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The P2X7 receptor: A main player in inflammation
Open accessAbstract
Damage associated molecular patterns (DAMPs) are intracellular molecules released from infected or injured cells to activate inflammatory and reparatory responses. One of the most ancient and conserved DAMPs is extracellular ATP that exerts its phlogistic activity mainly through activation of the P2X7 receptor (P2X7R). The P2X7R is an ATP gated ion channel, expressed by most immune cells, including the monocyte-derived cell lineages, T and B lymphocytes and their precursors. Here we give an overview of recent and established literature on the role of P2X7R in septic and sterile inflammation. P2X7R ability in restraining intracellular bacteria and parasite infection by modulation of the immune response are described, with particular focus on Mycobacteria and Plasmodium. Emerging literature on the role of P2X7 in viral infections such as HIV-1 is also briefly covered. Finally, we describe the numerous intracellular pathways related to inflammation and activated by the P2X7R, including the NLRP3 inflammasome, NF-kB, NFAT, GSK3β and VEGF, and discuss the involvement of P2X7R in chronic diseases. The possible therapeutic applications of P2X7R antagonists are also described.
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“their activation induced by viral infection leads to molecular (mainly neuroimmune response activation, reactive oxygen species (ROS) formation, and glutamate release) and behavioral alterations [17, 20] as well as to mental disorders [21].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [20]
In the citing paper
“Consequently, there is an activation of caspase-1 and maturation of IL-1β and IL-18, resulting in pro-inflammatory cytokine release [16, 20, 52, 71, 73].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [20]
In the citing paper
“The P2X7 receptor, as a central player in inflammation, participates in viral infections. Exerting mostly pro-inflammatory roles [20], the P2X7 receptor is important for pathogen elimination [108], but on the other hand, its activation may be detrimental to the host due to the induction of exacerbated inflammatory responses.”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [20]
Citations
Cites
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
Immunological and inflammatory functions of the interleukin-1 family
Dinarello, C. A. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132612 · Cited by 3,466
Pyroptosis: host cell death and inflammation
Bergsbaken, T., Fink, S. L., & Cookson, B. T. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2070 · Cited by 3,288
A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J. G., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,613
Muñoz-Planillo, R., Kuffa, P., Martínez-Colón, G. J., Smith, B. L., Rajendiran, T. M., & Núñez, G. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.016 · Cited by 2,167
The Cytolytic P 2Z Receptor for Extracellular ATP Identified as a P 2X Receptor (P2X 7 )
Surprenant, A., Rassendren, F., Kawashima, E., North, R. A., & Buell, G. (1996) · Science · doi:10.1126/science.272.5262.735 · Cited by 1,739
Pannexin‐1 mediates large pore formation and interleukin‐1β release by the ATP‐gated P2X7 receptor
Pelegrı́n, P., & Surprenant, A. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601378 · Cited by 1,490
Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration
Pétrilli, V, Papin, S., Dostert, C., Mayor, A., Martinon, F., & Tschopp, J. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402195 · Cited by 1,445
NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux
He, Y., Zeng, M. Y., Yang, D., Motro, B., & Núñez, G. (2016) · Nature · doi:10.1038/nature16959 · Cited by 1,295
The P2X7 Receptor in Infection and Inflammation
Di Virgilio, F., Dal Ben, D., Sarti, A. C., Giuliani, A. L., & Falzoni, S. (2017) · Immunity · doi:10.1016/j.immuni.2017.06.020 · Cited by 1,267
Self-citationMartin, M., Rehani, K., Jope, R. S., & Michalek, S. M. (2005) · Nature Immunology · doi:10.1038/ni1221 · Cited by 1,099
The P2X7 Receptor: A Key Player in IL-1 Processing and Release
Ferrari, D., Pizzirani, C., Adinolfi, E., Lemoli, R. M., Curti, A., Idzko, M., Panther, E., & Di Virgilio, F. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.7.3877 · Cited by 1,025
Self-citationNucleotide signalling during inflammation
Idzko, M., Ferrari, D., & Eltzschig, H. K. (2014) · Nature · doi:10.1038/nature13085 · Cited by 930
Multiple Sclerosis: A Coordinated Immunological Attack against Myelin in the Central Nervous System
Steinman, L. (1996) · Cell · doi:10.1016/s0092-8674(00)81107-1 · Cited by 892
Immune cell regulation by autocrine purinergic signalling
