Beyond the grave: When is cell death critical for immunity to infection?

Current Opinion in Immunology

Volumn 38, Issue , 2016, Pages 59-66

  Stephenson, H N ^a   Herzig, A ^a   Zychlinsky, A ^a  

^a MAX PLANCK INSTITUTE FOR INFECTION BIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL INFECTION; CELL ASSAY; CELL DEATH; CELLULAR PARAMETERS; DANGER ASSOCIATED MOLECULAR PATTERN; HUMAN; IMMUNE RESPONSE; IMMUNOCOMPETENT CELL; MOLECULAR DYNAMICS; NECROPTOSIS; NETOSIS; NONHUMAN; OUTCOME ASSESSMENT; PYROPTOSIS; REGULATED CELL DEATH; REVIEW; SIGNAL TRANSDUCTION; ANIMAL; GENE EXPRESSION REGULATION; GENETICS; HOST PATHOGEN INTERACTION; IMMUNOLOGY; INNATE IMMUNITY; MACROPHAGE; MICROBIOLOGY; PATHOLOGY; VIRUS INFECTION;

ALARMIN; INTERLEUKIN 1BETA;

ALARMINS; ANIMALS; BACTERIAL INFECTIONS; CELL DEATH; GENE EXPRESSION REGULATION; HOST-PATHOGEN INTERACTIONS; HUMANS; IMMUNITY, INNATE; INTERLEUKIN-1BETA; MACROPHAGES; SIGNAL TRANSDUCTION; VIRUS DISEASES;

EID: 84949970938     PISSN: 09527915     EISSN: 18790372     Source Type: Journal    
DOI: 10.1016/j.coi.2015.11.004     Document Type: Review

References (106)

1. Galluzzi L., Bravo-San Pedro J.M., Vitale I., Aaronson S.A., Abrams J.M., Adam D., Alnemri E.S., Altucci L., Andrews D., Annicchiarico-Petruzzelli M., et al. Essential versus accessory aspects of cell death: recommendations of the NCCD 2015. Cell Death Differ 2015, 22:58-73.
2. Inoue H., Tani K. Multimodal immunogenic cancer cell death as a consequence of anticancer cytotoxic treatments. Cell Death Differ 2014, 21:39-49.
3. Bianchi M.E. DAMPs PAMPs and alarmins: all we need to know about danger. J Leukoc Biol 2007, 81:1-5.
4. Chen G.Y., Nunez G. Sterile inflammation: sensing and reacting to damage. Nat Rev Immunol 2010, 10:826-837.
5. Kono H., Rock K.L. How dying cells alert the immune system to danger. Nat Rev Immunol 2008, 8:279-289.
6. Rock K.L., Kono H. The inflammatory response to cell death. Annu Rev Pathol 2008, 3:99-126.
7. Matzinger P. Tolerance, danger, and the extended family. Annu Rev Immunol 1994, 12:991-1045.
8. Matzinger P. The danger model: a renewed sense of self. Science 2002, 296:301-305.
9. Jorgensen I., Miao E.A. Pyroptotic cell death defends against intracellular pathogens. Immunol Rev 2015, 265:130-142.
10. Cullen S.P., Kearney C.J., Clancy D.M., Martin S.J. Diverse activators of the NLRP3 inflammasome promote IL-1beta secretion by triggering necrosis. Cell Rep 2015, 11:1535-1548.
11. Kayagaki N., Stowe I.B., Lee B.L., O'Rourke K., Anderson K., Warming S., Cuellar T., Haley B., Roose-Girma M., Phung Q.T., et al. Caspase-11 cleaves gasdermin D for non-canonical inflammasome signaling. Nature 2015.
12. Shi J., Zhao Y., Wang K., Shi X., Wang Y., Huang H., Zhuang Y., Cai T., Wang F., Shao F. Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature 2015.
