References
- Jackson SP, Darbousset R, Schoenwaelder SM. Thromboinflammation: challenges of therapeutically targeting coagulation and other host defense mechanisms. Blood 2019;133:906–918. doi:https://doi.org/10.1182/blood-2018-11-882993.
- Palacios-Acedo AL, Mège D, Crescence L, Dignat-George F, Dubois C, Panicot-Dubois L. Platelets, thrombo-inflammation, and cancer: collaborating with the enemy. Front Immunol 2019;10:1805. https://www.frontiersin.org/article/https://doi.org/10.3389/fimmu.2019.01805
- Peter L. Inflammation in atherosclerosis. Arterioscler Thromb Vasc Biol 2012;32:2045–2051. doi:https://doi.org/10.1161/ATVBAHA.108.179705.
- Lorenzatti AJ, Servato ML. New evidence on the role of inflammation in CVD risk. Curr Opin Cardiol 2019;34:418–423. https://journals.lww.com/co-cardiology/Fulltext/2019/07000/New_evidence_on_the_role_of_inflammation_in_CVD.17.aspx
- Rayes J, Bourne JH, Brill A, Watson SP. The dual role of platelet-innate immune cell interactions in thrombo-inflammation. Res Pract Thromb Haemost 2020;4:23–35. doi:https://doi.org/10.1002/rth2.12266.
- Burnstock G. Purine and purinergic receptors. Brain Neurosci Adv 2018;2:2398212818817494. doi:https://doi.org/10.1177/2398212818817494.
- North RA. P2X receptors. Philos Trans R Soc Lond B Biol Sci 2016;371:20150427. doi:https://doi.org/10.1098/rstb.2015.0427.
- Burnstock G. Dual control of local blood flow by purinesa. Ann N Y Acad Sci 1990;603:31–44. doi:https://doi.org/10.1111/j.1749-6632.1990.tb37659.x.
- Mahaut-Smith MP, Jones S, Evans RJ. The P2X1 receptor and platelet function. Purinergic Signal 2011;7:341–356. doi:https://doi.org/10.1007/s11302-011-9224-0.
- Chvatchko Y, Valera S, Aubry J-P, Renno T, Buell G, Bonnefoy J-Y. The involvement of an ATP-gated ion channel, P2X1, in thymocyte apoptosis. Immunity 1996;5:275–283. doi:https://doi.org/10.1016/S1074-7613(00)80322-2.
- Lecut C, Frederix K, Johnson DM, Deroanne C, Thiry M, Faccinetto C, Marée R, Evans RJ, Volders PGA, Bours V, et al. P2X1 ion channels promote neutrophil chemotaxis through Rho Kinase activation. J Immunol 2009;183:2801–2809. doi:https://doi.org/10.4049/jimmunol.0804007.
- Fryatt AG, Dayl S, Stavrou A, Schmid R, Evans RJ. Organization of ATP-gated P2X1 receptor intracellular termini in apo and desensitized states. J Gen Physiol 2019;151:146–155. doi:https://doi.org/10.1085/jgp.201812108.
- Roberts JA, Allsopp RC, El Ajouz S, Vial C, Schmid R, Young MT, Evans RJ. Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel. Proc Natl Acad Sci 2012;109: 4663LP - 4667. doi:https://doi.org/10.1073/pnas.1201872109.
- Idzko M, Ferrari D, Eltzschig HK. Nucleotide signalling during inflammation. Nature 2014;509:310–317. doi:https://doi.org/10.1038/nature13085.
- Vénéreau E, Ceriotti C, Bianchi M. DAMPs from cell death to new life. Front Immunol 2015;6:422. doi:https://doi.org/10.3389/fimmu.2015.00422.
- Trautmann A. Extracellular ATP in the immune system: more than just a “Danger Signal”. Sci Signal 2009;2: pe6 LP-pe6. doi:https://doi.org/10.1126/scisignal.256pe6.