JUNGER, W. G. (2011) · Nature reviews. Immunology · doi:10.1038/nri2938 · Cited by 855
The inflammasome: an integrated view
Gross, O., Thomas, C. J., Guarda, G., & Tschopp, J. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01046.x · Cited by 778
Perregaux, D. G., & Gabel, C. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36591-2 · Cited by 775
Shi, H., Wang, Y., Li, X., Zhan, X., Tang, M., Fina, M., Su, L., Pratt, D., Bu, C. H., Hildebrand, S., et al. (2015) · Nature Immunology · doi:10.1038/ni.3333 · Cited by 771
Crystal structure of the ATP-gated P2X4 ion channel in the closed state
Kawate, T., Michel, J. J. C., Birdsong, W. T., & Gouaux, E. (2009) · Nature · doi:10.1038/nature08198 · Cited by 739
Yang, D., He, Y., Muñoz-Planillo, R., Liu, Q., & Núñez, G. (2015) · Immunity · doi:10.1016/j.immuni.2015.10.009 · Cited by 622
Ferrari, D., Chiozzi, P., Falzoni, S., Susino, M. D., Melchiorri, L., Baricordi, O. R., & Virgilio, F. D. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.159.3.1451 · Cited by 616
Molecular mechanism of ATP binding and ion channel activation in P2X receptors
Hattori, M., & Gouaux, E. (2012) · Nature · doi:10.1038/nature11010 · Cited by 580
Identification of a Plant Receptor for Extracellular ATP
Choi, J., Tanaka, K., Cao, Y., Qi, Y. A., Qiu, J., Liang, Y., Lee, S. Y., & Stacey, G. S. (2014) · Science · doi:10.1126/science.343.6168.290 · Cited by 578
Extracellular purines, purinergic receptors and tumor growth
Virgilio, F. D., & Adinolfi, E. (2016) · Oncogene · doi:10.1038/onc.2016.206 · Cited by 567
Self-citationYiangou, Y., Facer, P., Durrenberger, P., Chessell, I. P., Naylor, A., Bountra, C., Banati, R. R., & Anand, P. (2006) · BMC Neurology · doi:10.1186/1471-2377-6-12 · Cited by 509
Molloy, A., Laochumroonvorapong, P., & Kaplan, G. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.180.4.1499 · Cited by 501
NOD-Like Receptors in Infection, Immunity, and Diseases
Kim, Y. K., Shin, J., & Nahm, M. H. (2015) · Yonsei Medical Journal · doi:10.3349/ymj.2016.57.1.5 · Cited by 481
The Inflammasome: First Line of the Immune Response to Cell Stress
Ogura, Y., Sutterwala, F. S., & Flavell, R. A. (2006) · Cell · doi:10.1016/j.cell.2006.08.002 · Cited by 474
Ferrari, D., Chiozzi, P., Falzoni, S., Hanau, S., & Virgilio, F. D. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.3.579 · Cited by 474
Piccini, A., Carta, S., Tassi, S., Lasigliè, D., Fossati, G., & Rubartelli, A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709684105 · Cited by 460
Neutrophil P2X7 receptors mediate NLRP3 inflammasome-dependent IL-1β secretion in response to ATP
Karmakar, M., Katsnelson, M. A., Dubyak, G. R., & Pearlman, E. (2016) · Nature Communications · doi:10.1038/ncomms10555 · Cited by 450
Honoré, P., Donnelly‐Roberts, D. L., Namovic, M. T., Hsieh, G. C., Zhu, C., Mikusa, J. P., Hernandez, G., Zhong, C., Gauvin, D. M., Chandran, P., et al. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.111559 · Cited by 433
Elssner, A., Duncan, M., Gavrilin, M. A., & Wewers, M. D. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.8.4987 · Cited by 425
Pore dilation of neuronal P2X receptor channels
Virginio, C., MacKenzie, A., Rassendren, F. A., North, R. A., & Surprenant, A. (1999) · Nature Neuroscience · doi:10.1038/7225 · Cited by 410
Brilliant Blue G Selectively Blocks ATP-Gated Rat P2X7Receptors
Jiang, L., Mackenzie, A. B., North, R. A., & Surprenant, A. (2000) · Molecular Pharmacology · doi:10.1124/mol.58.1.82 · Cited by 401
ATP4- permeabilizes the plasma membrane of mouse macrophages to fluorescent dyes.
Steinberg, T. H., Newman, A. S., Swanson, J. A., & Silverstein, S. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47497-2 · Cited by 397
P2X7 receptors in the nervous system
Sperlágh, B., Vizi, E. S., Wirkner, K., & Illés, P. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.03.007 · Cited by 383
Proteomic and functional evidence for a P2X7 receptor signalling complex
Kim, M., Jiang, L., Wilson, H. L., North, R. A., & Surprenant, A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.22.6347 · Cited by 379
Innate and adaptive immune responses regulated by glycogen synthase kinase-3 (GSK3)
Beurel, E., Michalek, S. M., & Jope, R. S. (2009) · Trends in Immunology · doi:10.1016/j.it.2009.09.007 · Cited by 378
The P2Z purinoceptor: an intriguing role in immunity, inflammation and cell death
Virgilio, F. D. (1995) · Immunology Today · doi:10.1016/0167-5699(95)80045-x · Cited by 374
NLRP3 inflammasome is expressed and functional in mouse brain microglia but not in astrocytes
Gustin, A., Kirchmeyer, M., Koncina, E., Felten, P., Losciuto, S., Heurtaux, T., Tardivel, A., Heuschling, P., & Dostert, C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130624 · Cited by 369
Oxidized ATP. An irreversible inhibitor of the macrophage purinergic P2Z receptor.
