메뉴 건너뛰기




Volumn 26, Issue 5, 2015, Pages 263-271

Mitochondria in autoinflammation: Cause, mediator or bystander?

Author keywords

Autoinflammation; Inflammasome; Interleukin 1 ; Mitochondria

Indexed keywords

CALCIUM; GUANOSINE TRIPHOSPHATASE; INFLAMMASOME; MITOCHONDRIAL DNA; REACTIVE OXYGEN METABOLITE; DNA;

EID: 84928703375     PISSN: 10432760     EISSN: 18793061     Source Type: Journal    
DOI: 10.1016/j.tem.2015.03.004     Document Type: Review
Times cited : (27)

References (87)
  • 1
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance J.E. Phospholipid synthesis in a membrane fraction associated with mitochondria. J. Biol. Chem. 1990, 265:7248-7256.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 2
    • 66749163678 scopus 로고    scopus 로고
    • Disulfide formation in the ER and mitochondria: two solutions to a common process
    • Riemer J., et al. Disulfide formation in the ER and mitochondria: two solutions to a common process. Science 2009, 324:1284-1287.
    • (2009) Science , vol.324 , pp. 1284-1287
    • Riemer, J.1
  • 3
    • 84871726622 scopus 로고    scopus 로고
    • Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM)
    • Raturi A., Simmen T. Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM). Biochim. Biophys. Acta 2013, 1833:213-224.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 213-224
    • Raturi, A.1    Simmen, T.2
  • 4
    • 84879165160 scopus 로고    scopus 로고
    • Oxidative stress: the mitochondria-dependent and mitochondria-independent pathways of apoptosis
    • Sinha K., et al. Oxidative stress: the mitochondria-dependent and mitochondria-independent pathways of apoptosis. Arch. Toxicol. 2013, 87:1157-1180.
    • (2013) Arch. Toxicol. , vol.87 , pp. 1157-1180
    • Sinha, K.1
  • 5
    • 79955161193 scopus 로고    scopus 로고
    • Mitochondria: Sovereign of inflammation?
    • Tschopp J. Mitochondria: Sovereign of inflammation?. Eur. J. Immunol. 2011, 41:1196-1202.
    • (2011) Eur. J. Immunol. , vol.41 , pp. 1196-1202
    • Tschopp, J.1
  • 6
    • 77952294609 scopus 로고    scopus 로고
    • The sterile inflammatory response
    • Rock K.L., et al. The sterile inflammatory response. Annu. Rev. Immunol. 2010, 28:321-342.
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 321-342
    • Rock, K.L.1
  • 7
    • 84922515812 scopus 로고    scopus 로고
    • The hereditary autoinflammatory disorders uncovered
    • Rigante D., et al. The hereditary autoinflammatory disorders uncovered. Autoimmun. Rev. 2014, 13:892-900.
    • (2014) Autoimmun. Rev. , vol.13 , pp. 892-900
    • Rigante, D.1
  • 8
    • 67650736238 scopus 로고    scopus 로고
    • Horror autoinflammaticus: the molecular pathophysiology of autoinflammatory disease (*)
    • Masters S.L., et al. Horror autoinflammaticus: the molecular pathophysiology of autoinflammatory disease (*). Annu. Rev. Immunol. 2009, 27:621-668.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 621-668
    • Masters, S.L.1
  • 9
    • 84928704887 scopus 로고    scopus 로고
    • Hierarchical regulation of wound healing by NOD-like receptors in cardiovascular disease
    • Published online November 10, 2014
    • Bracey N.a., et al. Hierarchical regulation of wound healing by NOD-like receptors in cardiovascular disease. Antioxid. Redox Signal. 2014, Published online November 10, 2014.
    • (2014) Antioxid. Redox Signal.
    • Bracey, N.1
  • 10
    • 84901506090 scopus 로고    scopus 로고
    • Leukocyte infiltration and activation of the NLRP3 inflammasome in white adipose tissue following thermal injury
    • Stanojcic M., et al. Leukocyte infiltration and activation of the NLRP3 inflammasome in white adipose tissue following thermal injury. Crit. Care Med. 2014, 42:1357-1364.