13. Netea M.G., Simon A., van de Veerdonk F., Kullberg B.J., Van der Meer J.W., Joosten L.A. IL-1beta processing in host defense: beyond the inflammasomes. PLoS Pathog 2010, 6:e1000661.
14. Mariathasan S., Weiss D.S., Dixit V.M., Monack D.M. Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis. J Exp Med 2005, 202:1043-1049.
15. Raupach B., Peuschel S.K., Monack D.M., Zychlinsky A. Caspase-1-mediated activation of interleukin-1beta (IL-1beta) and IL-18 contributes to innate immune defenses against Salmonella enterica serovar Typhimurium infection. Infect Immun 2006, 74:4922-4926.
16. Sahoo M., Ceballos-Olvera I., del Barrio L., Re F. Role of the inflammasome, IL-1beta, and IL-18 in bacterial infections. ScientificWorldJournal 2011, 11:2037-2050.
17. Miao E.A., Leaf I.A., Treuting P.M., Mao D.P., Dors M., Sarkar A., Warren S.E., Wewers M.D., Aderem A. Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat Immunol 2010, 11:1136-1142.
18. Sauer J.D., Pereyre S., Archer K.A., Burke T.P., Hanson B., Lauer P., Portnoy D.A. Listeria monocytogenes engineered to activate the Nlrc4 inflammasome are severely attenuated and are poor inducers of protective immunity. Proc Natl Acad Sci U S A 2011, 108:12419-12424.
19. Holler N., Zaru R., Micheau O., Thome M., Attinger A., Valitutti S., Bodmer J.L., Schneider P., Seed B., Tschopp J. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat Immunol 2000, 1:489-495.
20. Matsumura H., Shimizu Y., Ohsawa Y., Kawahara A., Uchiyama Y., Nagata S. Necrotic death pathway in Fas receptor signaling. J Cell Biol 2000, 151:1247-1256.
21. Wang H., Sun L., Su L., Rizo J., Liu L., Wang L-F., Wang F-S., Wang X. Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3. Mol Cell 2014, 54:133-146.
22. Cai Z., Jitkaew S., Zhao J., Chiang H-C., Choksi S., Liu J., Ward Y., Wu L-G., Liu Z-G. Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nat Cell Biol 2014, 16:55-65.
23. Murphy J.M., Czabotar P.E., Hildebrand J.M., Lucet I.S., Zhang J-G., Alvarez-Diaz S., Lewis R., Lalaoui N., Metcalf D., Webb A.I., et al. The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism. Immunity 2013, 39:443-453.
24. Wu J., Huang Z., Ren J., Zhang Z., He P., Li Y., Ma J., Chen W., Zhang Y., Zhou X., et al. Mlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis. Cell Res 2013, 23:994-1006.
25. Bleriot C., Dupuis T., Jouvion G., Eberl G., Disson O., Lecuit M. Liver-resident macrophage necroptosis orchestrates type 1 microbicidal inflammation and type-2-mediated tissue repair during bacterial infection. Immunity 2015, 42:145-158.
26. Kang T.B., Yang S.H., Toth B., Kovalenko A., Wallach D. Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity 2013, 38:27-40.
27. Robinson N., McComb S., Mulligan R., Dudani R., Krishnan L., Sad S. Type I interferon induces necroptosis in macrophages during infection with Salmonella enterica serovar Typhimurium. Nat Immunol 2012, 13:954-962.
28. Roca F.J., Ramakrishnan L. TNF dually mediates resistance and susceptibility to mycobacteria via mitochondrial reactive oxygen species. Cell 2013, 153:521-534.
29. Kitur K., Parker D., Nieto P., Ahn D.S., Cohen T.S., Chung S., Wachtel S., Bueno S., Prince A. Toxin-induced necroptosis is a major mechanism of Staphylococcus aureus lung damage. PLoS Pathog 2015, 11:e1004820.
30. Chan F.K-M., Luz N.F., Moriwaki K. Programmed necrosis in the cross talk of cell death and inflammation. Annu Rev Immunol 2015, 33:79-106.