Murgia, M., Hanau, S., Pizzo, P., Rippa, M., & Virgilio, F. D. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53082-9 · Cited by 367
Expression of P2X7 Receptor Increases In Vivo Tumor Growth
Adinolfi, E., Raffaghello, L., Giuliani, A. L., Cavazzini, L., Capece, M., Chiozzi, P., Bianchi, G., Kroemer, G., Pistoia, V., & Virgilio, F. D. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-1947 · Cited by 366
Self-citationMouse microglial cells express a plasma membrane pore gated by extracellular ATP
Ferrari, D., Villalba, M., Chiozzi, P., Falzoni, S., Ricciardi‐Castagnoli, P., & Virgilio, F. D. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.4.1531 · Cited by 352
Human astrocytes express a novel NLRP2 inflammasome
Minkiewicz, J., Vaccari, J. P. D. R., & Keane, R. W. (2013) · Glia · doi:10.1002/glia.22499 · Cited by 343
Structural basis for subtype-specific inhibition of the P2X7 receptor
Karasawa, A., & Kawate, T. (2016) · eLife · doi:10.7554/elife.22153 · Cited by 322
Vesicular and conductive mechanisms of nucleotide release
Lazarowski, E. R. (2012) · Purinergic Signalling · doi:10.1007/s11302-012-9304-9 · Cited by 314
Autocrine regulation of T‐cell activation by ATP release and P2X 7 receptors
Yip, L., Woehrle, T., Corriden, R., Hirsh, M., Chen, Y., Inoue, Y., Ferrari, V., Insel, P. A., & JUNGER, W. G. (2009) · The FASEB Journal · doi:10.1096/fj.08-126458 · Cited by 303
Yegutkin, G. G. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2014.953627 · Cited by 299
A Novel Recombinant Plasma Membrane-targeted Luciferase Reveals a New Pathway for ATP Secretion
Pellegatti, P., Falzoni, S., Pinton, P., Rizzuto, R., & Virgilio, F. D. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-03-0222 · Cited by 296
Activation of Microglia by Amyloid β Requires P2X7 Receptor Expression
Sanz, J. M., Chiozzi, P., Ferrari, D., Colaianna, M., Idzko, M., Falzoni, S., Fellin, R., Trabace, L., & Di Virgilio, F. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803612 · Cited by 293
Ferrari, D., Wesselborg, S., Bauer, M. K. A., & Schulze‐Osthoff, K. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.7.1635 · Cited by 286
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. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00233.x · Cited by 271
North, R. A., & Jarvis, M. F. (2012) · Molecular Pharmacology · doi:10.1124/mol.112.083758 · Cited by 271
X-ray structures define human P2X3 receptor gating cycle and antagonist action
Mansoor, S., Lü, W., Oosterheert, W., Shekhar, M., Tajkhorshid, E., & Gouaux, E. (2016) · Nature · doi:10.1038/nature19367 · Cited by 269
Medicinal chemistry of adenosine, P2Y and P2X receptors
Jacobson, K. A., & Müller, C. E. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.12.001 · Cited by 262
Trophic activity of a naturally occurring truncated isoform of the P2X7 receptor
Adinolfi, E., Cirillo, M., Woltersdorf, R., Falzoni, S., Chiozzi, P., Pellegatti, P., Callegari, M. G., Sandonà, D., Markwárdt, F., Schmalzing, G., et al. (2010) · The FASEB Journal · doi:10.1096/fj.09-153601 · Cited by 254
Self-citationFalzoni, S., Munerati, M., Ferrari, D., Spisani, S., Moretti, S., & Virgilio, F. D. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117770 · Cited by 249
Evidence for Functional P2X4/P2X7 Heteromeric Receptors
Guo, C. Y., Masin, M., Qureshi, O. S., & Murrell‐Lagnado, R. D. (2007) · Molecular Pharmacology · doi:10.1124/mol.107.035980 · Cited by 239
Sluyter, R. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/5584_2017_59 · Cited by 235
Extracellular ATP acts as a damage-associated molecular pattern (DAMP) signal in plants
Tanaka, K., Choi, J., Cao, Y., & Stacey, G. S. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00446 · Cited by 229
Nucleoside reverse transcriptase inhibitors possess intrinsic anti-inflammatory activity
Fowler, B. J., Gelfand, B. D., Kim, Y., Kerur, N., Tarallo, V., Hirano, Y., Amarnath, S., Fowler, D. H., Radwan, M., Young, M. T., et al. (2014) · Science · doi:10.1126/science.1261754 · Cited by 225
The P2X7 receptor directly interacts with the NLRP3 inflammasome scaffold protein
Franceschini, A., Capece, M., Chiozzi, P., Falzoni, S., Sanz, J. M., Sarti, A. C., Bonora, M., Pinton, P., & Di Virgilio, F. (2015) · The FASEB Journal · doi:10.1096/fj.14-268714 · Cited by 225
K+ regulates Ca2+ to drive inflammasome signaling: dynamic visualization of ion flux in live cells
Yaron, J. R., Gangaraju, S., Rao, M. Y., Kong, X., Zhang, L., Su, F., Tian, Y., Glenn, H. L., & Meldrum, D. R. (2015) · Cell Death & Disease · doi:10.1038/cddis.2015.277 · Cited by 212 · cited 1×
“Reactive oxygen species (ROS) formation may also play a role in inducing inflammasome aggregation and IL-1β secretion downstream to P2X7R activation [110-113].”
