اینفلامازوم و نقش آنها در بیماری‌ها

نوع مقاله : مقاله مروری

نویسندگان

1 دانشجوی دکتری، گروه بیوتکنولوژی، دانشکده‌ی دامپزشکی، دانشگاه فردوسی مشهد، مشهد، ایران

2 استادیار، گروه ایمونولوژی و بیوتکنولوژی، دانشکده‌ی دامپزشکی و پژوهشکده‌ی فناوری زیستی، دانشگاه فردوسی مشهد، مشهد، ایران

چکیده

اینفلامازوم‌ها گیرنده‌های سیتوزولی هستند که توانایی شناسایی پاتوژن‌های میکروبی و سیگنال‌های خطرناک درون زاد حاصل از استرس یا آسیب سلولی را دارند. کمپلکس اینفلامازوم یا از اعضای خانواده‌ی پروتئینی NLR (Nod-like receptor) است و یا از 2AIM (2Absent in melanoma) که عضو خانواده‌ی پروتئینی PYHIN است، شکل می‌گیرد. فعال شدن اینفلامازوم سبب فعال شدن کاسپاز التهابی به نام کاسپاز1 می‌گردد که این به نوبه‌ی خود، باعث بلوغ سایتوکاین‌های التهاب‌زا می‌شود. در این مقاله، در ابتدا انواع اینفلامازوم‌های شناخته شده و ویژگی‌های ساختاری آن‌ها معرفی می‌شوند و سپس مکانیسم‌های مولکولی انواع اینفلامازوم در چندین بیماری مطرح می‌گردند. فهم این مکانیسم‌ها، علاوه بر فراهم آوردن اطلاعات ارزشمند در مورد چگونگی تکوین و گسترش این اختلالات، می‌تواند در دریافت راه‌های جدید درمانی نیز مؤثر باشد. 

کلیدواژه‌ها

عنوان مقاله [English]

Inflammasomes and Their Role in Diseases

نویسندگان [English]

  • Amin Tavassoli 1
  • Alireza Haghparast 2
1 PhD Candidate, Department of Biotechnology, School of Veterinary Medicine, Ferdowsi University of Mashhad, Mashhad, Iran
2 Assistant Professor, Department of Immunology and Biotechnology, School of Veterinary Medicine AND Institute of Biotechnology, Ferdowsi University of Mashhad, Mashhad, Iran
چکیده [English]

Inflammasomes are cytosolic receptors which can detect microbial pathogens and endogenous danger signals resulting from stress or cell damages. Inflammasome complexes are either formed in cytosol by NOD (nucleotide-binding oligomerization domain)-like receptor (NLRs) family or the absent in melanoma 2 (Aim2) protein, a member of PYHIN (pyrin and HIN domain-containing protein) family. Inflammasome activation leads to the activation of caspase 1, which in turns leads to the maturation of pro-inflammatory cytokines. In this review, first the structural features and biological functions of different types of inflammasomes will be discussed and then we will focus on the molecular mechanisms of inflammasomes in several diseases pathogenesis. Understanding these mechanisms will provide us with valuable information underlying disease pathogenesis as well as development of new and effective therapeutic and preventive strategies to combat these disorders.