    • (2014) Crit. Care Med. , vol.42 , pp. 1357-1364
    • Stanojcic, M.1
  • 11
    • 84892839044 scopus 로고    scopus 로고
    • Treating inflammation by blocking interleukin-1 in humans
    • Dinarello C.A., van der Meer J.W.M. Treating inflammation by blocking interleukin-1 in humans. Semin. Immunol. 2013, 25:469-484.
    • (2013) Semin. Immunol. , vol.25 , pp. 469-484
    • Dinarello, C.A.1    van der Meer, J.W.M.2
  • 12
    • 84895064425 scopus 로고    scopus 로고
    • Targeted next-generation sequencing: a novel diagnostic tool for primary immunodeficiencies
    • Nijman I.J., et al. Targeted next-generation sequencing: a novel diagnostic tool for primary immunodeficiencies. J. Allergy Clin. Immunol. 2014, 133:529-534.
    • (2014) J. Allergy Clin. Immunol. , vol.133 , pp. 529-534
    • Nijman, I.J.1
  • 13
    • 84866851735 scopus 로고    scopus 로고
    • Autoinflammation and autoimmunity: bridging the divide
    • Doria, A, et al. Autoinflammation and autoimmunity: bridging the divide. Autoimmun. Rev. 2012, 12:22-30.
    • (2012) Autoimmun. Rev. , vol.12 , pp. 22-30
    • Doria, A.1
  • 14
    • 84884332722 scopus 로고    scopus 로고
    • Mechanisms of NOD-like receptor-associated inflammasome activation
    • Wen H., et al. Mechanisms of NOD-like receptor-associated inflammasome activation. Immunity 2013, 39:432-441.
    • (2013) Immunity , vol.39 , pp. 432-441
    • Wen, H.1
  • 15
    • 84902970152 scopus 로고    scopus 로고
    • Mechanism of NLRP3 inflammasome activation
    • Sutterwala F.S., et al. Mechanism of NLRP3 inflammasome activation. Ann. N. Y. Acad. Sci. 2014, 1319:82-95.
    • (2014) Ann. N. Y. Acad. Sci. , vol.1319 , pp. 82-95
    • Sutterwala, F.S.1
  • 16
    • 84879596906 scopus 로고    scopus 로고
    • K+ Efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter
    • Muñoz-Planillo R., et al. K+ Efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity 2013, 38:1142-1153.
    • (2013) Immunity , vol.38 , pp. 1142-1153
    • Muñoz-Planillo, R.1
  • 17
    • 84928706286 scopus 로고    scopus 로고
    • Mitochondrial Ca(2+)-dependent NLRP3 activation exacerbates the Pseudomonas aeruginosa-driven inflammatory response in cystic fibrosis
    • Rimessi A., et al. Mitochondrial Ca(2+)-dependent NLRP3 activation exacerbates the Pseudomonas aeruginosa-driven inflammatory response in cystic fibrosis. Nat. Commun. 2015, 6:6201.
    • (2015) Nat. Commun. , vol.6 , pp. 6201
    • Rimessi, A.1
  • 18
    • 75649096002 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein links oxidative stress to inflammasome activation
    • Zhou R., et al. Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nat. Immunol. 2010, 11:136-140.
    • (2010) Nat. Immunol. , vol.11 , pp. 136-140
    • Zhou, R.1
  • 19
    • 84907584408 scopus 로고    scopus 로고
    • Reactive oxygen species regulate caspase-11 expression and activation of the non-canonical NLRP3 inflammasome during enteric pathogen infection
    • Lupfer C.R., et al. Reactive oxygen species regulate caspase-11 expression and activation of the non-canonical NLRP3 inflammasome during enteric pathogen infection. PLoS Pathog. 2014, 10:e1004410.
    • (2014) PLoS Pathog. , vol.10 , pp. e1004410
    • Lupfer, C.R.1
  • 20
    • 84904692363 scopus 로고    scopus 로고
    • The adaptor ASC has extracellular and "prionoid" activities that propagate inflammation
    • Franklin B.S., et al. The adaptor ASC has extracellular and "prionoid" activities that propagate inflammation. Nat. Immunol. 2014, 15:727-737.
    • (2014) Nat. Immunol. , vol.15 , pp. 727-737
    • Franklin, B.S.1
  • 21
    • 84921730204 scopus 로고    scopus 로고
    • Structural mechanisms of inflammasome assembly
    • Lu A., Wu H. Structural mechanisms of inflammasome assembly. FEBS J. 2014, 282:435-444.