Bhattacharya, A., Wang, Q., Ao, H., Shoblock, J. R., Lord, B., Aluisio, L. E., Fraser, I. C., Nepomuceno, D. H., Neff, R. A., Welty, N., et al. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12314 · Cited by 204
Amoroso, F., Capece, M., Rotondò, A., Cangelosi, D., Ferracin, M., Franceschini, A., Raffaghello, L., Pistoia, V., Varesio, L., & Adinolfi, E. (2015) · Oncogene · doi:10.1038/onc.2014.444 · Cited by 194
Self-citationZhao, J., Wang, H., Dai, C., Wang, H., Zhang, H., Huang, Y., Wang, S., Gaskin, F., Yang, N., & Fu, S. M. (2013) · Arthritis & Rheumatism · doi:10.1002/art.38174 · Cited by 192
The isoquinoline derivative KN‐62 a potent antagonist of the P2Z‐receptor of human lymphocytes
Gargett, C. E., & Wiley, J. S. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0701081 · Cited by 191
Nanobodies that block gating of the P2X7 ion channel ameliorate inflammation
Danquah, W., Meyer‐Schwesinger, C., Rissiek, B., Pinto, C., Prat, A. S., Amadi, M., Iacenda, D., Knop, J., Hammel, A., Bergmann, P., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf8463 · Cited by 191
North, R. A. (2016) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2015.0427 · Cited by 191
An ATP-activated channel is involved in mitogenic stimulation of human T lymphocytes
Baricordi, O., Ferrari, D., Melchiorri, L., Chiozzi, P., Hanau, S., Chiari, E., Rubini, M., & Virgilio, F. D. (1996) · Blood · doi:10.1182/blood.v87.2.682.bloodjournal872682 · Cited by 185
Epithelial Membrane Proteins Induce Membrane Blebbing and Interact with the P2X7 Receptor C Terminus
Wilson, H. L., Wilson, S. A., Surprenant, A., & North, R. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205120200 · Cited by 181
Neuronal P2X7 Receptors Revisited: Do They Really Exist?
Illes, P., Khan, T. M., & Rubini, P. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.3103-16.2017 · Cited by 179
Hung, S.-C., Choi, C. H., Sadier, N. S., Johnson, L., Atanasova, K. R., Sellami, H., Yilmaz, Ö., & Ojcius, D. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070210 · Cited by 176
Virgilio, F. D., Bronte, V., Collavo, D., & Zanovello, P. (1989) · The Journal of Immunology · doi:10.4049/jimmunol.143.6.1955 · Cited by 175
Recent insights into the molecular mechanisms of the NLRP3 inflammasome activation
Próchnicki, T., Mangan, M., & Latz, E. (2016) · F1000Research · doi:10.12688/f1000research.8614.1 · Cited by 174
Tafani, M., Schito, L., Pellegrini, L., Villanova, L., Marfè, G., Anwar, T., Rosa, R., Indelicato, M., Fini, M., Pucci, B., et al. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr101 · Cited by 172
The Therapeutic Potential of Modifying Inflammasomes and NOD-Like Receptors
Virgilio, F. D. (2013) · Pharmacological Reviews · doi:10.1124/pr.112.006171 · Cited by 168
Tomasinsig, L., Pizzirani, C., Skerlavaj, B., Pellegatti, P., Gulinelli, S., Tossi, A., Virgilio, F. D., & Zanetti, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802185200 · Cited by 158
Inhibition of Chlamydial Infectious Activity due to P2X7R-Dependent Phospholipase D Activation
Coutinho‐Silva, R., Welter-Stahl, L., Raymond, M., Jungas, T., Verbeke, P., Burnstock, G., Darville, T. L., & Ojcius, D. M. (2003) · Immunity · doi:10.1016/s1074-7613(03)00235-8 · Cited by 157
The P2X7 receptor is a key modulator of aerobic glycolysis
Amoroso, F., Falzoni, S., Adinolfi, E., Ferrari, D., & Virgilio, F. D. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.105 · Cited by 157
Self-citationThe microbial and danger signals that activate Nod-like receptors
Benkő, S., Philpott, D. J., & Girardin, S. E. (2008) · Cytokine · doi:10.1016/j.cyto.2008.07.013 · Cited by 156
P2X7/P2Z Purinoreceptor-mediated Activation of Transcription Factor NFAT in Microglial Cells
Ferrari, D., Stroh, C., & Schulze‐Osthoff, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13205 · Cited by 156
Neuronal P2X7 Receptor: Involvement in Neuronal Physiology and Pathology
