메뉴 건너뛰기




Volumn 289, Issue 48, 2014, Pages 33391-33403

3 Asbestos-induced disruption of calcium homeostasis induces endoplasmic reticulum stress in macrophages

Author keywords

[No Author keywords available]

Indexed keywords

ASBESTOS; CALCIUM; CELL MEMBRANES; GENE EXPRESSION; MAMMALS; PROTEINS; SERPENTINE;

EID: 84912558059     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.579870     Document Type: Article
Times cited : (36)

References (50)
  • 2
    • 84867006695 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress and the unfolded protein response in fibrosis
    • Lenna, S., and Trojanowska, M. (2012) The role of endoplasmic reticulum stress and the unfolded protein response in fibrosis. Curr. Opin. Rheumatol. 24, 663-668
    • (2012) Curr. Opin. Rheumatol. , vol.24 , pp. 663-668
    • Lenna, S.1    Trojanowska, M.2
  • 3
    • 84859740294 scopus 로고    scopus 로고
    • Emerging evidence for endoplasmic reticulum stress in the pathogenesis of idiopathic pulmonary fibrosis
    • Tanjore, H., Blackwell, T. S., and Lawson, W. E. (2012) Emerging evidence for endoplasmic reticulum stress in the pathogenesis of idiopathic pulmonary fibrosis. Am. J. Physiol. Lung Cell. Mol. Physiol. 302, L721-729
    • (2012) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.302 , pp. L721-L729
    • Tanjore, H.1    Blackwell, T.S.2    Lawson, W.E.3
  • 4
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • Hetz, C. (2012) The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13, 89-102
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 5
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: Disease relevance and therapeutic opportunities
    • Kim, I., Xu, W., and Reed, J. C. (2008) Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities. Nat. Rev. Drug Discov. 7, 1013-1030
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 6
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • Xu, C., Bailly-Maitre, B., and Reed, J. C. (2005) Endoplasmic reticulum stress: cell life and death decisions. J. Clin. Investig. 115, 2656-2664
    • (2005) J. Clin. Investig. , vol.115 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 10
    • 77954589474 scopus 로고    scopus 로고
    • Surfactant protein A2 mutations associated with pulmonary fibrosis lead to protein instability and endoplasmic reticulum stress
    • Maitra, M., Wang, Y., Gerard, R. D., Mendelson, C. R., and Garcia, C. K. (2010) Surfactant protein A2 mutations associated with pulmonary fibrosis lead to protein instability and endoplasmic reticulum stress. J. Biol. Chem. 285, 22103-22113
    • (2010) J. Biol. Chem. , vol.285 , pp. 22103-22113
    • Maitra, M.1    Wang, Y.2    Gerard, R.D.3    Mendelson, C.R.4    Garcia, C.K.5
  • 13
    • 84880062414 scopus 로고    scopus 로고
    • Accelerated development of pulmonary fibrosis via Cu,Zn-superoxide dismutase-induced alternative activation of macrophages
    • He, C., Ryan, A. J., Murthy, S., and Carter, A. B. (2013) Accelerated development of pulmonary fibrosis via Cu,Zn-superoxide dismutase-induced alternative activation of macrophages. J. Biol. Chem. 288, 20745-20757
    • (2013) J. Biol. Chem. , vol.288 , pp. 20745-20757
    • He, C.1    Ryan, A.J.2    Murthy, S.3    Carter, A.B.4
  • 15
    • 84856279893 scopus 로고    scopus 로고
    • Mitochondrial Rac1 GTPase import and electron transfer from cytochrome c are required for pulmonary fibrosis
    • Osborn-Heaford, H. L., Ryan, A. J., Murthy, S., Racila, A. M., He, C., Sieren, J. C., Spitz, D. R., and Carter, A. B. (2012) Mitochondrial Rac1 GTPase import and electron transfer from cytochrome c are required for pulmonary fibrosis. J. Biol. Chem. 287, 3301-3312
    • (2012) J. Biol. Chem. , vol.287 , pp. 3301-3312
    • Osborn-Heaford, H.L.1    Ryan, A.J.2    Murthy, S.3    Racila, A.M.4    He, C.5    Sieren, J.C.6    Spitz, D.R.7    Carter, A.B.8
  • 18