    • (2014) FEBS J. , vol.282 , pp. 435-444
    • Lu, A.1    Wu, H.2
  • 22
    • 0034194079 scopus 로고    scopus 로고
    • The NACHT family - A new group of predicted NTPases implicated in apoptosis and MHC transcription activation
    • Koonin E.V., Aravind L. The NACHT family - A new group of predicted NTPases implicated in apoptosis and MHC transcription activation. Trends Biochem. Sci. 2000, 25:223-224.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 223-224
    • Koonin, E.V.1    Aravind, L.2
  • 23
    • 84884972334 scopus 로고    scopus 로고
    • Biochemical and structural aspects of the ATP-binding domain in inflammasome-forming human NLRP proteins
    • MacDonald J., a, et al. Biochemical and structural aspects of the ATP-binding domain in inflammasome-forming human NLRP proteins. IUBMB Life 2013, 65:851-862.
    • (2013) IUBMB Life , vol.65 , pp. 851-862
    • MacDonald, J.1
  • 24
    • 0242626505 scopus 로고    scopus 로고
    • Structural localization of disease-associated sequence variations in the NACHT and LRR domains of PYPAF1 and NOD2
    • Albrecht M., et al. Structural localization of disease-associated sequence variations in the NACHT and LRR domains of PYPAF1 and NOD2. FEBS Lett. 2003, 554:520-528.
    • (2003) FEBS Lett. , vol.554 , pp. 520-528
    • Albrecht, M.1
  • 25
    • 84891917420 scopus 로고    scopus 로고
    • 3,4-methylenedioxy-β-nitrostyrene inhibits NLRP3 inflammasome activation by blocking assembly of the inflammasome
    • He Y., et al. 3,4-methylenedioxy-β-nitrostyrene inhibits NLRP3 inflammasome activation by blocking assembly of the inflammasome. J. Biol. Chem. 2014, 289:1142-1150.
    • (2014) J. Biol. Chem. , vol.289 , pp. 1142-1150
    • He, Y.1
  • 26
    • 84867770402 scopus 로고    scopus 로고
    • Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation
    • Juliana C., et al. Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J. Biol. Chem. 2012, 287:36617-36622.
    • (2012) J. Biol. Chem. , vol.287 , pp. 36617-36622
    • Juliana, C.1
  • 27
    • 77956958947 scopus 로고    scopus 로고
    • Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes
    • Masters S.L., et al. Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes. Nat. Immunol. 2010, 11:897-904.
    • (2010) Nat. Immunol. , vol.11 , pp. 897-904
    • Masters, S.L.1
  • 28
    • 84924993872 scopus 로고    scopus 로고
    • Activation of NLRP3 and AIM2 inflammasomes in Kupffer cells in hepatic ischemia/reperfusion
    • Kim H-Y., et al. Activation of NLRP3 and AIM2 inflammasomes in Kupffer cells in hepatic ischemia/reperfusion. FEBS J. 2015, 282:259-270.
    • (2015) FEBS J. , vol.282 , pp. 259-270
    • Kim, H.-Y.1
  • 29
    • 84924034834 scopus 로고    scopus 로고
    • Redox Regulation of NLRP3 inflammasomes: ROS as trigger or effector?
    • Published online October 20, 2014
    • Abais J.M., et al. Redox Regulation of NLRP3 inflammasomes: ROS as trigger or effector?. Antioxid. Redox Signal. 2014, Published online October 20, 2014. 10.1089/ars.2014.5994.
    • (2014) Antioxid. Redox Signal.
    • Abais, J.M.1
  • 30
    • 84905254968 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein mediates NALP3 inflammasome activation in podocytes during diabetic nephropathy
    • Gao P., et al. Thioredoxin-interacting protein mediates NALP3 inflammasome activation in podocytes during diabetic nephropathy. Biochim. Biophys. Acta 2014, 1843:2448-2460.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 2448-2460
    • Gao, P.1
  • 31
    • 84903866180 scopus 로고    scopus 로고
    • TXNIP mediates NLRP3 inflammasome activation in cardiac microvascular endothelial cells as a novel mechanism in myocardial ischemia/reperfusion injury
    • Liu Y., et al. TXNIP mediates NLRP3 inflammasome activation in cardiac microvascular endothelial cells as a novel mechanism in myocardial ischemia/reperfusion injury. Basic Res. Cardiol. 2014, 109:415.