- Amores-Iniesta J, Barberà-Cremades M, Martínez CM, Pons JA, Revilla-Nuin B, Martínez-Alarcón L, Di Virgilio F, Parrilla P, Baroja-Mazo A, Pelegrín P. Extracellular ATP activates the NLRP3 inflammasome and is an early danger signal of skin allograft rejection. Cell Rep 2017;21:3414–3426. doi:https://doi.org/10.1016/j.celrep.2017.11.079.
- Chen Y, Corriden R, Inoue Y, Yip L, Hashiguchi N, Zinkernagel A, Nizet V, Insel PA, Junger WG. ATP release guides neutrophil chemotaxis via P2Y2 and A3 receptors. Science 2006;314: 1792LP - 1795. doi:https://doi.org/10.1126/science.1132559.
- Boada-Romero E, Martinez J, Heckmann BL, Green DR. The clearance of dead cells by efferocytosis. Nat Rev Mol Cell Biol 2020;21:398–414. doi:https://doi.org/10.1038/s41580-020-0232-1.
- Antonioli L, Pacher P, Vizi ES, Haskó G. CD39 and CD73 in immunity and inflammation. Trends Mol Med 2013;19:355–367. doi:https://doi.org/10.1016/j.molmed.2013.03.005.
- Maître B, Magnenat S, Heim V, Ravanat C, Evans RJ, de la Salle H, Gachet C, Hechler B. The P2X1 receptor is required for neutrophil extravasation during lipopolysaccharide-induced lethal endotoxemia in mice. J Immunol 2015;194: 739LP - 749. doi:https://doi.org/10.4049/jimmunol.1401786.
- Lecut C, Faccinetto C, Delierneux C, van Oerle R, Spronk HMH, Evans RJ, El Benna J, Bours V, Oury C. ATP-gated P2X 1 ion channels protect against endotoxemia by dampening neutrophil activation. J Thromb Haemost 2012;10:453–465. doi:https://doi.org/10.1111/j.1538-7836.2011.04606.x.
- El Mdawar M-B, Maître B, Magnenat S, Gachet C, Hechler B, de la Salle H. The ATP-gated P2X1 ion channel contributes to the severity of antibody-mediated transfusion-related acute lung injury in mice. Sci Rep 2019;9:5159. doi:https://doi.org/10.1038/s41598-019-41742-9.
- Looney MR, Nguyen JX, Hu Y, van Ziffle JA, Lowell CA, Matthay MA. Platelet depletion and aspirin treatment protect mice in a two-event model of transfusion-related acute lung injury. J Clin Invest 2009;119:3450–3461. doi:https://doi.org/10.1172/JCI38432.
- Caudrillier A, Kessenbrock K, Gilliss BM, Nguyen JX, Marques MB, Monestier M, Toy P, Werb Z, Looney MR. Platelets induce neutrophil extracellular traps in transfusion-related acute lung injury. J Clin Invest 2012;122:2661–2671. doi:https://doi.org/10.1172/JCI61303.
- Tariket S, Hamzeh-Cognasse H, Laradi S, Arthaud C-A, Eyraud M-A, Bourlet T, Berthelot P, Garraud O, Cognasse F. Evidence of CD40L/CD40 pathway involvement in experimental transfusion-related acute lung injury. Sci Rep 2019;9:12536. doi:https://doi.org/10.1038/s41598-019-49040-0.
- Hechler B, Magnenat S, Zighetti ML. Inhibition of platelet functions and thrombosis through selective or nonselective inhibition of the platelet P2 receptors with increasing doses of NF449 [4,4′,4″,4″′-(Carbonylbis(imino-5,1,3-benzenetriylbis-(carbonylimino)))tetrakis-benzene-1,3-disulfonic acid octasodium salt]. J Pharmacol Exp Ther 2005;314: 232LP - 243. doi:https://doi.org/10.1124/jpet.105.084673.
