Frontline science: Multiple cathepsins promote inflammasome-independent, particle-induced cell death during NLRP3-dependent IL-1β activation

Journal of Leukocyte Biology

Volumn 102, Issue 1, 2017, Pages 7-17

  Orlowski, Gregory M ^a   Sharma, Shruti ^a   Colbert, Jeff D ^a   Bogyo, Matthew ^b   Robertson, Stephanie A ^c   Kataoka, Hiroshi ^a   Chan, Francis K ^a   Rock, Kenneth L ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Caspase 1; Inflammation; Macrophage; Peritonitis; Pyroptosis

Indexed keywords

CASPASE 11; CASPASE 8; CASPASE INHIBITOR; CATHEPSIN B; CATHEPSIN INHIBITOR; CATHEPSIN X; CRYOPYRIN; CYSTEINE PROTEINASE INHIBITOR; INFLAMMASOME; INTERLEUKIN 1ALPHA; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; LIPOPOLYSACCHARIDE; N BENZHYDRYL DECAHYDRO 5 [2 (METHYLAMINO)PROPIONAMIDO] 3 (3 METHYLBUTANOYL) 6 OXOPYRROLO[1,2 A][1,5]DIAZOCINE 8 CARBOXAMIDE; NIGERICIN; SMALL INTERFERING RNA; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; CATHEPSIN; CATHEPSIN X, MOUSE; CTSB PROTEIN, MOUSE; IL1B PROTEIN, MOUSE; NLRP3 PROTEIN, MOUSE; PARTICULATE MATTER;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BONE MARROW; BONE MARROW DERIVED MACROPHAGE; CELL LYSATE; CONTROLLED STUDY; CYTOKINE PRODUCTION; CYTOKINE RELEASE; CYTOSOL; ENZYME ACTIVITY; GENE SILENCING; GENETIC MODEL; LYSOSOME; MACROPHAGE; MAST CELL; MOUSE; NECROPTOSIS; NEWBORN; NONHUMAN; PHAGOCYTOSIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PYROPTOSIS; QUANTITATIVE ANALYSIS; WILD TYPE; ADVERSE EFFECTS; ANIMAL; APOPTOSIS; CHEMICALLY INDUCED; DRUG EFFECTS; GENETICS; KNOCKOUT MOUSE; METABOLISM; PARTICULATE MATTER; PATHOLOGY; PERITONITIS; PHARMACOLOGY;

ANIMALS; APOPTOSIS; CASPASE 1; CATHEPSIN B; CATHEPSINS; INFLAMMASOMES; INTERLEUKIN-1BETA; MACROPHAGES; MICE; MICE, KNOCKOUT; NLR FAMILY, PYRIN DOMAIN-CONTAINING 3 PROTEIN; PARTICULATE MATTER; PERITONITIS;

EID: 85021738895     PISSN: 07415400     EISSN: 19383673     Source Type: Journal    
DOI: 10.1189/jlb.3HI0316-152R     Document Type: Article

References (81)

1. Shen, H., Kreisel, D., Goldstein, D. R. (2013) Processes of sterile inflammation. J. Immunol. 191, 2857-2863.
2. Dostert, C., Pétrilli, V., Van Bruggen, R., Steele, C., Mossman, B. T., Tschopp, J. (2008) Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science 320, 674-677.
3. Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., Latz, E. (2008) Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat. Immunol. 9, 847-856.
4. Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., Golenbock, D. T. (2008) The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat. Immunol. 9, 857-865.
5. Cassel, S. L., Eisenbarth, S. C., Iyer, S. S., Sadler, J. J., Colegio, O. R., Tephly, L. A., Carter, A. B., Rothman, P. B., Flavell, R. A., Sutterwala, F. S. (2008) The Nalp3 inflammasome is essential for the development of silicosis. Proc. Natl. Acad. Sci. USA 105, 9035-9040.
6. Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., Tschopp, J. (2006) Goutassociated uric acid crystals activate the NALP3 inflammasome. Nature 440, 237-241.
7. Duewell, P., Kono, H., Rayner, K. J., Sirois, C. M., Vladimer, G., Bauernfeind, F. G., Abela, G. S., Franchi, L., Nuñez, G., Schnurr, M., Espevik, T., Lien, E., Fitzgerald, K. A., Rock, K. L., Moore, K. J., Wright, S. D., Hornung, V., Latz, E. (2010) NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature 464, 1357-1361.