    • (2014) Basic Res. Cardiol. , vol.109 , pp. 415
    • Liu, Y.1
  • 32
    • 84893663061 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein is required for endothelial NLRP3 inflammasome activation and cell death in a rat model of high-fat diet
    • Mohamed I.N., et al. Thioredoxin-interacting protein is required for endothelial NLRP3 inflammasome activation and cell death in a rat model of high-fat diet. Diabetologia 2014, 57:413-423.
    • (2014) Diabetologia , vol.57 , pp. 413-423
    • Mohamed, I.N.1
  • 33
    • 7344255810 scopus 로고    scopus 로고
    • Non-founder mutations in the MEFV gene establish this gene as the cause of familial Mediterranean fever (FMF)
    • Bernot A., et al. Non-founder mutations in the MEFV gene establish this gene as the cause of familial Mediterranean fever (FMF). Hum. Mol. Genet. 1998, 7:1317-1325.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1317-1325
    • Bernot, A.1
  • 34
    • 16944365196 scopus 로고    scopus 로고
    • A candidate gene for familial Mediterranean fever
    • A candidate gene for familial Mediterranean fever. Nat. Genet. 1997, 17:25-31. French FMF Consortium.
    • (1997) Nat. Genet. , vol.17 , pp. 25-31
  • 35
    • 84907270863 scopus 로고    scopus 로고
    • Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome
    • Xu H., et al. Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome. Nature 2014, 513:237-241.
    • (2014) Nature , vol.513 , pp. 237-241
    • Xu, H.1
  • 36
    • 0032987982 scopus 로고    scopus 로고
    • Mutations in MVK, encoding mevalonate kinase, cause hyperimmunoglobulinaemia D and periodic fever syndrome
    • Houten S.M., et al. Mutations in MVK, encoding mevalonate kinase, cause hyperimmunoglobulinaemia D and periodic fever syndrome. Nat. Genet. 1999, 22:175-177.
    • (1999) Nat. Genet. , vol.22 , pp. 175-177
    • Houten, S.M.1
  • 37
    • 33750965780 scopus 로고    scopus 로고
    • A role for geranylgeranylation in interleukin-1beta secretion
    • Mandey S.H.L., et al. A role for geranylgeranylation in interleukin-1beta secretion. Arthritis Rheum. 2006, 54:3690-3695.
    • (2006) Arthritis Rheum. , vol.54 , pp. 3690-3695
    • Mandey, S.H.L.1
  • 38
    • 40349108709 scopus 로고    scopus 로고
    • Statin synergizes with LPS to induce IL-1beta release by THP-1 cells through activation of caspase-1
    • Kuijk L.M., et al. Statin synergizes with LPS to induce IL-1beta release by THP-1 cells through activation of caspase-1. Mol. Immunol. 2008, 45:2158-2165.
    • (2008) Mol. Immunol. , vol.45 , pp. 2158-2165
    • Kuijk, L.M.1
  • 39
    • 77957560947 scopus 로고    scopus 로고
    • Compromized geranylgeranylation of RhoA and Rac1 in mevalonate kinase deficiency
    • Henneman L., et al. Compromized geranylgeranylation of RhoA and Rac1 in mevalonate kinase deficiency. J. Inherit. Metab. Dis. 2010, 33:625-632.
    • (2010) J. Inherit. Metab. Dis. , vol.33 , pp. 625-632
    • Henneman, L.1
  • 40
    • 84907487955 scopus 로고    scopus 로고
    • Unprenylated RhoA contributes to IL-1β hypersecretion in mevalonate kinase deficiency model through stimulation of Rac1 activity
    • Van der Burgh R., et al. Unprenylated RhoA contributes to IL-1β hypersecretion in mevalonate kinase deficiency model through stimulation of Rac1 activity. J. Biol. Chem. 2014, 289:27757-27765.
    • (2014) J. Biol. Chem. , vol.289 , pp. 27757-27765
    • Van der Burgh, R.1
  • 41
    • 0033515520 scopus 로고    scopus 로고
    • Germline mutations in the extracellular domains of the 55kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes
    • McDermott M.F., et al. Germline mutations in the extracellular domains of the 55kDa TNF receptor, TNFR1, define a family of dominantly inherited autoinflammatory syndromes. Cell 1999, 97:133-144.