- López-López C, Jaramillo-Polanco J, Portales-Pérez DP, Gómez-Coronado KS, Rodríguez-Meléndez JG, Cortés-García JD, Espinosa-Luna R, Montaño LM, Barajas-López C. Two P2X1 receptor transcripts able to form functional channels are present in most human monocytes. Eur J Pharmacol 2016;793:82–88. doi:https://doi.org/10.1016/j.ejphar.2016.10.033.
- Hoylaerts MF, Oury C, Toth-Zsamboki E, Vermylen J. ADP receptors in platelet activation and aggregation. Platelets 2000;11:307–309. doi:https://doi.org/10.1080/09537100050144713.
- Oury C, Toth-Zsamboki E, Thys C, Tytgat J, Vermylen J, Hoylaerts M. The ATP-gated P2X1 ion channel acts as a positive regulator of platelet responses to collagen. Thromb Haemost 2001;86:1264–1271. doi:https://doi.org/10.1055/s-0037-1616060.
- Oury C, Toth-Zsamboki E, Vermylen J, Hoylaerts MF. P2X1-mediated activation of extracellular signal-regulated kinase 2 contributes to platelet secretion and aggregation induced by collagen. Blood 2002;100:2499–2505. doi:https://doi.org/10.1182/blood-2002-03-0812.
- Fung CYE, Cendana C, Farndale RW, Mahaut-Smith MP. Primary and secondary agonists can use P2X(1) receptors as a major pathway to increase intracellular Ca(2+) in the human platelet. J Thromb Haemost 2007;5:910–917. doi:https://doi.org/10.1111/j.1538-7836.2007.02525.x.
- Erhardt JA, Toomey JR, Douglas SA, Johns DG. P2X1 stimulation promotes thrombin receptor-mediated platelet aggregation. J Thromb Haemost 2006;4:882–890. doi:https://doi.org/10.1111/j.1538-7836.2006.01849.x.
- Fung CYE, Jones S, Ntrakwah A, Naseem KM, Farndale RW, Mahaut-Smith MP. Platelet Ca2+ responses coupled to glycoprotein VI and Toll-like receptors persist in the presence of endothelial-derived inhibitors: roles for secondary activation of P2X1 receptors and release from intracellular Ca2+ stores. Blood 2012;119:3613–3621. doi:https://doi.org/10.1182/blood-2011-10-386052.
- Hechler B, Lenain N, Marchese P, Vial C, Heim V, Freund M, Cazenave J-P, Cattaneo M, Ruggeri ZM, Evans R, et al. A role of the fast ATP-gated P2X1 cation channel in thrombosis of small arteries in vivo. J Exp Med 2003;198:661–667. doi:https://doi.org/10.1084/jem.20030144.
- Oury C, Daenens K, Hu H, Toth-Zsamboki E, Bryckaerth M, Hoylaerts MF. ERK2 activation in arteriolar and venular murine thrombosis: platelet receptor GPIb vs. P2X1. J Thromb Haemost 2006;4:443–452. doi:https://doi.org/10.1111/j.1538-7836.2006.01745.x.
- Oury C, Kuijpers MJE, Toth-Zsamboki E, Bonnefoy A, Danloy S, Vreys I, Feijge MAH, de vos R, Vermylen J, Heemskerk JWM, et al. Overexpression of the platelet P2X1 ion channel in transgenic mice generates a novel prothrombotic phenotype. Blood 2003;101:3969–3976. doi:https://doi.org/10.1182/blood-2002-10-3215.
- Béatrice H, Christian G. Purinergic receptors in thrombosis and inflammation. Arterioscler Thromb Vasc Biol 2015;35:2307–2315. doi:https://doi.org/10.1161/ATVBAHA.115.303395.
- Trier DA, Gank KD, Kupferwasser D, Yount NY, French WJ, Michelson AD, Kupferwasser LI, Xiong YQ, Bayer AS, Yeaman MR, et al. Platelet antistaphylococcal responses occur through P2X1 and P2Y12 receptor-induced activation and kinocidin release. Infect Immun 2008;76:5706–5713. doi:https://doi.org/10.1128/IAI.00935-08.