31. Pasparakis M., Vandenabeele P. Necroptosis and its role in inflammation. Nature 2015, 517:311-320.
32. Silke J., Rickard J.A., Gerlic M. The diverse role of RIP kinases in necroptosis and inflammation. Nat Immunol 2015, 16:689-697.
33. Huang Z., Wu S.Q., Liang Y., Zhou X., Chen W., Li L., Wu J., Zhuang Q., Chen C., Li J., et al. RIP1/RIP3 binding to HSV-1 ICP6 initiates necroptosis to restrict virus propagation in mice. Cell Host Microbe 2015, 17:229-242.
34. Dondelinger Y., Aguileta M.A., Goossens V., Dubuisson C., Grootjans S., Dejardin E., Vandenabeele P., Bertrand M.J.M. RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition. Cell Death Differ 2013, 20:1381-1392.
35. Lawlor K.E., Khan N., Mildenhall A., Gerlic M., Croker B.A., D'Cruz A.A., Hall C., Kaur Spall S., Anderton H., Masters S.L., et al. RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL. Nat Commun 2015, 6:6282.
36. Orozco S., Yatim N., Werner M.R., Tran H., Gunja S.Y., Tait S.W.G., Albert M.L., Green D.R., Oberst A. RIPK1 both positively and negatively regulates RIPK3 oligomerization and necroptosis. Cell Death Differ 2014, 21:1511-1521.
37. Kang T-B., Yang S-H., Toth B., Kovalenko A., Wallach D. Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity 2013, 38:27-40.
38. Lukens J.R., Vogel P., Johnson G.R., Kelliher M.A., Iwakura Y., Lamkanfi M., Kanneganti T.D. RIP1-driven autoinflammation targets IL-1alpha independently of inflammasomes and RIP3. Nature 2013, 498:224-227.
39. Brinkmann V., Reichard U., Goosmann C., Fauler B., Uhlemann Y., Weiss D.S., Weinrauch Y., Zychlinsky A. Neutrophil extracellular traps kill bacteria. Science 2004, 303:1532-1535.
40. von Kockritz-Blickwede M., Goldmann O., Thulin P., Heinemann K., Norrby-Teglund A., Rohde M., Medina E. Phagocytosis-independent antimicrobial activity of mast cells by means of extracellular trap formation. Blood 2008, 111:3070-3080.
41. Thammavongsa V., Missiakas D.M., Schneewind O. Staphylococcus aureus degrades neutrophil extracellular traps to promote immune cell death. Science 2013, 342:863-866.
42. Brinkmann V., Zychlinsky A. Neutrophil extracellular traps: is immunity the second function of chromatin?. J Cell Biol 2012, 198:773-783.
43. Kaplan A., Ma J., Kyme P., Wolf A.J., Becker C.A., Tseng C.W., Liu G.Y., Underhill D.M. Failure to induce IFN-beta production during Staphylococcus aureus infection contributes to pathogenicity. J Immunol 2012, 189:4537-4545.
44. Hirsch J.G. Bactericidal action of histone. J Exp Med 1958, 108:925-944.
45. Urban C.F., Ermert D., Schmid M., Abu-Abed U., Goosmann C., Nacken W., Brinkmann V., Jungblut P.R., Zychlinsky A. Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans. PLoS Pathog 2009, 5:e1000639.
46. Halverson T.W., Wilton M., Poon K.K., Petri B., Lewenza S. DNA is an antimicrobial component of neutrophil extracellular traps. PLoS Pathog 2015, 11:e1004593.
47. Hawes M.C., Curlango-Rivera G., Wen F., White G.J., Vanetten H.D., Xiong Z. Extracellular DNA: the tip of root defenses?. Plant Sci 2011, 180:741-745.