مراجع

  1. Khare S, Luc N, Dorfleutner A, Stehlik C. Inflammasomes and their activation. Crit Rev Immunol 2010; 30(5): 463-87.
  2. Janeway CA, Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol 1989; 54 Pt 1: 1-13.
  3. Mankan AK, Kubarenko A, Hornung V. Immunology in clinic review series; focus on autoinflammatory diseases: inflammasomes: mechanisms of activation. Clin Exp Immunol 2012; 167(3): 369-81.
  4. Wells JM, Rossi O, Meijerink M, van BP. Epithelial crosstalk at the microbiota-mucosal interface. Proc Natl Acad Sci U S A 2011; 108(Suppl 1): 4607-14.
  5. Franchi L, Nunez G. Immunology. Orchestrating inflammasomes. Science 2012; 337(6100): 1299-300.
  6. Abdul-Sater AA, Said-Sadier N, Ojcius DM, Yilmaz O, Kelly KA. Inflammasomes bridge signaling between pathogen identification and the immune response. Drugs Today (Barc ) 2009; 45(Suppl B): 105-12.
  7. Haghparast A, Heidari KM, Malvandi AM. Down-regulation of CD14 transcripts in human glioblastoma cell line U87 MG. Iran J Immunol 2011; 8(2): 111-9.
  8. Suzuki S, Franchi L, He Y, Munoz-Planillo R, Mimuro H, Suzuki T, et al. Shigella type III secretion protein MxiI is recognized by Naip2 to induce Nlrc4 inflammasome activation independently of Pkcdelta. PLoS Pathog 2014; 10(2): e1003926.
  9. Baccala R, Gonzalez-Quintial R, Lawson BR, Stern ME, Kono DH, Beutler B, et al. Sensors of the innate immune system: their mode of action. Nat Rev Rheumatol 2009; 5(8): 448-56.
  10. Burckstummer T, Baumann C, Bluml S, Dixit E, Durnberger G, Jahn H, et al. An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. Nat Immunol 2009; 10(3): 266-72.
  11. Fernandes-Alnemri T, Yu JW, Datta P, Wu J, Alnemri ES. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 2009; 458(7237): 509-13.
  12. Tschopp J, Martinon F, Burns K. NALPs: a novel protein family involved in inflammation. Nat Rev Mol Cell Biol 2003; 4(2): 95-104.
  13. Keller M, Ruegg A, Werner S, Beer HD. Active caspase-1 is a regulator of unconventional protein secretion. Cell 2008; 132(5): 818-31.
  14. Ting JP, Lovering RC, Alnemri ES, Bertin J, Boss JM, Davis BK, et al. The NLR gene family: a standard nomenclature. Immunity 2008; 28(3): 285-7.
  15. Hornung V, Ablasser A, Charrel-Dennis M, Bauernfeind F, Horvath G, Caffrey DR, et al. AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature 2009; 458(7237): 514-8.
  16. Jin T, Perry A, Jiang J, Smith P, Curry JA, Unterholzner L, et al. Structures of the HIN domain:DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor. Immunity 2012; 36(4): 561-71.
  17. Bauernfeind F, Bartok E, Rieger A, Franchi L, Nunez G, Hornung V. Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J Immunol 2011; 187(2): 613-7.
  18. Bauernfeind F, Hornung V. Of inflammasomes and pathogens--sensing of microbes by the inflammasome. EMBO Mol Med 2013; 5(6): 814-26.
  19. Yuan S, Yu X, Topf M, Ludtke SJ, Wang X, Akey CW. Structure of an apoptosome-procaspase-9 CARD complex. Structure 2010; 18(5): 571-83.
  20. Yuan S, Yu X, Topf M, Dorstyn L, Kumar S, Ludtke SJ, et al. Structure of the Drosophila apoptosome at 6.9 a resolution. Structure 2011; 19(1): 128-40.
  21. Shirasu K. The HSP90-SGT1 chaperone complex for NLR immune sensors. Annu Rev Plant Biol 2009; 60: 139-64.