Miras‐Portugal, M. T., Sebastián‐Serrano, Á., García, L. D. D., & Dı́az-Hernández, M. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.3104-16.2017 · Cited by 154
El-Moatassim, C., & Dubyak, G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35890-3 · Cited by 153
P2X7 receptor‐stimulation causes fever via PGE2 and IL‐1β release
Barberà‐Cremades, M., Baroja‐Mazo, A., Gomez, A. I., Machado, F., Di Virgilio, F., & Pelegrín, P. (2012) · The FASEB Journal · doi:10.1096/fj.12-205765 · Cited by 142
Extracellular Nucleotides Act Through P2X7 Receptors to Activate NF-κB in Osteoclasts
Korčok, J., Raimundo, L., Ke, H. Z., Sims, S. M., & Dixon, S. J. (2004) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.040108 · Cited by 138
Territo, P. R., Meyer, J. A., Peters, J. S., Riley, A. K., McCarthy, B. P., Gao, M., Wang, M., Green, M. A., Zheng, Q., & Hutchins, G. D. (2016) · Journal of Nuclear Medicine · doi:10.2967/jnumed.116.181354 · Cited by 138
Gicquel, T., Robert, S., Loyer, P., Victoni, T., Bodin, A., Ribault, C., Gléonnec, F., Couillin, I., Boichot, E., & Lagente, V. (2015) · The FASEB Journal · doi:10.1096/fj.14-267393 · Cited by 133
Lees, M. P., Fuller, S. J., McLeod, R. L., Boulter, N. R., Miller, C., Zakrzewski, A. M., Mui, E. J., Witola, W. H., Coyne, J. J., Hargrave, A. C., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000012 · Cited by 132
Lee, H. G., Won, S. M., Gwag, B. J., & Lee, Y. B. (2011) · Experimental & Molecular Medicine · doi:10.3858/emm.2011.43.1.001 · Cited by 122
Oxidized ATP (oATP) attenuates proinflammatory signaling via P2 receptor‐independent mechanisms
Beigi, R. D., Kertesy, S. B., Aquilina, G. R., & Dubyak, G. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705470 · Cited by 120
Apolloni, S., Amadio, S., Parisi, C., Matteucci, A., Potenza, R. L., Armida, M., Popoli, P., D’Ambrosi, N., & Volonté, C. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.017038 · Cited by 119
The P2X7 Receptor is an Important Regulator of Extracellular ATP Levels
Brandao‐Burch, A., Key, M. L., Patel, J. J., Arnett, T. R., & Orriss, I. R. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00041 · Cited by 117
P2X7 Receptor as a Therapeutic Target
Marchi, E. D., Orioli, E., Ben, D. D., & Adinolfi, E. (2016) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2015.11.004 · Cited by 117
Self-citationCaspase-1–mediated pathway promotes generation of thromboinflammatory microparticles
Rothmeier, A. S., Marchese, P., Petrich, B. G., Furlan-Freguia, C., Ginsberg, M. H., Ruggeri, Z. M., & Ruf, W. (2015) · Journal of Clinical Investigation · doi:10.1172/jci79329 · Cited by 111
Nylander, S., & Schulz, R. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13429 · Cited by 110
Apolloni, S., Amadio, S., Montilli, C., Volonte, C., & D'Ambrosi, N. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt259 · Cited by 109
Long-Term Heart Transplant Survival by Targeting the Ionotropic Purinergic Receptor P2X7
Vergani, A., Tezza, S., D’Addio, F., Fotino, C., Liu, K., Niewczas, M. A., Bassi, R., Molano, R. D., Kleffel, S., Petrelli, A., et al. (2012) · Circulation · doi:10.1161/circulationaha.112.123653 · Cited by 108
Adinolfi, E., Callegari, M. G., Cirillo, M., Pinton, P., Giorgi, C., Cavagna, D., Rizzuto, R., & Virgilio, F. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805805200 · Cited by 107
Self-citationHill, L. M., Gavala, M. L., Lenertz, L. Y., & Bertics, P. J. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1001298 · Cited by 107
Adinolfi, E., Kim, M., Young, M. T., Virgilio, F. D., & Surprenant, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301508200 · Cited by 104
Self-citationGilbert, S. M., Baird, A. G., Glazer, S., Barden, J. A., Glazer, A., Teh, L. C., & King, J. (2017) · British Journal of Dermatology · doi:10.1111/bjd.15364 · Cited by 104
Lee, B. H., Hwang, D. M., Palaniyar, N., Grinstein, S., Philpott, D. J., & Hu, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035812 · Cited by 102
Gene structure and chromosomal localization of the human P2X7 receptor.