    • (1999) Cell , vol.97 , pp. 133-144
    • McDermott, M.F.1
  • 42
    • 84877625422 scopus 로고    scopus 로고
    • Autophagy contributes to inflammation in patients with TNFR-associated periodic syndrome (TRAPS)
    • Bachetti T., et al. Autophagy contributes to inflammation in patients with TNFR-associated periodic syndrome (TRAPS). Ann. Rheum. Dis. 2013, 72:1044-1052.
    • (2013) Ann. Rheum. Dis. , vol.72 , pp. 1044-1052
    • Bachetti, T.1
  • 43
    • 79952184583 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species promote production of proinflammatory cytokines and are elevated in TNFR1-associated periodic syndrome (TRAPS)
    • Bulua A.C., et al. Mitochondrial reactive oxygen species promote production of proinflammatory cytokines and are elevated in TNFR1-associated periodic syndrome (TRAPS). J. Exp. Med. 2011, 208:519-533.
    • (2011) J. Exp. Med. , vol.208 , pp. 519-533
    • Bulua, A.C.1
  • 44
    • 0035179970 scopus 로고    scopus 로고
    • Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome
    • Hoffman H.M., et al. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat. Genet. 2001, 29:301-305.
    • (2001) Nat. Genet. , vol.29 , pp. 301-305
    • Hoffman, H.M.1
  • 45
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein J.C., et al. The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol. 2000, 2:156-162.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 156-162
    • Goldstein, J.C.1
  • 46
    • 47849097202 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
    • Hornung V., et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat. Immunol. 2008, 9:847-856.
    • (2008) Nat. Immunol. , vol.9 , pp. 847-856
    • Hornung, V.1
  • 47
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • Zhou R., et al. A role for mitochondria in NLRP3 inflammasome activation. Nature 2011, 469:221-225.
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1
  • 48
    • 84917705991 scopus 로고    scopus 로고
    • Protoporphyrin IX induces a necrotic cell death in human THP-1 macrophages through activation of reactive oxygen species/c-Jun N-terminal protein kinase pathway and opening of mitochondrial permeability transition pore
    • Xu H., et al. Protoporphyrin IX induces a necrotic cell death in human THP-1 macrophages through activation of reactive oxygen species/c-Jun N-terminal protein kinase pathway and opening of mitochondrial permeability transition pore. Cell. Physiol. Biochem. 2014, 34:1835-1848.
    • (2014) Cell. Physiol. Biochem. , vol.34 , pp. 1835-1848
    • Xu, H.1
  • 49
    • 84894481149 scopus 로고    scopus 로고
    • Defects in mitochondrial clearance predispose human monocytes to interleukin-1β hypersecretion
    • Van der Burgh R., et al. Defects in mitochondrial clearance predispose human monocytes to interleukin-1β hypersecretion. J. Biol. Chem. 2014, 289:5000-5012.
    • (2014) J. Biol. Chem. , vol.289 , pp. 5000-5012
    • Van der Burgh, R.1
  • 50
    • 84862884156 scopus 로고    scopus 로고
    • Mitochondrial quality control: an integrated network of pathways
    • Fischer F., et al. Mitochondrial quality control: an integrated network of pathways. Trends Biochem. Sci. 2012, 37:284-292.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 284-292
    • Fischer, F.1
  • 51
    • 79951642032 scopus 로고    scopus 로고
    • Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
    • Nakahira K., et al. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat. Immunol. 2011, 12:222-230.
    • (2011) Nat. Immunol. , vol.12 , pp. 222-230
    • Nakahira, K.1
  • 52
    • 84908544666 scopus 로고    scopus 로고
    • Inflammasome activation leads to caspase-1-dependent mitochondrial damage and block of mitophagy
    • Yu J., et al. Inflammasome activation leads to caspase-1-dependent mitochondrial damage and block of mitophagy. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:15514-15519.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 15514-15519
    • Yu, J.1
  • 53
    • 77955041880 scopus 로고    scopus 로고
    • Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca2+ transfer to mitochondria
    • Cárdenas C., et al. Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca2+ transfer to mitochondria. Cell 2010, 142:270-283.