8. Rajamäki, K., Lappalainen, J., Oörni, K., Välimäki, E., Matikainen, S., Kovanen, P. T., Eklund, K. K. (2010) Cholesterol crystals activate the NLRP3 inflammasome in human macrophages: a novel link between cholesterol metabolism and inflammation. PLoS One 5, e11765.
9. Ashida, H., Mimuro, H., Ogawa, M., Kobayashi, T., Sanada, T., Kim, M., Sasakawa, C. (2011) Cell death and infection: a double-edged sword for host and pathogen survival. J. Cell Biol. 195, 931-942.
10. Miao, E. A., Leaf, I. A., Treuting, P. M., Mao, D. P., Dors, M., Sarkar, A., Warren, S. E., Wewers, M. D., Aderem, A. (2010) Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat. Immunol. 11, 1136-1142.
11. Brodsky, I. E., Medzhitov, R. (2011) Pyroptosis: macrophage suicide exposes hidden invaders. Curr. Biol. 21, R72-R75.
12. Nair, P. N., Sjögren, U., Sundqvist, G. (1998) Cholesterol crystals as an etiological factor in non-resolving chronic inflammation: an experimental study in guinea pigs. Eur. J. Oral Sci. 106, 644-650.
13. Ellson, C. D., Dunmore, R., Hogaboam, C. M., Sleeman, M. A., Murray, L. A. (2014) Danger-associated molecular patterns and danger signals in idiopathic pulmonary fibrosis. Am. J. Respir. Cell Mol. Biol. 51, 163-168.
14. Kono, H., Rock, K. L. (2008) How dying cells alert the immune system to danger. Nat. Rev. Immunol. 8, 279-289.
15. Kono, H., Karmarkar, D., Iwakura, Y., Rock, K. L. (2010) Identification of the cellular sensor that stimulates the inflammatory response to sterile cell death. J. Immunol. 184, 4470-4478.
16. Dutta, D., Moudgil, B. M. (2007) Crystalline silica particles mediated lung injury. Kona. 25, 76-87.
17. Kono, H., Orlowski, G. M., Patel, Z., Rock, K. L. (2012) The IL-1-dependent sterile inflammatory response has a substantial caspase-1-independent component that requires cathepsin C. J. Immunol. 189, 3734-3740.
18. Chen, C. J., Kono, H., Golenbock, D., Reed, G., Akira, S., Rock, K. L. (2007) Identification of a key pathway required for the sterile inflammatory response triggered by dying cells. Nat. Med. 13, 851-856.
19. Bauernfeind, F. G., Horvath, G., Stutz, A., Alnemri, E. S., MacDonald, K., Speert, D., Fernandes-Alnemri, T., Wu, J., Monks, B. G., Fitzgerald, K. A., Hornung, V., Latz, E. (2009) Cutting edge: NF-kB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression. J. Immunol. 183, 787-791.
20. Bauernfeind, F., Bartok, E., Rieger, A., Franchi, L., Núñez, G., Hornung, V. (2011) Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J. Immunol. 187, 613-617.
21. Mariathasan, S., Newton, K., Monack, D. M., Vucic, D., French, D. M., Lee, W. P., Roose-Girma, M., Erickson, S., Dixit, V. M. (2004) Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430, 213-218.
22. Agostini, L., Martinon, F., Burns, K., McDermott, M. F., Hawkins, P. N., Tschopp, J. (2004) NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity 20, 319-325.
23. Lamkanfi, M., Dixit, V. M. (2012) Inflammasomes and their roles in health and disease. Annu. Rev. Cell Dev. Biol. 28, 137-161.
24. Kayagaki, N., Warming, S., Lamkanfi, M., Vande Walle, L., Louie, S., Dong, J., Newton, K., Qu, Y., Liu, J., Heldens, S., Zhang, J., Lee, W. P., Roose-Girma, M., Dixit, V. M. (2011) Non-canonical inflammasome activation targets caspase-11. Nature 479, 117-121.
25. Barlan, A. U., Griffin, T. M., McGuire, K. A., Wiethoff, C. M. (2011) Adenovirus membrane penetration activates the NLRP3 inflammasome. J. Virol. 85, 146-155.