  22. Ting JP, Duncan JA, Lei Y. How the noninflammasome NLRs function in the innate immune system. Science 2010; 327(5963): 286-90.
  23. Kadota Y, Shirasu K, Guerois R. NLR sensors meet at the SGT1-HSP90 crossroad. Trends Biochem Sci 2010; 35(4): 199-207.
  24. Mayor A, Martinon F, De ST, Petrilli V, Tschopp J. A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses. Nat Immunol 2007; 8(5): 497-503.
  25. Zhou R, Tardivel A, Thorens B, Choi I, Tschopp J. Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nat Immunol 2010; 11(2): 136-40.
  26. Zhou R, Yazdi AS, Menu P, Tschopp J. A role for mitochondria in NLRP3 inflammasome activation. Nature 2011; 469(7329): 221-5.
  27. Inohara N, Koseki T, del PL, Hu Y, Yee C, Chen S, et al. Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB. J Biol Chem 1999; 274(21): 14560-7.
  28. Tada H, Aiba S, Shibata K, Ohteki T, Takada H. Synergistic effect of Nod1 and Nod2 agonists with toll-like receptor agonists on human dendritic cells to generate interleukin-12 and T helper type 1 cells. Infect Immun 2005; 73(12): 7967-76.
  29. Ogura Y, Lala S, Xin W, Smith E, Dowds TA, Chen FF, et al. Expression of NOD2 in Paneth cells: a possible link to Crohn's ileitis. Gut 2003; 52(11): 1591-7.
  30. Hisamatsu T, Suzuki M, Reinecker HC, Nadeau WJ, McCormick BA, Podolsky DK. CARD15/NOD2 functions as an antibacterial factor in human intestinal epithelial cells. Gastroenterology 2003; 124(4): 993-1000.
  31. Barnich N, Aguirre JE, Reinecker HC, Xavier R, Podolsky DK. Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition. J Cell Biol 2005; 170(1): 21-6.
  32. Hasegawa M, Yang K, Hashimoto M, Park JH, Kim YG, Fujimoto Y, et al. Differential release and distribution of Nod1 and Nod2 immunostimulatory molecules among bacterial species and environments. J Biol Chem 2006; 281(39): 29054-63.
  33. Shaw PJ, Lamkanfi M, Kanneganti TD. NOD-like receptor (NLR) signaling beyond the inflammasome. Eur J Immunol 2010; 40(3): 624-7.
  34. Asoodeh A, Haghparast A, Kashef R, Chamani J. Pro-Inflammatory Cytokine Responses of A549 Epithelial Cells to Antimicrobial Peptide Brevinin-2R. Int J Pept Res Ther 2013; 19(2): 157-62.
  35. Martinon F, Burns K, Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 2002; 10(2): 417-26.
  36. Letunic I, Doerks T, Bork P. SMART 6: recent updates and new developments. Nucleic Acids Res 2009; 37(Database issue): D229-D232.
  37. Schultz J, Milpetz F, Bork P, Ponting CP. SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci U S A 1998; 95(11): 5857-64.
  38. Faustin B, Lartigue L, Bruey JM, Luciano F, Sergienko E, Bailly-Maitre B, et al. Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol Cell 2007; 25(5): 713-24.
  39. Gorfu G, Cirelli KM, Melo MB, Mayer-Barber K, Crown D, Koller BH, et al. Dual role for inflammasome sensors NLRP1 and NLRP3 in murine resistance to Toxoplasma gondii. MBio 2014; 5(1).
  40. Boyden ED, Dietrich WF. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat Genet 2006; 38(2): 240-4.
  41. Newman ZL, Leppla SH, Moayeri M. CA-074Me protection against anthrax lethal toxin. Infect Immun 2009; 77(10): 4327-36.
  42. Agostini L, Martinon F, Burns K, McDermott MF, Hawkins PN, Tschopp J. NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity 2004; 20(3): 319-25.