    • (2010) Cell , vol.142 , pp. 270-283
    • Cárdenas, C.1
  • 54
    • 0033598828 scopus 로고    scopus 로고
    • Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
    • Jouaville L.S., et al. Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:13807-13812.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13807-13812
    • Jouaville, L.S.1
  • 55
    • 0025292743 scopus 로고
    • Mechanisms by which mitochondria transport calcium
    • Gunter T.E., Pfeiffer D.R. Mechanisms by which mitochondria transport calcium. Am. J. Physiol. 1990, 258:C755-C786.
    • (1990) Am. J. Physiol. , vol.258 , pp. C755-C786
    • Gunter, T.E.1    Pfeiffer, D.R.2
  • 56
    • 0027058138 scopus 로고
    • Range of messenger action of calcium ion and inositol 1,4,5-trisphosphate
    • Allbritton N.L., et al. Range of messenger action of calcium ion and inositol 1,4,5-trisphosphate. Science 1992, 258:1812-1815.
    • (1992) Science , vol.258 , pp. 1812-1815
    • Allbritton, N.L.1
  • 57
    • 21844450590 scopus 로고    scopus 로고
    • Basal activation of the P2X7 ATP receptor elevates mitochondrial calcium and potential, increases cellular ATP levels, and promotes serum-independent growth
    • Adinolfi E., et al. Basal activation of the P2X7 ATP receptor elevates mitochondrial calcium and potential, increases cellular ATP levels, and promotes serum-independent growth. Mol. Biol. Cell 2005, 16:3260-3272.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3260-3272
    • Adinolfi, E.1
  • 58
    • 77953725586 scopus 로고    scopus 로고
    • Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM)
    • Simmen T., et al. Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM). Biochim. Biophys. Acta 2010, 1798:1465-1473.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1465-1473
    • Simmen, T.1
  • 59
    • 84875908991 scopus 로고    scopus 로고
    • TRPM2 links oxidative stress to NLRP3 inflammasome activation
    • Zhong Z., et al. TRPM2 links oxidative stress to NLRP3 inflammasome activation. Nat. Commun. 2013, 4:1611.
    • (2013) Nat. Commun. , vol.4 , pp. 1611
    • Zhong, Z.1
  • 60
    • 77950275298 scopus 로고    scopus 로고
    • Circulating mitochondrial DAMPs cause inflammatory responses to injury
    • Zhang Q., et al. Circulating mitochondrial DAMPs cause inflammatory responses to injury. Nature 2010, 464:104-107.
    • (2010) Nature , vol.464 , pp. 104-107
    • Zhang, Q.1
  • 61
    • 84862777872 scopus 로고    scopus 로고
    • Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
    • Shimada K., et al. Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity 2012, 36:401-414.
    • (2012) Immunity , vol.36 , pp. 401-414
    • Shimada, K.1
  • 62
    • 84904967279 scopus 로고    scopus 로고
    • New functions of mitochondria associated membranes in cellular signaling
    • Van Vliet A.R., et al. New functions of mitochondria associated membranes in cellular signaling. Biochim. Biophys. Acta 2014, 1843:2253-2262.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 2253-2262
    • Van Vliet, A.R.1
  • 63
    • 80052281413 scopus 로고    scopus 로고
    • Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus
    • Horner S.M., et al. Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:14590-14595.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14590-14595
    • Horner, S.M.1
  • 64
    • 84859232387 scopus 로고    scopus 로고
    • Fluxes at the endoplasmic reticulum-mitochondria interface (MAM)
    • Anelli T., et al. Fluxes at the endoplasmic reticulum-mitochondria interface (MAM). Antioxid. Redox Signal. 2012, 16:1077-1087.
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 1077-1087
    • Anelli, T.1
  • 65
    • 11844269232 scopus 로고    scopus 로고
    • Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44
    • Higo T., et al. Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell 2005, 120:85-98.
    • (2005) Cell , vol.120 , pp. 85-98
    • Higo, T.1
  • 66
    • 84892646801 scopus 로고    scopus 로고
    • Unfolded protein response signaling and metabolic diseases
    • Lee J., Ozcan U. Unfolded protein response signaling and metabolic diseases. J. Biol. Chem. 2014, 289:1203-1211.