26. Jacobson, L. S., Lima, H., Jr., Goldberg, M. F., Gocheva, V., Tsiperson, V., Sutterwala, F. S., Joyce, J. A., Gapp, B. V., Blomen, V. A., Chandran, K., Brummelkamp, T. R., Diaz-Griffero, F., Brojatsch, J. (2013) Cathepsinmediated necrosis controls the adaptive immune response by Th2 (T helper type 2)-associated adjuvants. J. Biol. Chem. 288, 7481-7491.
27. Brojatsch, J., Lima, H., Kar, A. K., Jacobson, L. S., Muehlbauer, S. M., Chandran, K., Diaz-Griffero, F. (2014) A proteolytic cascade controls lysosome rupture and necrotic cell death mediated by lysosomedestabilizing adjuvants. PLoS One 9, e95032.
28. Lima, H., Jr., Jacobson, L. S., Goldberg, M. F., Chandran, K., Diaz-Griffero, F., Lisanti, M. P., Brojatsch, J. (2013) Role of lysosome rupture in controlling Nlrp3 signaling and necrotic cell death. Cell Cycle 12, 1868-1878.
29. Bruchard, M., Mignot, G., Derangère, V., Chalmin, F., Chevriaux, A., Végran, F., Boireau, W., Simon, B., Ryffel, B., Connat, J. L., Kanellopoulos, J., Martin, F., Rébé, C., Apetoh, L., Ghiringhelli, F. (2013) Chemotherapy-triggered cathepsin B release in myeloid-derived suppressor cells activates the Nlrp3 inflammasome and promotes tumor growth. Nat. Med. 19, 57-64.
30. Terada, K., Yamada, J., Hayashi, Y., Wu, Z., Uchiyama, Y., Peters, C., Nakanishi, H. (2010) Involvement of cathepsin B in the processing and secretion of interleukin-1beta in chromogranin A-stimulated microglia. Glia 58, 114-124.
31. Newman, Z. L., Leppla, S. H., Moayeri, M. (2009) CA-074Me protection against anthrax lethal toxin. Infect. Immun. 77, 4327-4336.
32. Dostert, C., Guarda, G., Romero, J. F., Menu, P., Gross, O., Tardivel, A., Suva, M. L., Stehle, J. C., Kopf, M., Stamenkovic, I., Corradin, G., Tschopp, J. (2009) Malarial hemozoin is a Nalp3 inflammasome activating danger signal. PLoS One 4, e6510.
33. Montaser, M., Lalmanach, G., Mach, L. (2002) CA-074, but not its methyl ester CA-074Me, is a selective inhibitor of cathepsin B within living cells. Biol. Chem. 383, 1305-1308.
34. Mihalik, R., Imre, G., Petak, I., Szende, B., Kopper, L. (2004) Cathepsin B-independent abrogation of cell death by CA-074-OMe upstream of lysosomal breakdown. Cell Death Differ. 11, 1357-1360.
35. Klemenčič, I., Carmona, A. K., Cezari, M. H., Juliano, M. A., Juliano, L., Guncar, G., Turk, D., Krizaj, I., Turk, V., Turk, B. (2000) Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase. Eur. J. Biochem. 267, 5404-5412.
36. Bogyo, M., Verhelst, S., Bellingard-Dubouchaud, V., Toba, S., Greenbaum, D. (2000) Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs. Chem. Biol. 7, 27-38.
37. Orlowski, G. M., Colbert, J. D., Sharma, S., Bogyo, M., Robertson, S. A., Rock, K. L. (2015) Multiple Cathepsins promote pro-IL-1β synthesis and NLRP3-mediated IL-1β activation. J. Immunol. 195, 1685-1697.
38. Felbor, U., Kessler, B., Mothes, W., Goebel, H. H., Ploegh, H. L., Bronson, R. T., Olsen, B. R. (2002) Neuronal loss and brain atrophy in mice lacking cathepsins B and L. Proc. Natl. Acad. Sci. USA 99, 7883-7888.
39. Vasiljeva, O., Papazoglou, A., Krüger, A., Brodoefel, H., Korovin, M., Deussing, J., Augustin, N., Nielsen, B. S., Almholt, K., Bogyo, M., Peters, C., Reinheckel, T. (2006) Tumor cell-derived and macrophage-derived cathepsin B promotes progression and lung metastasis of mammary cancer. Cancer Res. 66, 5242-5250.