48. Robb C.T., Dyrynda E.A., Gray R.D., Rossi A.G., Smith V.J. Invertebrate extracellular phagocyte traps show that chromatin is an ancient defence weapon. Nat Commun 2014, 5:4627.
49. Fuchs T.A., Abed U., Goosmann C., Hurwitz R., Schulze I., Wahn V., Weinrauch Y., Brinkmann V., Zychlinsky A. Novel cell death program leads to neutrophil extracellular traps. J Cell Biol 2007, 176:231-241.
50. Metzler K.D., Fuchs T.A., Nauseef W.M., Reumaux D., Roesler J., Schulze I., Wahn V., Papayannopoulos V., Zychlinsky A. Myeloperoxidase is required for neutrophil extracellular trap formation: implications for innate immunity. Blood 2011, 117:953-959.
51. Metzler K.D., Goosmann C., Lubojemska A., Zychlinsky A., Papayannopoulos V. A myeloperoxidase-containing complex regulates neutrophil elastase release and actin dynamics during NETosis. Cell Rep 2014, 8:883-896.
52. Goldmann O., Medina E. The expanding world of extracellular traps: not only neutrophils but much more. Front Immunol 2012, 3:420.
53. Li P., Li M., Lindberg M.R., Kennett M.J., Xiong N., Wang Y. PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps. J Exp Med 2010, 207:1853-1862.
54. Kuhns D.B., Alvord W.G., Heller T., Feld J.J., Pike K.M., Marciano B.E., Uzel G., DeRavin S.S., Priel D.A., Soule B.P., et al. Residual NADPH oxidase and survival in chronic granulomatous disease. N Engl J Med 2010, 363:2600-2610.
55. Aratani Y., Koyama H., Nyui S., Suzuki K., Kura F., Maeda N. Severe impairment in early host defense against Candida albicans in mice deficient in myeloperoxidase. Infect Immun 1999, 67:1828-1836.
56. Pollock J.D., Williams D.A., Gifford M.A., Li L.L., Du X., Fisherman J., Orkin S.H., Doerschuk C.M., Dinauer M.C. Mouse model of X-linked chronic granulomatous disease, an inherited defect in phagocyte superoxide production. Nat Genet 1995, 9:202-209.
57. Belaaouaj A., McCarthy R., Baumann M., Gao Z., Ley T.J., Abraham S.N., Shapiro S.D. Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis. Nat Med 1998, 4:615-618.
58. Tkalcevic J., Novelli M., Phylactides M., Iredale J.P., Segal A.W., Roes J. Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G. Immunity 2000, 12:201-210.
59. Rammes A., Roth J., Goebeler M., Klempt M., Hartmann M., Sorg C. Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway. J Biol Chem 1997, 272:9496-9502.
60. Majno G., La Gattuta M., Thompson T.E. Cellular death and necrosis: chemical, physical and morphologic changes in rat liver. Virchows Arch Pathol Anat Physiol Klin Med 1960, 333:421-465.
61. Tian J., Avalos A.M., Mao S.Y., Chen B., Senthil K., Wu H., Parroche P., Drabic S., Golenbock D., Sirois C., et al. Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE. Nat Immunol 2007, 8:487-496.
62. Qin Y.H., Dai S.M., Tang G.S., Zhang J., Ren D., Wang Z.W., Shen Q. HMGB1 enhances the proinflammatory activity of lipopolysaccharide by promoting the phosphorylation of MAPK p38 through receptor for advanced glycation end products. J Immunol 2009, 183:6244-6250.
63. Donato R., Cannon B.R., Sorci G., Riuzzi F., Hsu K., Weber D.J., Geczy C.L. Functions of S100 proteins. Curr Mol Med 2013, 13:24-57.
64. Ehrchen J.M., Sunderkotter C., Foell D., Vogl T., Roth J. The endogenous Toll-like receptor 4 agonist S100A8/S100A9 (calprotectin) as innate amplifier of infection, autoimmunity, and cancer. J Leukoc Biol 2009, 86:557-566.