    • (2014) J. Biol. Chem. , vol.289 , pp. 1203-1211
    • Lee, J.1    Ozcan, U.2
  • 67
    • 84908082447 scopus 로고    scopus 로고
    • Stress-responsive regulation of mitochondria through the ER unfolded protein response
    • Rainbolt T.K., et al. Stress-responsive regulation of mitochondria through the ER unfolded protein response. Trends Endocrinol. Metab. 2014, 25:528-537.
    • (2014) Trends Endocrinol. Metab. , vol.25 , pp. 528-537
    • Rainbolt, T.K.1
  • 68
    • 33746998472 scopus 로고    scopus 로고
    • Mutational spectrum and genotype-phenotype correlations in mevalonate kinase deficiency
    • Mandey S.H.L., et al. Mutational spectrum and genotype-phenotype correlations in mevalonate kinase deficiency. Hum. Mutat. 2006, 27:796-802.
    • (2006) Hum. Mutat. , vol.27 , pp. 796-802
    • Mandey, S.H.L.1
  • 69
    • 84908222221 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is sufficient for the induction of IL-1β production via activation of the NF-κB and inflammasome pathways
    • Kim S., et al. Endoplasmic reticulum stress is sufficient for the induction of IL-1β production via activation of the NF-κB and inflammasome pathways. Innate Immun. 2014, 20:799-815.
    • (2014) Innate Immun. , vol.20 , pp. 799-815
    • Kim, S.1
  • 70
    • 84908105412 scopus 로고    scopus 로고
    • The mitochondrial complex I inhibitor rotenone induces endoplasmic reticulum stress and activation of GSK3 in cultured rat retinal cells
    • Han G., et al. The mitochondrial complex I inhibitor rotenone induces endoplasmic reticulum stress and activation of GSK3 in cultured rat retinal cells. Invest. Ophthalmol. Vis. Sci. 2014, 55:5616-5628.
    • (2014) Invest. Ophthalmol. Vis. Sci. , vol.55 , pp. 5616-5628
    • Han, G.1
  • 71
    • 84896500701 scopus 로고    scopus 로고
    • Cutting edge: Endoplasmic reticulum stress licenses macrophages to produce mature IL-1β in response to TLR4 stimulation through a caspase-8- and TRIF-dependent pathway
    • Shenderov K., et al. Cutting edge: Endoplasmic reticulum stress licenses macrophages to produce mature IL-1β in response to TLR4 stimulation through a caspase-8- and TRIF-dependent pathway. J. Immunol. 2014, 192:2029-2033.
    • (2014) J. Immunol. , vol.192 , pp. 2029-2033
    • Shenderov, K.1
  • 72
    • 2342418629 scopus 로고    scopus 로고
    • Rho-family GTPases: it's not only Rac and Rho (and I like it)
    • Wennerberg K., Der C.J. Rho-family GTPases: it's not only Rac and Rho (and I like it). J. Cell Sci. 2004, 117:1301-1312.
    • (2004) J. Cell Sci. , vol.117 , pp. 1301-1312
    • Wennerberg, K.1    Der, C.J.2
  • 73
    • 77957790021 scopus 로고    scopus 로고
    • Rab32 modulates apoptosis onset and mitochondria-associated membrane (MAM) properties
    • Bui M., et al. Rab32 modulates apoptosis onset and mitochondria-associated membrane (MAM) properties. J. Biol. Chem. 2010, 285:31590-31602.
    • (2010) J. Biol. Chem. , vol.285 , pp. 31590-31602
    • Bui, M.1
  • 74
    • 0033039501 scopus 로고    scopus 로고
    • Mutations in the gene encoding mevalonate kinase cause hyper-IgD and periodic fever syndrome. International Hyper-IgD Study Group
    • Drenth J.P., et al. Mutations in the gene encoding mevalonate kinase cause hyper-IgD and periodic fever syndrome. International Hyper-IgD Study Group. Nat. Genet. 1999, 22:178-181.
    • (1999) Nat. Genet. , vol.22 , pp. 178-181
    • Drenth, J.P.1
  • 75
    • 12144288979 scopus 로고    scopus 로고
    • Molecular basis of the spectral expression of CIAS1 mutations associated with phagocytic cell-mediated autoinflammatory disorders CINCA/NOMID, MWS, and FCU
    • Neven B., et al. Molecular basis of the spectral expression of CIAS1 mutations associated with phagocytic cell-mediated autoinflammatory disorders CINCA/NOMID, MWS, and FCU. Blood 2004, 103:2809-2815.