40. Stehlik, C. (2009) Multiple interleukin-1beta-converting enzymes contribute to inflammatory arthritis. Arthritis Rheum. 60, 3524-3530.
41. Joosten, L. A., Netea, M. G., Fantuzzi, G., Koenders, M. I., Helsen, M. M., Sparrer, H., Pham, C. T., van der Meer, J. W., Dinarello, C. A., van den Berg, W. B. (2009) Inflammatory arthritis in caspase 1 gene-deficient mice: contribution of proteinase 3 to caspase 1-independent production of bioactive interleukin-1β. Arthritis Rheum. 60, 3651-3662.
42. Fantuzzi, G., Ku, G., Harding, M. W., Livingston, D. J., Sipe, J. D., Kuida, K., Flavell, R. A., Dinarello, C. A. (1997) Response to local inflammation of IL-1 beta-converting enzyme- deficient mice. J. Immunol. 158, 1818-1824.
43. Guma, M., Ronacher, L., Liu-Bryan, R., Takai, S., Karin, M., Corr, M. (2009) Caspase 1-independent activation of interleukin-1β in neutrophilpredominant inflammation. Arthritis Rheum. 60, 3642-3650.
44. Shi, Y., Evans, J. E., Rock, K. L. (2003) Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 425, 516-521.
45. Kuida, K., Lippke, J. A., Ku, G., Harding, M. W., Livingston, D. J., Su, M. S., Flavell, R. A. (1995) Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme. Science 267, 2000-2003.
46. Kanneganti, T. D., Ozören, N., Body-Malapel, M., Amer, A., Park, J. H., Franchi, L., Whitfield, J., Barchet, W., Colonna, M., Vandenabeele, P., Bertin, J., Coyle, A., Grant, E. P., Akira, S., Núñez, G. (2006) Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature 440, 233-236.
47. Shi, G. P., Villadangos, J. A., Dranoff, G., Small, C., Gu, L., Haley, K. J., Riese, R., Ploegh, H. L., Chapman, H. A. (1999) Cathepsin S required for normal MHC class II peptide loading and germinal center development. Immunity 10, 197-206.
48. Nakagawa, T., Roth, W., Wong, P., Nelson, A., Farr, A., Deussing, J., Villadangos, J. A., Ploegh, H., Peters, C., Rudensky, A. Y. (1998) Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus. Science 280, 450-453.
49. Deussing, J., Roth, W., Saftig, P., Peters, C., Ploegh, H. L., Villadangos, J. A. (1998) Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation. Proc. Natl. Acad. Sci. USA 95, 4516-4521.
50. Pham, C. T., Ley, T. J. (1999) Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc. Natl. Acad. Sci. USA 96, 8627-8632.
51. Jensen, B. M., Swindle, E. J., Iwaki, S., Gilfillan, A. M. (2006). Generation, isolation, and maintenance of rodent mast cells and mast cell lines in Current Protocols Immunology. John Wiley & Sons, Inc., New York, Unit 3.23.
52. Gullapalli, R., Wong, A., Brigham, E., Kwong, G., Wadsworth, A., Willits, C., Quinn, K., Goldbach, E., Samant, B. (2012) Development of ALZET®osmotic pump compatible solvent compositions to solubilize poorly soluble compounds for preclinical studies. Drug Deliv. 19, 239-246.
53. Vince, J. E., Wong, W. W., Gentle, I., Lawlor, K. E., Allam, R., O’Reilly, L., Mason, K., Gross, O., Ma, S., Guarda, G., Anderton, H., Castillo, R., Häcker, G., Silke, J., Tschopp, J. (2012) Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation. Immunity 36, 215-227.
54. Cai, Q., Sun, H., Peng, Y., Lu, J., Nikolovska-Coleska, Z., McEachern, D., Liu, L., Qiu, S., Yang, C. Y., Miller, R., Yi, H., Zhang, T., Sun, D., Kang, S., Guo, M., Leopold, L., Yang, D., Wang, S. (2011) A potent and orally active antagonist (SM-406/AT-406) of multiple inhibitor of apoptosis proteins (IAPs) in clinical development for cancer treatment. J. Med. Chem. 54, 2714-2726.