  43. Rathinam VA, Vanaja SK, Waggoner L, Sokolovska A, Becker C, Stuart LM, et al. TRIF licenses caspase-11-dependent NLRP3 inflammasome activation by gram-negative bacteria. Cell 2012; 150(3): 606-19.
  44. Allen IC, Scull MA, Moore CB, Holl EK, McElvania-TeKippe E, Taxman DJ, et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity 2009; 30(4): 556-65.
  45. Gross O, Poeck H, Bscheider M, Dostert C, Hannesschlager N, Endres S, et al. Syk kinase signalling couples to the Nlrp3 inflammasome for anti-fungal host defence. Nature 2009; 459(7245): 433-6.
  46. Mariathasan S, Weiss DS, Newton K, McBride J, O'Rourke K, Roose-Girma M, et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 2006; 440(7081): 228-32.
  47. Harder J, Franchi L, Munoz-Planillo R, Park JH, Reimer T, Nunez G. Activation of the Nlrp3 inflammasome by Streptococcus pyogenes requires streptolysin O and NF-kappa B activation but proceeds independently of TLR signaling and P2X7 receptor. J Immunol 2009; 183(9): 5823-9.
  48. Ichinohe T, Pang IK, Iwasaki A. Influenza virus activates inflammasomes via its intracellular M2 ion channel. Nat Immunol 2010; 11(5): 404-10.
  49. Martinon F, Petrilli V, Mayor A, Tardivel A, Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 2006; 440(7081): 237-41.
  50. Halle A, Hornung V, Petzold GC, Stewart CR, Monks BG, Reinheckel T, et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol 2008; 9(8): 857-65.
  51. Duewell P, Kono H, Rayner KJ, Sirois CM, Vladimer G, Bauernfeind FG, et al. NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature 2010; 464(7293): 1357-61.
  52. Dostert C, Petrilli V, Van Bruggen R, Steele C, Mossman BT, Tschopp J. Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science 2008; 320(5876): 674-7.
  53. Cassel SL, Sutterwala FS. Sterile inflammatory responses mediated by the NLRP3 inflammasome. Eur J Immunol 2010; 40(3): 607-11.
  54. Franchi L, Munoz-Planillo R, Reimer T, Eigenbrod T, Nunez G. Inflammasomes as microbial sensors. Eur J Immunol 2010; 40(3): 611-5.
  55. Sodergren E, Weinstock GM, Davidson EH, Cameron RA, Gibbs RA, Angerer RC, et al. The genome of the sea urchin Strongylocentrotus purpuratus. Science 2006; 314(5801): 941-52.
  56. Iyer SS, Pulskens WP, Sadler JJ, Butter LM, Teske GJ, Ulland TK, et al. Necrotic cells trigger a sterile inflammatory response through the Nlrp3 inflammasome. Proc Natl Acad Sci U S A 2009; 106(48): 20388-93.
  57. Compan V, Baroja-Mazo A, Lopez-Castejon G, Gomez AI, Martinez CM, Angosto D, et al. Cell volume regulation modulates NLRP3 inflammasome activation. Immunity 2012; 37(3): 487-500.
  58. Ghiringhelli F, Apetoh L, Tesniere A, Aymeric L, Ma Y, Ortiz C, et al. Activation of the NLRP3 inflammasome in dendritic cells induces IL-1beta-dependent adaptive immunity against tumors. Nat Med 2009; 15(10): 1170-8.
  59. Ichinohe T, Lee HK, Ogura Y, Flavell R, Iwasaki A. Inflammasome recognition of influenza virus is essential for adaptive immune responses. J Exp Med 2009; 206(1): 79-87.
  60. Kanneganti TD, Body-Malapel M, Amer A, Park JH, Whitfield J, Franchi L, et al. Critical role for Cryopyrin/Nalp3 in activation of caspase-1 in response to viral infection and double-stranded RNA. J Biol Chem 2006; 281(48): 36560-8.