    • (2004) Blood , vol.103 , pp. 2809-2815
    • Neven, B.1
  • 76
    • 84892660511 scopus 로고    scopus 로고
    • Regulation of mitochondrial antiviral signaling (MAVS) expression and signaling by the mitochondria-associated endoplasmic reticulum membrane (MAM) protein Gp78
    • Jacobs J.L., et al. Regulation of mitochondrial antiviral signaling (MAVS) expression and signaling by the mitochondria-associated endoplasmic reticulum membrane (MAM) protein Gp78. J. Biol. Chem. 2014, 289:1604-1616.
    • (2014) J. Biol. Chem. , vol.289 , pp. 1604-1616
    • Jacobs, J.L.1
  • 77
    • 84885437002 scopus 로고    scopus 로고
    • The mitochondrial antiviral protein MAVS associates with NLRP3 and regulates its inflammasome activity
    • Park S., et al. The mitochondrial antiviral protein MAVS associates with NLRP3 and regulates its inflammasome activity. J. Immunol. 2013, 191:4358-4366.
    • (2013) J. Immunol. , vol.191 , pp. 4358-4366
    • Park, S.1
  • 78
    • 74049126045 scopus 로고    scopus 로고
    • Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1 beta production
    • Poeck H., et al. Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1 beta production. Nat. Immunol. 2010, 11:63-69.
    • (2010) Nat. Immunol. , vol.11 , pp. 63-69
    • Poeck, H.1
  • 79
    • 84907494143 scopus 로고    scopus 로고
    • Cytosolic double-stranded RNA activates the NLRP3 inflammasome via MAVS-induced membrane permeabilization and K+ efflux
    • Franchi L., et al. Cytosolic double-stranded RNA activates the NLRP3 inflammasome via MAVS-induced membrane permeabilization and K+ efflux. J. Immunol. 2014, 193:4214-4222.
    • (2014) J. Immunol. , vol.193 , pp. 4214-4222
    • Franchi, L.1
  • 80
    • 79955777383 scopus 로고    scopus 로고
    • A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection
    • Kim B-H., et al. A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection. Science 2011, 332:717-721.
    • (2011) Science , vol.332 , pp. 717-721
    • Kim, B.-H.1
  • 81
    • 84860225554 scopus 로고    scopus 로고
    • GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals
    • Shenoy A.R., et al. GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals. Science 2012, 336:481-485.
    • (2012) Science , vol.336 , pp. 481-485
    • Shenoy, A.R.1
  • 82
    • 34249941913 scopus 로고    scopus 로고
    • Cryopyrin/NALP3 binds ATP/dATP, is an ATPase, and requires ATP binding to mediate inflammatory signaling
    • Duncan J.A., et al. Cryopyrin/NALP3 binds ATP/dATP, is an ATPase, and requires ATP binding to mediate inflammatory signaling. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:8041-8046.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 8041-8046
    • Duncan, J.A.1
  • 83
    • 33750445482 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in mammals
    • Chan D.C. Mitochondrial fusion and fission in mammals. Annu. Rev. Cell Dev. Biol. 2006, 22:79-99.
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 79-99
    • Chan, D.C.1
  • 84
    • 77955287381 scopus 로고    scopus 로고
    • Physiological functions of mitochondrial fusion
    • Chen H., Chan D.C. Physiological functions of mitochondrial fusion. Ann. N. Y. Acad. Sci. 2010, 1201:21-25.
    • (2010) Ann. N. Y. Acad. Sci. , vol.1201 , pp. 21-25
    • Chen, H.1    Chan, D.C.2
  • 85
    • 84865547276 scopus 로고    scopus 로고
    • Cell biology. Mitochondrial dynamics and apoptosis - the ER connection
    • Hoppins S., Nunnari J. Cell biology. Mitochondrial dynamics and apoptosis - the ER connection. Science 2012, 337:1052-1054.
    • (2012) Science , vol.337 , pp. 1052-1054
    • Hoppins, S.1    Nunnari, J.2
  • 86
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D., et al. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 2008, 183:795-803.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1
  • 87
    • 79954417075 scopus 로고    scopus 로고
    • Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress
    • Bouman L., et al. Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress. Cell Death Differ. 2011, 18:769-782.
    • (2011) Cell Death Differ. , vol.18 , pp. 769-782
    • Bouman, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.