55. Conus, S., Simon, H. U. (2008) Cathepsins: key modulators of cell death and inflammatory responses. Biochem. Pharmacol. 76, 1374-1382.
56. Kaiser, W. J., Upton, J. W., Long, A. B., Livingston-Rosanoff, D., Daley-Bauer, L. P., Hakem, R., Caspary, T., Mocarski, E. S. (2011) RIP3 mediates the embryonic lethality of caspase-8-deficient mice. Nature 471, 368-372.
57. Verdoes, M., Oresic Bender, K., Segal, E., van der Linden, W. A., Syed, S., Withana, N. P., Sanman, L. E., Bogyo, M. (2013) Improved quenched fluorescent probe for imaging of cysteine cathepsin activity. J. Am. Chem. Soc. 135, 14726-14730.
58. Chen, Y. T., Brinen, L. S., Kerr, I. D., Hansell, E., Doyle, P. S., McKerrow, J. H., Roush, W. R. (2010) In vitro and in vivo studies of the trypanocidal properties of WRR-483 against Trypanosoma cruzi. PLoS Negl. Trop. Dis. 4, e825.
59. + efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity 38, 1142-1153.
60. Oberle, C., Huai, J., Reinheckel, T., Tacke, M., Rassner, M., Ekert, P. G., Buellesbach, J., Borner, C. (2010) Lysosomal membrane permeabilization and cathepsin release is a Bax/Bak-dependent, amplifying event of apoptosis in fibroblasts and monocytes. Cell Death Differ. 17, 1167-1178.
61. Fehrenbacher, N., Gyrd-Hansen, M., Poulsen, B., Felbor, U., Kallunki, T., Boes, M., Weber, E., Leist, M., Jäättelä, M. (2004) Sensitization to the lysosomal cell death pathway upon immortalization and transformation. Cancer Res. 64, 5301-5310.
62. Baskin-Bey, E. S., Canbay, A., Bronk, S. F., Werneburg, N., Guicciardi, M. E., Nyberg, S. L., Gores, G. J. (2005) Cathepsin B inactivation attenuates hepatocyte apoptosis and liver damage in steatotic livers after cold ischemia-warm reperfusion injury. Am. J. Physiol. Gastrointest. Liver Physiol. 288, G396-G402.
63. Guicciardi, M. E., Deussing, J., Miyoshi, H., Bronk, S. F., Svingen, P. A., Peters, C., Kaufmann, S. H., Gores, G. J. (2000) Cathepsin B contributes to TNF-α-mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c. J. Clin. Invest. 106, 1127-1137.
64. Guicciardi, M. E., Bronk, S. F., Werneburg, N. W., Gores, G. J. (2007) cFLIPL prevents TRAIL-induced apoptosis of hepatocellular carcinoma cells by inhibiting the lysosomal pathway of apoptosis. Am. J. Physiol. Gastrointest. Liver Physiol. 292, G1337-G1346.
65. Foghsgaard, L., Wissing, D., Mauch, D., Lademann, U., Bastholm, L., Boes, M., Elling, F., Leist, M., Jäättelä, M. (2001) Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor. J. Cell Biol. 153, 999-1010.
66. Di Piazza, M., Mader, C., Geletneky, K., Herrero Y Calle, M., Weber, E., Schlehofer, J., Deleu, L., Rommelaere, J. (2007) Cytosolic activation of cathepsins mediates parvovirus H-1-induced killing of cisplatin and TRAIL-resistant glioma cells. J. Virol. 81, 4186-4198.
67. Zhang, H., Zhong, C., Shi, L., Guo, Y., Fan, Z. (2009) Granulysin induces cathepsin B release from lysosomes of target tumor cells to attack mitochondria through processing of bid leading to Necroptosis. J. Immunol. 182, 6993-7000.
68. Zhou, Z. D., Yap, B. P., Gung, A. Y., Leong, S. M., Ang, S. T., Lim, T. M. (2006) Dopamine-related and caspase-independent apoptosis in dopaminergic neurons induced by overexpression of human wild type or mutant alpha-synuclein. Exp. Cell Res. 312, 156-170.
69. Michallet, M. C., Saltel, F., Flacher, M., Revillard, J. P., Genestier, L. (2004) Cathepsin-dependent apoptosis triggered by supraoptimal activation of T lymphocytes: a possible mechanism of high dose tolerance. J. Immunol. 172, 5405-5414.