65. Passey R.J., Williams E., Lichanska A.M., Wells C., Hu S., Geczy C.L., Little M.H., Hume D.A. A null mutation in the inflammation-associated S100 protein S100A8 causes early resorption of the mouse embryo. J Immunol 1999, 163:2209-2216.
66. Hobbs J.A., May R., Tanousis K., McNeill E., Mathies M., Gebhardt C., Henderson R., Robinson M.J., Hogg N. Myeloid cell function in MRP-14 (S100A9) null mice. Mol Cell Biol 2003, 23:2564-2576.
67. Manitz M.P., Horst B., Seeliger S., Strey A., Skryabin B.V., Gunzer M., Frings W., Schonlau F., Roth J., Sorg C., et al. Loss of S100A9 (MRP14) results in reduced interleukin-8-induced CD11b surface expression, a polarized microfilament system, and diminished responsiveness to chemoattractants in vitro. Mol Cell Biol 2003, 23:1034-1043.
68. Vogl T., Tenbrock K., Ludwig S., Leukert N., Ehrhardt C., van Zoelen M.A., Nacken W., Foell D., van der Poll T., Sorg C., et al. Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4, promoting lethal, endotoxin-induced shock. Nat Med 2007, 13:1042-1049.
69. van Zoelen M.A., Vogl T., Foell D., Van Veen S.Q., van Till J.W., Florquin S., Tanck M.W., Wittebole X., Laterre P.F., Boermeester M.A., et al. Expression and role of myeloid-related protein-14 in clinical and experimental sepsis. Am J Respir Crit Care Med 2009, 180:1098-1106.
70. Boyd J.H., Kan B., Roberts H., Wang Y., Walley K.R. S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction via the receptor for advanced glycation end products. Circ Res 2008, 102:1239-1246.
71. Achouiti A., Vogl T., Urban C.F., Rohm M., Hommes T.J., van Zoelen M.A., Florquin S., Roth J., van 't Veer C., de Vos A.F., et al. Myeloid-related protein-14 contributes to protective immunity in gram-negative pneumonia derived sepsis. PLoS Pathog 2012, 8:e1002987.
72. Corbin B.D., Seeley E.H., Raab A., Feldmann J., Miller M.R., Torres V.J., Anderson K.L., Dattilo B.M., Dunman P.M., Gerads R., et al. Metal chelation and inhibition of bacterial growth in tissue abscesses. Science 2008, 319:962-965.
73. Kehl-Fie T.E., Chitayat S., Hood M.I., Damo S., Restrepo N., Garcia C., Munro K.A., Chazin W.J., Skaar E.P. Nutrient metal sequestration by calprotectin inhibits bacterial superoxide defense, enhancing neutrophil killing of Staphylococcus aureus. Cell Host Microbe 2011, 10:158-164.
74. Ryckman C., Vandal K., Rouleau P., Talbot M., Tessier P.A. Proinflammatory activities of S100: proteins S100A8, S100A9, and S100A8/A9 induce neutrophil chemotaxis and adhesion. J Immunol 2003, 170:3233-3242.
75. Raquil M.A., Anceriz N., Rouleau P., Tessier P.A. Blockade of antimicrobial proteins S100A8 and S100A9 inhibits phagocyte migration to the alveoli in streptococcal pneumonia. J Immunol 2008, 180:3366-3374.
76. Vogl T., Ludwig S., Goebeler M., Strey A., Thorey I.S., Reichelt R., Foell D., Gerke V., Manitz M.P., Nacken W., et al. MRP8 and MRP14 control microtubule reorganization during transendothelial migration of phagocytes. Blood 2004, 104:4260-4268.
77. Wang H., Bloom O., Zhang M., Vishnubhakat J.M., Ombrellino M., Che J., Frazier A., Yang H., Ivanova S., Borovikova L., et al. HMG-1 as a late mediator of endotoxin lethality in mice. Science 1999, 285:248-251.