  61. Ghaemi-Bafghi M, Haghparast A. Viral evasion and subversion mechanisms of the host immune system. Zahedan J Res Med Sci 2013; 15(10): 1-6.
  62. Hise AG, Tomalka J, Ganesan S, Patel K, Hall BA, Brown GD, et al. An essential role for the NLRP3 inflammasome in host defense against the human fungal pathogen Candida albicans. Cell Host Microbe 2009; 5(5): 487-97.
  63. Dostert C, Guarda G, Romero JF, Menu P, Gross O, Tardivel A, et al. Malarial hemozoin is a Nalp3 inflammasome activating danger signal. PLoS One 2009; 4(8): e6510.
  64. Shio MT, Eisenbarth SC, Savaria M, Vinet AF, Bellemare MJ, Harder KW, et al. Malarial hemozoin activates the NLRP3 inflammasome through Lyn and Syk kinases. PLoS Pathog 2009; 5(8): e1000559.
  65. Hornung V, Bauernfeind F, Halle A, Samstad EO, Kono H, Rock KL, et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol 2008; 9(8): 847-56.
  66. Lima-Junior DS, Costa DL, Carregaro V, Cunha LD, Silva AL, Mineo TW, et al. Inflammasome-derived IL-1beta production induces nitric oxide-mediated resistance to Leishmania. Nat Med 2013; 19(7): 909-15.
  67. Grenier JM, Wang L, Manji GA, Huang WJ, Al-Garawi A, Kelly R, et al. Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-kappaB and caspase-1. FEBS Lett 2002; 530(1-3): 73-8.
  68. Elinav E, Strowig T, Kau AL, Henao-Mejia J, Thaiss CA, Booth CJ, et al. NLRP6 inflammasome regulates colonic microbial ecology and risk for colitis. Cell 2011; 145(5): 745-57.
  69. Wang L, Manji GA, Grenier JM, Al-Garawi A, Merriam S, Lora JM, et al. PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-kappa B and caspase-1-dependent cytokine processing. J Biol Chem 2002; 277(33): 29874-80.
  70. Mariathasan S, Newton K, Monack DM, Vucic D, French DM, Lee WP, et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 2004; 430(6996): 213-8.
  71. Poyet JL, Srinivasula SM, Tnani M, Razmara M, Fernandes-Alnemri T, Alnemri ES. Identification of Ipaf, a human caspase-1-activating protein related to Apaf-1. J Biol Chem 2001; 276(30): 28309-13.
  72. Miao EA, Mao DP, Yudkovsky N, Bonneau R, Lorang CG, Warren SE, et al. Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome. Proc Natl Acad Sci U S A 2010; 107(7): 3076-80.
  73. Zamboni DS, Kobayashi KS, Kohlsdorf T, Ogura Y, Long EM, Vance RE, et al. The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection. Nat Immunol 2006; 7(3): 318-25.
  74. Damm A, Lautz K, Kufer TA. Roles of NLRP10 in innate and adaptive immunity. Microbes Infect 2013; 15(6-7): 516-23.
  75. Wang Y, Hasegawa M, Imamura R, Kinoshita T, Kondo C, Konaka K, et al. PYNOD, a novel Apaf-1/CED4-like protein is an inhibitor of ASC and caspase-1. Int Immunol 2004; 16(6): 777-86.
  76. Lech M, Avila-Ferrufino A, Skuginna V, Susanti HE, Anders HJ. Quantitative expression of RIG-like helicase, NOD-like receptor and inflammasome-related mRNAs in humans and mice. Int Immunol 2010; 22(9): 717-28.
  77. Krishnaswamy JK, Chu T, Eisenbarth SC. Beyond pattern recognition: NOD-like receptors in dendritic cells. Trends Immunol 2013; 34(5): 224-33.
  78. Eisenbarth SC, Williams A, Colegio OR, Meng H, Strowig T, Rongvaux A, et al. NLRP10 is a NOD-like receptor essential to initiate adaptive immunity by dendritic cells. Nature 2012; 484(7395): 510-3.