Buell, G. N., Talabot, F., Gos, A., Lorenz, J., Lai, E., Morris, M. A., & Antonarakis, S. E. (1998) · PubMed · Cited by 101
Chang, X., He, H., Zhu, L., Gao, J., Wei, T., Zhan-qian, M., & Yan, T. (2015) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2015.04.021 · Cited by 100
Amaral, E. P., Ribeiro, S. C. M., Lanes, V. R., Almeida, F. M., de Andrade, M. R. M., Bomfim, C. C. B., de Salles, É. M., Bortoluci, K. R., Coutinho‐Silva, R., Hirata, M. H., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004188 · Cited by 99
Orioli, E., Marchi, E. D., Giuliani, A. L., & Adinolfi, E. (2017) · Current Medicinal Chemistry · doi:10.2174/0929867324666170303161659 · Cited by 99
Self-citationCorrêa, G., Marques-da-Silva, C., Moreira-Souza, A. C. A., Vommaro, R. C., & Coutinho‐Silva, R. (2010) · Microbes and Infection · doi:10.1016/j.micinf.2010.03.004 · Cited by 98
Trophic Activity of Human P2X7 Receptor Isoforms A and B in Osteosarcoma
Giuliani, A. L., Colognesi, D., Ricco, T., Roncato, C., Capece, M., Amoroso, F., Wang, Q., Marchi, E. D., Gartland, A., Virgilio, F. D., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107224 · Cited by 97
Self-citationAlves, L. A., Soares‐Bezerra, R. J., Faria, R. X., Ferreira, L., & Frutuoso, V. D. S. (2013) · Molecules · doi:10.3390/molecules180910953 · Cited by 97
Purinergic mechanism in the immune system: A signal of danger for dendritic cells
Virgilio, F. D. (2005) · Purinergic Signalling · doi:10.1007/s11302-005-6312-z · Cited by 96
Ory, D., Celen, S., Gijsbers, R., den Haute, C. V., Postnov, A. A., Koole, M. J. B., Vandeputte, C., Andrés, J.-I., Alcázar, J., Angelis, M. D., et al. (2016) · Journal of Nuclear Medicine · doi:10.2967/jnumed.115.169995 · Cited by 96
Effect of P2Y12 inhibitors on inflammation and immunity
Storey, R. F., & Thomas, M. (2015) · Thrombosis and Haemostasis · doi:10.1160/th14-12-1068 · Cited by 95
Baldini, C., Rossi, C., Ferro, F., Santini, E., Seccia, V., Donati, V. L., & Solini, A. (2013) · Journal of Internal Medicine · doi:10.1111/joim.12115 · Cited by 93
Pyroptosis: Caspase-11 Unlocks the Gates of Death
Gassart, A. D., & Martinon, F. (2015) · Immunity · doi:10.1016/j.immuni.2015.10.024 · Cited by 92
The Antibiotic Polymyxin B Modulates P2X7 Receptor Function
Ferrari, D., Pizzirani, C., Adinolfi, E., Forchap, S., Sitta, B., Turchet, L., Falzoni, S., Minelli, M., Baricordi, R., & Virgilio, F. D. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.7.4652 · Cited by 91
Self-citationP2X7 as a new target for chrysophanol to treat lipopolysaccharide-induced depression in mice
Zhang, K., Liu, J., You, X., Kong, P., Song, Y., Cao, L., Yang, S. T., Wang, W., Fu, Q., & Ma, Z. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.12.043 · Cited by 90
Turner, C. M., Tam, F. W. K., Lai, P., Tarzi, R. M., Burnstock, G., Pusey, C. D., Cook, H. T., & Unwin, R. J. (2006) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfl589 · Cited by 89
Chaves, S. P., Torres-Santos, E. C., Marques, C. F. D. O., Figliuolo, V. R., Persechini, P. M., Coutinho‐Silva, R., & Rossi‐Bergmann, B. (2009) · Microbes and Infection · doi:10.1016/j.micinf.2009.05.001 · Cited by 87
Effect of the Purinergic Inhibitor Oxidized ATP in a Model of Islet Allograft Rejection
Vergani, A., Fotino, C., D’Addio, F., Tezza, S., Podetta, M., Gatti, F., Chin, M., Bassi, R., Molano, R. D., Corradi, D., et al. (2013) · Diabetes · doi:10.2337/db12-0242 · Cited by 87
Allsopp, R. C., Dayl, S. A., Schmid, R., & Evans, R. J. (2017) · Scientific Reports · doi:10.1038/s41598-017-00732-5 · Cited by 87
P2X Receptors and Inflammation
Virgilio, F. D. (2015) · Current Medicinal Chemistry · doi:10.2174/0929867322666141210155311 · Cited by 81
The role of p2x7 receptor in infectious inflammatory diseases and the influence of ectonucleotidases
Coutinho-Silva, R., Morandini, A., & Savio, L. B. (2014) · Biomedical Journal · doi:10.4103/2319-4170.127803 · Cited by 81
Prophylactic systemic P2X7 receptor blockade prevents experimental colitis
Marques, C. C., Castelo-Branco, M. T., Pacheco, R. G., Buongusto, F., do Rosário, A., Schanaider, A., Coutinho-Silva, R., & de Souza, H. S. P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.012 · Cited by 78
Graziano, F., Desdouits, M., Garzetti, L., Podini, P., Alfano, M., Rubartelli, A., Furlan, R., Benaroch, P., & Poli, G. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500656112 · Cited by 77
Dysfunctional inflammasome in Schnitzler's syndrome