78. Scaffidi P., Misteli T., Bianchi M.E. Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature 2002, 418:191-195.
79. Calogero S., Grassi F., Aguzzi A., Voigtlander T., Ferrier P., Ferrari S., Bianchi M.E. The lack of chromosomal protein Hmg1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice. Nat Genet 1999, 22:276-280.
80. Yanai H., Matsuda A., An J., Koshiba R., Nishio J., Negishi H., Ikushima H., Onoe T., Ohdan H., Yoshida N., et al. Conditional ablation of HMGB1 in mice reveals its protective function against endotoxemia and bacterial infection. Proc Natl Acad Sci U S A 2013, 110:20699-20704.
81. Huang H., Nace G.W., McDonald K.A., Tai S., Klune J.R., Rosborough B.R., Ding Q., Loughran P., Zhu X., Beer-Stolz D., et al. Hepatocyte-specific high-mobility group box 1 deletion worsens the injury in liver ischemia/reperfusion: a role for intracellular high-mobility group box 1 in cellular protection. Hepatology 2014, 59:1984-1997.
82. Tang D., Kang R., Livesey K.M., Cheh C.W., Farkas A., Loughran P., Hoppe G., Bianchi M.E., Tracey K.J., Zeh H.J., et al. Endogenous HMGB1 regulates autophagy. J Cell Biol 2010, 190:881-892.
83. Lam G.Y., Czuczman M.A., Higgins D.E., Brumell J.H. Interactions of Listeria monocytogenes with the autophagy system of host cells. Adv Immunol 2012, 113:7-18.
84. Garlanda C., Dinarello C.A., Mantovani A. The interleukin-1 family: back to the future. Immunity 2013, 39:1003-1018.
85. Cayrol C., Girard J.P. IL-33: an alarmin cytokine with crucial roles in innate immunity, inflammation and allergy. Curr Opin Immunol 2014, 31:31-37.
86. Hung L.Y., Lewkowich I.P., Dawson L.A., Downey J., Yang Y., Smith D.E., Herbert D.R. IL-33 drives biphasic IL-13 production for noncanonical Type 2 immunity against hookworms. Proc Natl Acad Sci U S A 2013, 110:282-287.
87. Barry K.C., Fontana M.F., Portman J.L., Dugan A.S., Vance R.E. IL-1alpha signaling initiates the inflammatory response to virulent Legionella pneumophila in vivo. J Immunol 2013, 190:6329-6339.
88. Mayer-Barber K.D., Andrade B.B., Barber D.L., Hieny S., Feng C.G., Caspar P., Oland S., Gordon S., Sher A. Innate and adaptive interferons suppress IL-1alpha and IL-1beta production by distinct pulmonary myeloid subsets during Mycobacterium tuberculosis infection. Immunity 2011, 35:1023-1034.
89. Bourigault M.L., Segueni N., Rose S., Court N., Vacher R., Vasseur V., Erard F., Le Bert M., Garcia I., Iwakura Y., et al. Relative contribution of IL-1alpha, IL-1beta and TNF to the host response to Mycobacterium tuberculosis and attenuated M. bovis BCG. Immun Inflamm Dis 2013, 1:47-62.
90. Al Moussawi K., Kazmierczak B.I. Distinct contributions of interleukin-1alpha (IL-1alpha) and IL-1beta to innate immune recognition of Pseudomonas aeruginosa in the lung. Infect Immun 2014, 82:4204-4211.
91. Remijsen Q., Goossens V., Grootjans S., Van den Haute C., Vanlangenakker N., Dondelinger Y., Roelandt R., Bruggeman I., Goncalves A., Bertrand M.J.M., et al. Depletion of RIPK3 or MLKL blocks TNF-driven necroptosis and switches towards a delayed RIPK1 kinase-dependent apoptosis. Cell Death Dis 2014, 5:e1004.