  79. Roberts TL, Idris A, Dunn JA, Kelly GM, Burnton CM, Hodgson S, et al. HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA. Science 2009; 323(5917): 1057-60.
  80. Kawane K, Ohtani M, Miwa K, Kizawa T, Kanbara Y, Yoshioka Y, et al. Chronic polyarthritis caused by mammalian DNA that escapes from degradation in macrophages. Nature 2006; 443(7114): 998-1002.
  81. Rathinam VA, Jiang Z, Waggoner SN, Sharma S, Cole LE, Waggoner L, et al. The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat Immunol 2010; 11(5): 395-402.
  82. Kim S, Bauernfeind F, Ablasser A, Hartmann G, Fitzgerald KA, Latz E, et al. Listeria monocytogenes is sensed by the NLRP3 and AIM2 inflammasome. Eur J Immunol 2010; 40(6): 1545-51.
  83. Fernandes-Alnemri T, Yu JW, Juliana C, Solorzano L, Kang S, Wu J, et al. The AIM2 inflammasome is critical for innate immunity to Francisella tularensis. Nat Immunol 2010; 11(5): 385-93.
  84. Ge J, Gong YN, Xu Y, Shao F. Preventing bacterial DNA release and absent in melanoma 2 inflammasome activation by a Legionella effector functioning in membrane trafficking. Proc Natl Acad Sci U S A 2012; 109(16): 6193-8.
  85. Liu L, Chan C. The role of inflammasome in Alzheimer's disease. Ageing Res Rev 2014; 15: 6-15.
  86. Frackowiak J, Wisniewski HM, Wegiel J, Merz GS, Iqbal K, Wang KC. Ultrastructure of the microglia that phagocytose amyloid and the microglia that produce beta-amyloid fibrils. Acta Neuropathol 1992; 84(3): 225-33.
  87. Mueller-Steiner S, Zhou Y, Arai H, Roberson ED, Sun B, Chen J, et al. Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease. Neuron 2006; 51(6): 703-14.
  88. Lusis AJ. Atherosclerosis. Nature 2000; 407(6801): 233-41.
  89. Wright SD, Burton C, Hernandez M, Hassing H, Montenegro J, Mundt S, et al. Infectious agents are not necessary for murine atherogenesis. J Exp Med 2000; 191(8): 1437-42.
  90. Goldstein JL, Brown MS. Lipoprotein receptors, cholesterol metabolism, and atherosclerosis. Arch Pathol 1975; 99(4): 181-4.
  91. Rajamaki K, Lappalainen J, Oorni K, Valimaki E, Matikainen S, Kovanen PT, et al. Cholesterol crystals activate the NLRP3 inflammasome in human macrophages: a novel link between cholesterol metabolism and inflammation. PLoS One 2010; 5(7): e11765.
  92. Stewart CR, Stuart LM, Wilkinson K, van Gils JM, Deng J, Halle A, et al. CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer. Nat Immunol 2010; 11(2): 155-61.
  93. Kleemann R, Zadelaar S, Kooistra T. Cytokines and atherosclerosis: a comprehensive review of studies in mice. Cardiovasc Res 2008; 79(3): 360-76.
  94. Febbraio M, Podrez EA, Smith JD, Hajjar DP, Hazen SL, Hoff HF, et al. Targeted disruption of the class B scavenger receptor CD36 protects against atherosclerotic lesion development in mice. J Clin Invest 2000; 105(8): 1049-56.
  95. Napoli C, de NF, Palinski W. Multiple role of reactive oxygen species in the arterial wall. J Cell Biochem 2001; 82(4): 674-82.
  96. De ND, Latz E. NLRP3 inflammasomes link inflammation and metabolic disease. Trends Immunol 2011; 32(8): 373-9.
  97. Kahn SE, Hull RL, Utzschneider KM. Mechanisms linking obesity to insulin resistance and type 2 diabetes. Nature 2006; 444(7121): 840-6.