Pizzirani, C., Falzoni, S., Govoni, M., Corte, R. L., Donadei, S., Virgilio, F. D., Trotta, F., & Monaco, A. L. (2009) · Lara D. Veeken · doi:10.1093/rheumatology/kep222 · Cited by 77
Gómez‐Villafuertes, R., del Puerto, A., Dı́az-Hernández, M., Bustillo, D., Díaz‐Hernandéz, J. I., Huerta, P. G., Artalejo, A. R., Garrido, J. J., & Miras‐Portugal, M. T. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07228.x · Cited by 75
Abdi, M. H., Beswick, P., Billinton, A., Chambers, L. J., Charlton, A., Collins, S. D., Collis, K. L., Dean, D. K., Fonfría, E., Gleave, R. J., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.07.033 · Cited by 74
Pharmacology of a Novel Central Nervous System–Penetrant P2X7 Antagonist JNJ-42253432
Lord, B., Aluisio, L. E., Shoblock, J. R., Neff, R. A., Varlinskaya, E. I., Ceusters, M., Lovenberg, T. W., Carruthers, N. I., Bonaventure, P., Letavic, M. A., et al. (2014) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.218487 · Cited by 73
Lenertz, L. Y., Gavala, M. L., Zhu, Y., & Bertics, P. J. (2011) · Immunologic Research · doi:10.1007/s12026-011-8203-4 · Cited by 71
Involvement of the Purinergic P2X7 Receptor in the Formation of Multinucleated Giant Cells
Lemaire, I. B., Falzoni, S., Leduc, N., Zhang, B., Pellegatti, P., Adinolfi, E., Chiozzi, P., & Virgilio, F. D. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.10.7257 · Cited by 71
Self-citationToki, Y., Takenouchi, T., Harada, H., Tanuma, S., Kitani, H., Kojima, S., & Tsukimoto, M. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.011 · Cited by 70
P2X7 blockade attenuates mouse liver fibrosis
Huang, C., Yu, W., Cui, H., WANG, Y., Zhang, L., Han, F., & Huang, T. (2013) · Molecular Medicine Reports · doi:10.3892/mmr.2013.1807 · Cited by 68
de Salles, É. M., de Menezes, M. N., Siqueira, R., da Silva, H. B., Amaral, E. P., Castillo-Méndez, S. I., Cunha, I., Cassado, A. D. A., Vieira, F. S., Olivieri, D. N., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006595 · Cited by 68
P2X7 receptor positively regulates MyD88-dependent NF-κB activation
Liu, Y., Xiao, Y., & Li, Z. (2011) · Cytokine · doi:10.1016/j.cyto.2011.05.003 · Cited by 67
Darville, T. L., Welter-Stahl, L., da Cruz, C. M., Sater, A. A. A., Andrews, C. W., & Ojcius, D. M. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.6.3707 · Cited by 63
Dendritic Cell IL-1α and IL-1β Are Polyubiquitinated and Degraded by the Proteasome
Ainscough, J. S., Gerberick, G. F., Zahedi-Nejad, M., López‐Castejón, G., Brough, D., Kimber, I., & Dearman, R. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.595686 · Cited by 63
Fantoni, E., Ben, D. D., Falzoni, S., Virgilio, F. D., Lovestone, S., & Gee, A. D. (2017) · EJNMMI Research · doi:10.1186/s13550-017-0275-2 · Cited by 63
Emerging Roles of P2X Receptors in Cancer
Adinolfi, E., Capece, M., Amoroso, F., Marchi, E. D., & Franceschini, A. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666141012172913 · Cited by 62
Self-citationInvolvement of the P2X7-NLRP3 axis in leukemic cell proliferation and death
Salaro, E., Rambaldi, A., Falzoni, S., Amoroso, F., Franceschini, A., Sarti, A. C., Bonora, M., Cavazzini, F., Rigolin, G. M., Ciccone, M., et al. (2016) · Scientific Reports · doi:10.1038/srep26280 · Cited by 59
Taylor, J. M., & Han, Z. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015784 · Cited by 57
Yu, T., JUNGER, W. G., Yuan, C., Jin, A., Zhao, Y. D., Zheng, X., Zeng, Y., & Liu, J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00342.2009 · Cited by 56
Liao, Y.-H., Lin, Y.-C., Tsao, S.-T., Lin, Y., Yang, A.-J., Huang, C.-T., Huang, K., & Lin, W. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0812409 · Cited by 56
P2 receptors in cancer progression and metastatic spreading
Virgilio, F. D., Falzoni, S., Giuliani, A. L., & Adinolfi, E. (2016) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2016.05.001 · Cited by 56
Self-citationBridging hypoxia, inflammation and estrogen receptors in thyroid cancer progression
Tafani, M., Santis, E. D., Coppola, L., Perrone, G. A., Carnevale, I., Russo, A., Pucci, B., Carpi, A., Bizzarri, M., & Russo, M. A. (2013) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2013.10.013 · Cited by 54
Helliwell, R. M., ShioukHuey, C. O., Dhuna, K., Molero, J. C., Ye, J. M., Xue, C. C., & Stokes, L. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13123 · Cited by 47
Exogenous ATP enhances calcium influx in intact thymocytes.
