. ATP-stimulated release of interleukin (IL)-1beta and IL-18 requires priming by lipopolysaccharide and is independent of caspase-1 cleavage. J. Biol. Chem. 276, 3820-3826 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 3820-3826
    • Mehta, V.B.1    Hart, J.2    Wewers, M.D.3
  • 49
    • 0035808396 scopus 로고    scopus 로고
    • Altered cytokine production in mice lacking P2X(7) receptors
    • Solle, M. et al. Altered cytokine production in mice lacking P2X(7) receptors. J. Biol. Chem. 276, 125-132 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 125-132
    • Solle, M.1
  • 50
    • 0029160229 scopus 로고
    • Extracellular ATP enhances mRNA levels of nitric oxide synthase and TNF-alpha in lipopolysaccharide-treated RAW 264.7 murine macrophages
    • Tonetti, M., Sturla, L., Giovine, M., Benatti, U. & De Flora, A. Extracellular ATP enhances mRNA levels of nitric oxide synthase and TNF-alpha in lipopolysaccharide-treated RAW 264.7 murine macrophages. Biochem. Biophys. Res. Commun. 214, 125-130 (1995).
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 125-130
    • Tonetti, M.1    Sturla, L.2    Giovine, M.3    Benatti, U.4    De Flora, A.5
  • 51
    • 33845708770 scopus 로고    scopus 로고
    • ATP release guides neutrophil chemotaxis via P2Y2 and A3 receptors
    • Chen, Y. et al. ATP release guides neutrophil chemotaxis via P2Y2 and A3 receptors. Science 314, 1792-1795 (2006).
    • (2006) Science , vol.314 , pp. 1792-1795
    • Chen, Y.1
  • 52
    • 77957943307 scopus 로고    scopus 로고
    • Intravascular danger signals guide neutrophils to sites of sterile inflammation
    • McDonald, B. et al. Intravascular danger signals guide neutrophils to sites of sterile inflammation. Science 330, 362-366 (2010).
    • (2010) Science , vol.330 , pp. 362-366
    • McDonald, B.1
  • 53
    • 0030589244 scopus 로고    scopus 로고
    • Induction of the P2z/P2X7 nucleotide receptor and associated phospholipase D activity by lipopolysaccharide and IFN-gamma in the human THP-1 monocytic cell line
    • Humphreys, B. D. & Dubyak, G. R. Induction of the P2z/P2X7 nucleotide receptor and associated phospholipase D activity by lipopolysaccharide and IFN-gamma in the human THP-1 monocytic cell line. J. Immunol. 157, 5627-5637 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 5627-5637
    • Humphreys, B.D.1    Dubyak, G.R.2
  • 54
    • 84867112397 scopus 로고    scopus 로고
    • Splice variants of the P2X7 receptor reveal differential agonist dependence and functional coupling with pannexin-1
    • Xu, X. J. et al. Splice variants of the P2X7 receptor reveal differential agonist dependence and functional coupling with pannexin-1. J. Cell Sci. 125, 3776-3789 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 3776-3789
    • Xu, X.J.1
  • 55
    • 28244480768 scopus 로고    scopus 로고
    • Inhibitory effects of chloride on the activation of caspase-1, IL-1beta secretion, and cytolysis by the P2X7 receptor
    • Verhoef, P. A., Kertesy, S. B., Lundberg, K., Kahlenberg, J. M. & Dubyak, G. R. Inhibitory effects of chloride on the activation of caspase-1, IL-1beta secretion, and cytolysis by the P2X7 receptor. J. Immunol. 175, 7623-7634 (2005).
    • (2005) J. Immunol. , vol.175 , pp. 7623-7634
    • Verhoef, P.A.1    Kertesy, S.B.2    Lundberg, K.3    Kahlenberg, J.M.4    Dubyak, G.R.5
  • 56
    • 0030840444 scopus 로고    scopus 로고
    • ATP-induced killing of mycobacteria by human macrophages is mediated by purinergic P2Z(P2X7) receptors
    • Lammas, D. A. et al. ATP-induced killing of mycobacteria by human macrophages is mediated by purinergic P2Z(P2X7) receptors. Immunity 7, 433-444 (1997).
    • (1997) Immunity , vol.7 , pp. 433-444
    • Lammas, D.A.1
  • 57
    • 0037032444 scopus 로고    scopus 로고
    • Response heterogeneity of human macrophages to ATP is associated with P2X7 receptor expression but not to polymorphisms in the P2RX7 promoter
    • Li, C. M., Campbell, S. J., Kumararatne, D. S., Hill, A. V. & Lammas, D. A. Response heterogeneity of human macrophages to ATP is associated with P2X7 receptor expression but not to polymorphisms in the P2RX7 promoter. FEBS Lett. 531, 127-131 (2002).
    • (2002) FEBS Lett. , vol.531 , pp. 127-131
    • Li, C.M.1    Campbell, S.J.2    Kumararatne, D.S.3    Hill, A.V.4    Lammas, D.A.5
  • 58
    • 0035815630 scopus 로고    scopus 로고
    • A Glu-496 to Ala polymorphism leads to loss of function of the human P2X7 receptor
    • Gu, B. J. et al. A Glu-496 to Ala polymorphism leads to loss of function of the human P2X7 receptor. J. Biol. Chem. 276, 11135-11142 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 11135-11142
    • Gu, B.J.1
  • 60
    • 17644379097 scopus 로고    scopus 로고
    • The purinergic P2X7 receptor is not required for control of pulmonary Mycobacterium tuberculosis infection
    • Myers, A. J., Eilertson, B., Fulton, S. A., Flynn, J. L. & Canaday, D. H. The purinergic P2X7 receptor is not required for control of pulmonary Mycobacterium tuberculosis infection. Infect. Immunol. 73, 3192-3195 (2005).
    • (2005) Infect. Immunol. , vol.73 , pp. 3192-3195
    • Myers, A.J.1    Eilertson, B.2    Fulton, S.A.3    Flynn, J.L.4    Canaday, D.H.5
  • 61
    • 78650399138 scopus 로고    scopus 로고
    • Metaanalysis of P2X7 gene polymorphisms and tuberculosis susceptibility
    • Xiao, J. et al. Metaanalysis of P2X7 gene polymorphisms and tuberculosis susceptibility. FEMS. Immunol. Med. Microbiol. 60, 165-170 (2010).
    • (2010) FEMS. Immunol. Med. Microbiol. , vol.60 , pp. 165-170
    • Xiao, J.1
  • 62
    • 77954887909 scopus 로고    scopus 로고
    • Evidence for associations between the purinergic receptor P2X(7) (P2RX7) and toxoplasmosis
    • Jamieson, S. E. et al. Evidence for associations between the purinergic receptor P2X(7) (P2RX7) and toxoplasmosis. Genes. Immunol. 11, 374-383 (2010).
    • (2010) Genes. Immunol. , vol.11 , pp. 374-383
    • Jamieson, S.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.