  98. de Koning EJ, van den Brand JJ, Mott VL, Charge SB, Hansen BC, Bodkin NL, et al. Macrophages and pancreatic islet amyloidosis. Amyloid 1998; 5(4): 247-54.
  99. Masters SL, Dunne A, Subramanian SL, Hull RL, Tannahill GM, Sharp FA, et al. Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1beta in type 2 diabetes. Nat Immunol 2010; 11(10): 897-904.
  100. Dixit VD. Nlrp3 inflammasome activation in type 2 diabetes: is it clinically relevant? Diabetes 2013; 62(1): 22-4.
  101. Feldmann J, Prieur AM, Quartier P, Berquin P, Certain S, Cortis E, et al. Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes. Am J Hum Genet 2002; 71(1): 198-203.
  102. Hoffman HM, Mueller JL, Broide DH, Wanderer AA, Kolodner RD. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat Genet 2001; 29(3): 301-5.
  103. Dowds TA, Masumoto J, Zhu L, Inohara N, Nunez G. Cryopyrin-induced interleukin 1beta secretion in monocytic cells: enhanced activity of disease-associated mutants and requirement for ASC. J Biol Chem 2004; 279(21): 21924-8.
  104. Brydges SD, Mueller JL, McGeough MD, Pena CA, Misaghi A, Gandhi C, et al. Inflammasome-mediated disease animal models reveal roles for innate but not adaptive immunity. Immunity 2009; 30(6): 875-87.
  105. Meng G, Zhang F, Fuss I, Kitani A, Strober W. A mutation in the Nlrp3 gene causing inflammasome hyperactivation potentiates Th17 cell-dominant immune responses. Immunity 2009; 30(6): 860-74.
  106. Ozkurede VU, Franchi L. Immunology in clinic review series; focus on autoinflammatory diseases: role of inflammasomes in autoinflammatory syndromes. Clin Exp Immunol 2012; 167(3): 382-90.
  107. Zitvogel L, Kepp O, Galluzzi L, Kroemer G. Inflammasomes in carcinogenesis and anticancer immune responses. Nat Immunol 2012; 13(4): 343-51.
  108. Tanaka T, Kohno H, Suzuki R, Yamada Y, Sugie S, Mori H. A novel inflammation-related mouse colon carcinogenesis model induced by azoxymethane and dextran sodium sulfate. Cancer Sci 2003; 94(11): 965-73.
  109. Huber S, Gagliani N, Zenewicz LA, Huber FJ, Bosurgi L, Hu B, et al. IL-22BP is regulated by the inflammasome and modulates tumorigenesis in the intestine. Nature 2012; 491(7423): 259-63.
  110. Nunes T, de Souza HS. Inflammasome in intestinal inflammation and cancer. Mediators Inflamm 2013; 2013: 654963.
  111. Salcedo R, Worschech A, Cardone M, Jones Y, Gyulai Z, Dai RM, et al. MyD88-mediated signaling prevents development of adenocarcinomas of the colon: role of interleukin 18. J Exp Med 2010; 207(8): 1625-36.
  112. Zaki MH, Vogel P, Body-Malapel M, Lamkanfi M, Kanneganti TD. IL-18 production downstream of the Nlrp3 inflammasome confers protection against colorectal tumor formation. J Immunol 2010; 185(8): 4912-20.
  113. Hu B, Elinav E, Huber S, Booth CJ, Strowig T, Jin C, et al. Inflammation-induced tumorigenesis in the colon is regulated by caspase-1 and NLRC4. Proc Natl Acad Sci U S A 2010; 107(50): 21635-40.
  114. Normand S, Delanoye-Crespin A, Bressenot A, Huot L, Grandjean T, Peyrin-Biroulet L, et al. Nod-like receptor pyrin domain-containing protein 6 (NLRP6) controls epithelial self-renewal and colorectal carcinogenesis upon injury. Proc Natl Acad Sci U S A 2011; 108(23): 9601-6.