Lin, J. H.-C., Krishnaraj, R., & Kemp, R. G. (1985) · The Journal of Immunology · doi:10.4049/jimmunol.135.5.3403 · Cited by 45
Portales‐Cervantes, L., Niño-Moreno, P., Salgado‐Bustamante, M., García-Hernández, M. H., Baranda-Candido, L., Reynaga-Hernández, E., Barajas‐López, C., González‐Amaro, R., & Portales‐Pérez, D. P. (2012) · Cellular Immunology · doi:10.1016/j.cellimm.2012.05.005 · Cited by 44
Mizutani, T., Fowler, B. J., Kim, Y., Yasuma, R., Krueger, L. A., Gelfand, B. D., & Ambati, J. (2015) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.15-17440 · Cited by 44
P2X7 receptor gene polymorphism analysis in rheumatoid arthritis
Al-Shukaili, A. K., Alkaabi, J., Hassan, B., Al‐Araimi, T., Tobi, M. A., Al-Kindi, M., Al-Maniri, A., Al-Gheilani, A., & Al-Ansari, A. (2011) · International Journal of Immunogenetics · doi:10.1111/j.1744-313x.2011.01019.x · Cited by 43
Al-Shukaili, A. K., Alkaabi, J., & Hassan, B. (2007) · Inflammation · doi:10.1007/s10753-007-9052-0 · Cited by 43
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Adinolfi, E., Amoroso, F., & Giuliani, A. L. (2012) · Journal of Osteoporosis · doi:10.1155/2012/637863 · Cited by 42
Self-citationComparative study of the P2X gene family in animals and plants
Hou, Z., & Cao, J. W. (2016) · Purinergic Signalling · doi:10.1007/s11302-016-9501-z · Cited by 41
Corrêa, G., Lindenberg, C. D. A., Fernandes-Santos, C., Gandini, M., de Paiva, F. P., Coutinho‐Silva, R., & Kubelka, C. F. (2016) · Immunobiology · doi:10.1016/j.imbio.2016.02.003 · Cited by 40
Chotjumlong, P., Bolscher, J. G. M., Nazmi, K., Reutrakul, V., Supanchart, C., Buranaphatthana, W., & Krisanaprakornkit, S. (2012) · Journal of Innate Immunity · doi:10.1159/000342928 · Cited by 38
Swanson, D. M., Savall, B. M., Coe, K. J., Schoetens, F., Koudriakova, T. B., Skaptason, J., Wall, J. L., Rech, J. C., Deng, X., Angelis, M. D., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00989 · Cited by 38
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Virgilio, F. D., & Giuliani, A. L. (2016) · Biomedical Journal · doi:10.1016/j.bj.2016.08.006 · Cited by 38
Self-citationWan, M., Soehnlein, O., Tang, X. Y., van der Does, A. M., Smedler, E., Uhlén, P., Lindbom, L., Agerberth, B., & Haeggström, J. Z. (2014) · The FASEB Journal · doi:10.1096/fj.14-251306 · Cited by 37
Figliuolo, V. R., Chaves, S. P., Savio, L. E. B., Thorstenberg, M. L., de Salles, É. M., Takiya, C. M., Lima, M. R. D., Guedes, H. L. D. M., Rossi‐Bergmann, B., & Coutinho‐Silva, R. (2016) · Purinergic Signalling · doi:10.1007/s11302-016-9544-1 · Cited by 37
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King, B. F. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707266 · Cited by 36
Anrather, J., Gallo, E. F., Kawano, T., Orio, M., Abe, T., Gooden, C., Zhou, P., & Iadecola, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025916 · Cited by 36
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Menkova, I., Hocini, H., Foucat, E., Tisserand, P., Bourdery, L., Delaugerre, C., Benne, C., Lévy, Y., & Lelièvre, J. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005571 · Cited by 31
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Dubyak, G., Cowen, D. S., & Lazarus, H. M. (1988) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1988.tb22339.x · Cited by 19
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Metadata
- Authors
- Adinolfi, E., Giuliani, A. L., De Marchi, E., Pegoraro, A., Orioli, E., & Di Virgilio, F.
- Affiliations
- University of Ferrara (IT)
- Venue
- Biochemical Pharmacology
- Publisher
- Elsevier BV
- Published
- 2018-05
- Volume
- 151
- Pages
- 234-244
- ISSN
- 0006-2952 (ISSN-L)
- OpenAlex
- W2779261291
- Cited by
- 385
- References
- 181
- Citations by year
- 2026: 35 · 2025: 40 · 2024: 43 · 2023: 54 · 2022: 61 · 2021: 60 · 2020: 46 · 2019: 26 · 2018: 20
- FWCI
- 2.65
- Type
- journal article
- Language
- en
- Open access
- Licence
- cc-by-nc-nd
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- Locations
- Biochemical Pharmacology (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System University of Ferrara (University of Ferrara) (submittedVersion, cc-by-nc-nd)
- Funders
- Italian Association for Cancer Research (IG 13025, IG 18581)
- Ministry of Health of Italy (RF-2011-02348435)
- University of Ferrara
- AIRC (IG 16812)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Adenosine and Purinergic Signaling
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Keywords
- P2X7 receptor, extracellular ATP, damage-associated molecular patterns, sepsis, sterile inflammation, Mycobacterium, Plasmodium, HIV-1, NLRP3 inflammasome, NF-kB, NFAT, GSK3β, vascular endothelial growth factor, chronic disease, P2X7 receptor antagonists, innate immunity
- MeSH terms
- Animals, Autoimmune Diseases, Chronic Disease, Clinical Trials as Topic, Communicable Diseases, Drug Evaluation, Preclinical, Humans, Inflammation, Neoplasms, Neurodegenerative Diseases, Receptors, Purinergic P2X7, Inflammasomes, Purinergic P2X Receptor Agonists, Purinergic P2X Receptor Antagonists
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