- Kälvegren H, Skoglund C, Helldahl C, Lerm M, Grenegård M, Bengtsson T. Toll-like receptor 2 stimulation of platelets is mediated by purinergic P2X1-dependent Ca2+ mobilisation, cyclooxygenase and purinergic P2Y1 and P2Y12 receptor activation. Thromb Haemost 2010;103:398–407. doi:https://doi.org/10.1160/TH09-07-0442.
- Ilkan Z, Watson S, Watson S, Mahaut-Smith M. P2X1 receptors amplify Fcγriia-induced Ca2+ increases and functional responses in human platelets. Thromb Haemost 2018;118:369–380. doi:https://doi.org/10.1160/TH17-07-0530.
- Wéra O, Lecut C, Servais L, Hego A, Delierneux C, Jiang Z, Keutgens A, Evans RJ, Delvenne P, Lancellotti P, et al. P2X1 ion channel deficiency causes massive bleeding in inflamed intestine and increases thrombosis. J Thromb Haemost 2020;18:44–56. doi:https://doi.org/10.1111/jth.14620.
- Chassaing B, Aitken JD, Malleshappa M, Vijay-Kumar M. Dextran Sulfate Sodium (DSS)-induced colitis in mice. Curr Protoc Immunol 2014;104:15.25.1–15.25.14. doi:https://doi.org/10.1002/0471142735.im1525s104.
- Giannotta M, Tapete G, Emmi G, Silvestri E, Milla M. Thrombosis in inflammatory bowel diseases: what’s the link? Thromb J 2015;13:14. doi:https://doi.org/10.1186/s12959-015-0044-2.
- Darbousset R, Delierneux C, Mezouar S, Hego A, Lecut C, Guillaumat I, Riederer MA, Evans RJ, Dignat-George F, Panicot-Dubois L, et al. P2X1 expressed on polymorphonuclear neutrophils and platelets is required for thrombosis in mice. Blood 2014;124:2575–2585. doi:https://doi.org/10.1182/blood-2014-04-571679.
- Papayannopoulos V. Neutrophil extracellular traps in immunity and disease. Nat Rev Immunol 2018;18:134–147. doi:https://doi.org/10.1038/nri.2017.105.
- Laridan E, Denorme F, Desender L. Neutrophil extracellular traps in ischemic stroke thrombi. Ann Neurol 2017;82:223–232. doi:https://doi.org/10.1002/ana.24993.
- Demers M, Wagner DD. Neutrophil extracellular traps: a new link to cancer-associated thrombosis and potential implications for tumor progression. Oncoimmunology 2013;2:e22946–e22946. doi:https://doi.org/10.4161/onci.22946.
- Demers M, Krause DS, Schatzberg D, Martinod K, Voorhees JR, Fuchs TA, Scadden DT, Wagner DD. Cancers predispose neutrophils to release extracellular DNA traps that contribute to cancer-associated thrombosis. Proc Natl Acad Sci U S A 2012;109:13076–13081. doi:https://doi.org/10.1073/pnas.1200419109.
- Alarcón P, Manosalva C, Quiroga J, Belmar I, Álvarez K, Díaz G, Taubert A, Hermosilla C, Carretta MD, Burgos RA, et al. Oleic and linoleic acids induce the release of neutrophil extracellular traps via pannexin 1-dependent ATP release and P2X1 receptor activation. Front Vet Sci 2020;7:260. doi:https://doi.org/10.3389/fvets.2020.00260.
- Quiroga J, Alarcón P, Manosalva C, Taubert A, Hermosilla C, Hidalgo MA, Carretta MD, Burgos RA. Mitochondria-derived ATP participates in the formation of neutrophil extracellular traps induced by platelet-activating factor through purinergic signaling in cows. Dev Comp Immunol 2020;113:103768. doi:https://doi.org/10.1016/j.dci.2020.103768.