  115. Kingsbury SR, Conaghan PG, McDermott MF. The role of the NLRP3 inflammasome in gout. J Inflamm Res 2011; 4: 39-49.
  116. Yagnik DR, Hillyer P, Marshall D, Smythe CD, Krausz T, Haskard DO, et al. Noninflammatory phagocytosis of monosodium urate monohydrate crystals by mouse macrophages. Implications for the control of joint inflammation in gout. Arthritis Rheum 2000; 43(8): 1779-89.
  117. Landis RC, Yagnik DR, Florey O, Philippidis P, Emons V, Mason JC, et al. Safe disposal of inflammatory monosodium urate monohydrate crystals by differentiated macrophages. Arthritis Rheum 2002; 46(11): 3026-33.
  118. Shi Y, Evans JE, Rock KL. Molecular identification of a danger signal that alerts the immune system to dying cells. Nature 2003; 425(6957): 516-21.
  119. Liu-Bryan R, Scott P, Sydlaske A, Rose DM, Terkeltaub R. Innate immunity conferred by Toll-like receptors 2 and 4 and myeloid differentiation factor 88 expression is pivotal to monosodium urate monohydrate crystal-induced inflammation. Arthritis Rheum 2005; 52(9): 2936-46.
  120. Jin Y, Mailloux CM, Gowan K, Riccardi SL, LaBerge G, Bennett DC, et al. NALP1 in vitiligo-associated multiple autoimmune disease. N Engl J Med 2007; 356(12): 1216-25.
  121. Martinon F, Mayor A, Tschopp J. The inflammasomes: guardians of the body. Annu Rev Immunol 2009; 27: 229-65.
  122. Jeru I, Duquesnoy P, Fernandes-Alnemri T, Cochet E, Yu JW, Lackmy-Port-Lis M, et al. Mutations in NALP12 cause hereditary periodic fever syndromes. Proc Natl Acad Sci U S A 2008; 105(5): 1614-9.
  123. Banwell V, Sena ES, Macleod MR. Systematic review and stratified meta-analysis of the efficacy of interleukin-1 receptor antagonist in animal models of stroke. J Stroke Cerebrovasc Dis 2009; 18(4): 269-76.
  124. Wanderer AA. Rationale for IL-1beta targeted therapy for ischemia-reperfusion induced pulmonary and other complications in sickle cell disease. J Pediatr Hematol Oncol 2009; 31(8): 537-8.
  125. Tabatabaeizadeh SE, Haghparast A. Improving the effectiveness of adjuvants: targeting innate immune receptors with a special focus on toll-like receptor agonists. J Isfahan Med Sch 2013; 30(214): 1986-2009. [In Persian].
  126. Hoffman HM. Therapy of autoinflammatory syndromes. J Allergy Clin Immunol 2009; 124(6): 1129-38.
  127. Hawkins PN, Lachmann HJ, McDermott MF. Interleukin-1-receptor antagonist in the Muckle-Wells syndrome. N Engl J Med 2003; 348(25): 2583-4.
  128. Quiniou C, Sapieha P, Lahaie I, Hou X, Brault S, Beauchamp M, et al. Development of a novel noncompetitive antagonist of IL-1 receptor. J Immunol 2008; 180(10): 6977-87.
  129. Molad Y. Update on colchicine and its mechanism of action. Curr Rheumatol Rep 2002; 4(3): 252-6.
  130. Crittenden DB, Pillinger MH. New therapies for gout. Annu Rev Med 2013; 64: 325-37.
  131. Lamkanfi M, Mueller JL, Vitari AC, Misaghi S, Fedorova A, Deshayes K, et al. Glyburide inhibits the Cryopyrin/Nalp3 inflammasome. J Cell Biol 2009; 187(1): 61-70.
مجله دانشکده پزشکی اصفهان
دوره 32، شماره 304 - شماره پیاپی 304
آذر و دی 1393
صفحه 1668-1689

فایل ها

سابقه مقاله

  • تاریخ دریافت: 20 اسفند 1392
  • تاریخ بازنگری: 11 آبان 1403
  • تاریخ پذیرش: 17 فروردین 1401

هم رسانی

ارجاع به این مقاله

آمار