92. Vanden Berghe T., Kalai M., van Loo G., Declercq W., Vandenabeele P. Disruption of HSP90 function reverts tumor necrosis factor-induced necrosis to apoptosis. J Biol Chem 2003, 278:5622-5629.
93. Los M., Mozoluk M., Ferrari D., Stepczynska A., Stroh C., Renz A., Herceg Z., Wang Z-Q., Schulze-Osthoff K. Activation and caspase-mediated inhibition of PARP: a molecular switch between fibroblast necrosis and apoptosis in death receptor signaling. Mol Biol Cell 2002, 13:978-988.
94. Gaymes T.J., Shall S., MacPherson L.J., Twine N.A., Lea N.C., Farzaneh F., Mufti G.J. Inhibitors of poly ADP-ribose polymerase (PARP) induce apoptosis of myeloid leukemic cells: potential for therapy of myeloid leukemia and myelodysplastic syndromes. Haematologica 2009, 94:638-646.
95. Yu M., Wang H., Ding A., Golenbock D.T., Latz E., Czura C.J., Fenton M.J., Tracey K.J., Yang H. HMGB1 signals through toll-like receptor (TLR) 4 and TLR2. Shock 2006, 26:174-179.
96. Hori O., Brett J., Slattery T., Cao R., Zhang J., Chen J.X., Nagashima M., Lundh E.R., Vijay S., Nitecki D., et al. The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of rage and amphoterin in the developing nervous system. J Biol Chem 1995, 270:25752-25761.
97. Chen G.Y., Tang J., Zheng P., Liu Y. CD24 and Siglec-10 selectively repress tissue damage-induced immune responses. Science 2009, 323:1722-1725.
98. Bonaldi T., Talamo F., Scaffidi P., Ferrera D., Porto A., Bachi A., Rubartelli A., Agresti A., Bianchi M.E. Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion. EMBO J 2003, 22:5551-5560.
99. Youn J.H., Shin J.S. Nucleocytoplasmic shuttling of HMGB1 is regulated by phosphorylation that redirects it toward secretion. J Immunol 2006, 177:7889-7897.
100. Hofmann M.A., Drury S., Fu C., Qu W., Taguchi A., Lu Y., Avila C., Kambham N., Bierhaus A., Nawroth P., et al. RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell 1999, 97:889-901.
101. Eigenbrod T., Park J.H., Harder J., Iwakura Y., Nunez G. Cutting edge: critical role for mesothelial cells in necrosis-induced inflammation through the recognition of IL-1 alpha released from dying cells. J Immunol 2008, 181:8194-8198.
102. Chen C.J., Kono H., Golenbock D., Reed G., Akira S., Rock K.L. Identification of a key pathway required for the sterile inflammatory response triggered by dying cells. Nat Med 2007, 13:851-856.
103. Fettelschoss A., Kistowska M., LeibundGut-Landmann S., Beer H.D., Johansen P., Senti G., Contassot E., Bachmann M.F., French L.E., Oxenius A., et al. Inflammasome activation and IL-1beta target IL-1alpha for secretion as opposed to surface expression. Proc Natl Acad Sci U S A 2011, 108:18055-18060.
104. Gross O., Yazdi A.S., Thomas C.J., Masin M., Heinz L.X., Guarda G., Quadroni M., Drexler S.K., Tschopp J. Inflammasome activators induce interleukin-1alpha secretion via distinct pathways with differential requirement for the protease function of caspase-1. Immunity 2012, 36:388-400.
105. Moussion C., Ortega N., Girard J.P. The IL-1-like cytokine IL-33 is constitutively expressed in the nucleus of endothelial cells and epithelial cells in vivo: a novel 'alarmin'?. PLoS ONE 2008, 3:e3331.
106. Cayrol C., Girard J.P. The IL-1-like cytokine IL-33 is inactivated after maturation by caspase-1. Proc Natl Acad Sci U S A 2009, 106:9021-9026.