- Zhou E, Conejeros I, Gärtner U, Mazurek S, Hermosilla C, Taubert A. Metabolic requirements of Besnoitia besnoiti tachyzoite-triggered NETosis. Parasitol Res 2020;119:545–557. doi:https://doi.org/10.1007/s00436-019-06543-z.
- Brinkmann V, Reichard U, Goosmann C. Neutrophil extracellular traps kill bacteria. Science 2004;303:1532–1535. doi:https://doi.org/10.1126/science.1092385.
- Lefrançais E, Mallavia B, Zhuo H, Calfee CS, Looney MR. Maladaptive role of neutrophil extracellular traps in pathogen-induced lung injury. JCI Insight 2018;3. doi:https://doi.org/10.1172/jci.insight.98178
- Chrysanthopoulou A, Mitroulis I, Apostolidou E, Arelaki S, Mikroulis D, Konstantinidis T, Sivridis E, Koffa M, Giatromanolaki A, Boumpas DT, et al. Neutrophil extracellular traps promote differentiation and function of fibroblasts. J Pathol 2014;233:294–307. doi:https://doi.org/10.1002/path.4359.
- Schönrich G, Raftery MJ. Neutrophil extracellular traps go viral. Front Immunol 2016;7:366. doi:https://doi.org/10.3389/fimmu.2016.00366.
- Radermecker C, Sabatel C, Vanwinge C, Ruscitti C, Maréchal P, Perin F, Schyns J, Rocks N, Toussaint M, Cataldo D, et al. Locally instructed CXCR4hi neutrophils trigger environment-driven allergic asthma through the release of neutrophil extracellular traps. Nat Immunol 2019;20:1444–1455. doi:https://doi.org/10.1038/s41590-019-0496-9.
- Zuo Y, Yalavarthi S, Shi H. Neutrophil extracellular traps in COVID-19. JCI Insight 2020;5. doi:https://doi.org/10.1172/jci.insight.138999.
- Middleton EA, He XY, Denorme F, Campbell RA, Ng D, Salvatore SP, Mostyka M, Baxter-Stoltzfus A, Borczuk AC, Loda M, et al. Neutrophil Extracellular Traps (NETs) contribute to immunothrombosis in COVID-19 acute respiratory distress syndrome. Blood 2020;136:1169–1179. Published online doi:https://doi.org/10.1182/blood.2020007008.
- Radermecker C, Detrembleur N, Guiot J, Cavalier E, Henket M, d’Emal C, Vanwinge C, Cataldo D, Oury C, Delvenne P, et al. Neutrophil extracellular traps infiltrate the lung airway, interstitial, and vascular compartments in severe COVID-19. J Exp Med 2020;217. doi:https://doi.org/10.1084/jem.20201012.
- Ridker PM, Everett BM, Thuren T, MacFadyen JG, Chang WH, Ballantyne C, Fonseca F, Nicolau J, Koenig W, Anker SD, et al. Antiinflammatory therapy with canakinumab for atherosclerotic disease. N Engl J Med 2017;377:1119–1131. doi:https://doi.org/10.1056/NEJMoa1707914.
- Consortium I-6 RMRA (IL6R M), Swerdlow DI, Holmes MV. The interleukin-6 receptor as a target for prevention of coronary heart disease: a mendelian randomisation analysis. Lancet (London, England) 2012;379:1214–1224. doi:https://doi.org/10.1016/S0140-6736(12)60110-X.
- Rosales C. Neutrophil: a cell with many roles in inflammation or several cell types? Front Physiol 2018;9:113. doi:https://doi.org/10.3389/fphys.2018.00113.
- Silvestre-Roig C, Hidalgo A, Soehnlein O. Neutrophil heterogeneity: implications for homeostasis and pathogenesis. Blood 2016;127:2173–2181. doi:https://doi.org/10.1182/blood-2016-01-688887.
- Silvestre-Roig C, Braster Q, Ortega-Gomez A, Soehnlein O. Neutrophils as regulators of cardiovascular inflammation. Nat Rev Cardiol 2020;17:327–340. Published online doi:https://doi.org/10.1038/s41569-019-0326-7.