70. Nylandsted, J., Rohde, M., Brand, K., Bastholm, L., Elling, F., Jäättelä, M. (2000) Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2. Proc. Natl. Acad. Sci. USA 97, 7871-7876.
71. Ostenfeld, M. S., Fehrenbacher, N., Høyer-Hansen, M., Thomsen, C., Farkas, T., Jäättelä, M. (2005) Effective tumor cell death by sigma-2 receptor ligand siramesine involves lysosomal leakage and oxidative stress. Cancer Res. 65, 8975-8983.
72. Nylandsted, J., Gyrd-Hansen, M., Danielewicz, A., Fehrenbacher, N., Lademann, U., Høyer-Hansen, M., Weber, E., Multhoff, G., Rohde, M., Jäättelä, M. (2004) Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization. J. Exp. Med. 200, 425-435.
73. Niemi, K., Teirilä, L., Lappalainen, J., Rajamäki, K., Baumann, M. H., Öörni, K., Wolff, H., Kovanen, P. T., Matikainen, S., Eklund, K. K. (2011) Serum amyloid A activates the NLRP3 inflammasome via P2X7 receptor and a cathepsin B-sensitive pathway. J. Immunol. 186, 6119-6128.
74. Meixenberger, K., Pache, F., Eitel, J., Schmeck, B., Hippenstiel, S., Slevogt, H., N’Guessan, P., Witzenrath, M., Netea, M. G., Chakraborty, T., Suttorp, N., Opitz, B. (2010) Listeria monocytogenes -infected human peripheral blood mononuclear cells produce IL-1beta, depending on listeriolysin O and NLRP3. J. Immunol. 184, 922-930.
75. Masters, S. L., Dunne, A., Subramanian, S. L., Hull, R. L., Tannahill, G. M., Sharp, F. A., Becker, C., Franchi, L., Yoshihara, E., Chen, Z., Mullooly, N., Mielke, L. A., Harris, J., Coll, R. C., Mills, K. H., Mok, K. H., Newsholme, P., Nuñez, G., Yodoi, J., Kahn, S. E., Lavelle, E. C., O’Neill, L. A. (2010) Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes. Nat. Immunol. 11, 897-904.
76. Hentze, H., Lin, X. Y., Choi, M. S., Porter, A. G. (2003) Critical role for cathepsin B in mediating caspase-1-dependent interleukin-18 maturation and caspase-1-independent necrosis triggered by the microbial toxin nigericin. Cell Death Differ. 10, 956-968.
77. Heid, M. E., Keyel, P. A., Kamga, C., Shiva, S., Watkins, S. C., Salter, R. D. (2013) Mitochondrial reactive oxygen species induces NLRP3-dependent lysosomal damage and inflammasome activation. J. Immunol. 191, 5230-5238.
78. Rintahaka, J., Lietzén, N., Öhman, T., Nyman, T. A., Matikainen, S. (2011) Recognition of cytoplasmic RNA results in cathepsin-dependent inflammasome activation and apoptosis in human macrophages. J. Immunol. 186, 3085-3092.
79. Saito, M., Nishikomori, R., Kambe, N., Fujisawa, A., Tanizaki, H., Takeichi, K., Imagawa, T., Iehara, T., Takada, H., Matsubayashi, T., Tanaka, H., Kawashima, H., Kawakami, K., Kagami, S., Okafuji, I., Yoshioka, T., Adachi, S., Heike, T., Miyachi, Y., Nakahata, T. (2008) Disease-associated CIAS1 mutations induce monocyte death, revealing low-level mosaicism in mutation-negative cryopyrin-associated periodic syndrome patients. Blood 111, 2132-2141.
80. Fujisawa, A., Kambe, N., Saito, M., Nishikomori, R., Tanizaki, H., Kanazawa, N., Adachi, S., Heike, T., Sagara, J., Suda, T., Nakahata, T., Miyachi, Y. (2007) Disease-associated mutations in CIAS1 induce cathepsin B-dependent rapid cell death of human THP-1 monocytic cells. Blood 109, 2903-2911.
81. Moore, S. F., MacKenzie, A. B. (2009) NADPH oxidase NOX2 mediates rapid cellular oxidation following ATP stimulation of endotoxin-primed macrophages. J. Immunol. 183, 3302-3308.