    • 77649192183 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium release potentiates the ER stress and cell death caused by an oxidative stress in MCF-7 cells
    • Dejeans, N., Tajeddine, N., Beck, R., Verrax, J., Taper, H., Gailly, P., and Calderon, P. B. (2010) Endoplasmic reticulum calcium release potentiates the ER stress and cell death caused by an oxidative stress in MCF-7 cells. Biochem. Pharmacol. 79, 1221-1230
    • (2010) Biochem. Pharmacol. , vol.79 , pp. 1221-1230
    • Dejeans, N.1    Tajeddine, N.2    Beck, R.3    Verrax, J.4    Taper, H.5    Gailly, P.6    Calderon, P.B.7
  • 21
    • 33845656359 scopus 로고    scopus 로고
    • Passive calcium leak via translocon is a first step for iPLA2-pathway regulated store operated channels activation
    • Flourakis, M., Van Coppenolle, F., Lehen'kyi, V., Beck, B., Skryma, R., and Prevarskaya, N. (2006) Passive calcium leak via translocon is a first step for iPLA2-pathway regulated store operated channels activation. FASEB J. 20, 1215-1217
    • (2006) FASEB J. , vol.20 , pp. 1215-1217
    • Flourakis, M.1    Van Coppenolle, F.2    Lehen'kyi, V.3    Beck, B.4    Skryma, R.5    Prevarskaya, N.6
  • 23
    • 77649271201 scopus 로고    scopus 로고
    • Bone marrow-derived macrophages (BMM): Isolation and applications
    • Weischenfeldt, J., and Porse, B. (2008) Bone marrow-derived macrophages (BMM): isolation and applications. CSH Protoc. 10.1101/pdb.prot5080
    • (2008) CSH Protoc.
    • Weischenfeldt, J.1    Porse, B.2
  • 24
    • 0032698069 scopus 로고    scopus 로고
    • The p38 mitogen-activated protein kinase is required for NF-κB-dependent gene expression: The role of TATA-binding protein (TBP)
    • Carter, A. B., Knudtson, K. L., Monick, M. M., and Hunninghake, G. W. (1999) The p38 mitogen-activated protein kinase is required for NF-κB-dependent gene expression: the role of TATA-binding protein (TBP). J. Biol. Chem. 274, 30858-30863
    • (1999) J. Biol. Chem. , vol.274 , pp. 30858-30863
    • Carter, A.B.1    Knudtson, K.L.2    Monick, M.M.3    Hunninghake, G.W.4
  • 25
    • 77955979773 scopus 로고    scopus 로고
    • Methods for monitoring endoplasmic reticulum stress and the unfolded protein response
    • Samali, A., Fitzgerald, U., Deegan, S., and Gupta, S. (2010) Methods for monitoring endoplasmic reticulum stress and the unfolded protein response. Int. J. Cell Biol. 2010, 830307
    • (2010) Int. J. Cell Biol. , vol.2010 , pp. 830307
    • Samali, A.1    Fitzgerald, U.2    Deegan, S.3    Gupta, S.4
  • 26
    • 44449101173 scopus 로고    scopus 로고
    • ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum
    • Adachi, Y., Yamamoto, K., Okada, T., Yoshida, H., Harada, A., and Mori, K. (2008) ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct. Funct. 33, 75-89
    • (2008) Cell Struct. Funct. , vol.33 , pp. 75-89
    • Adachi, Y.1    Yamamoto, K.2    Okada, T.3    Yoshida, H.4    Harada, A.5    Mori, K.6
  • 31
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-α-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li, G., Mongillo, M., Chin, K. T., Harding, H., Ron, D., Marks, A. R., and Tabas, I. (2009) Role of ERO1-α-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J. Cell Biol. 186, 783-792
    • (2009) J. Cell Biol. , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 32
    • 77956179509 scopus 로고    scopus 로고
    • Molecular mechanisms of asbestos-induced lung epithelial cell apoptosis
    • Liu, G., Beri, R., Mueller, A., and Kamp, D. W. (2010) Molecular mechanisms of asbestos-induced lung epithelial cell apoptosis. Chem-Biol. Interact. 188, 309-318
    • (2010) Chem-Biol. Interact. , vol.188 , pp. 309-318
    • Liu, G.1    Beri, R.2    Mueller, A.3    Kamp, D.W.4
  • 33
    • 79960381007 scopus 로고    scopus 로고
    • Integrating mechanisms of pulmonary fibrosis
    • Wynn, T. A. (2011) Integrating mechanisms of pulmonary fibrosis. J. Exp. Med. 208, 1339-1350
    • (2011) J. Exp. Med. , vol.208 , pp. 1339-1350
    • Wynn, T.A.1
  • 35
    • 79952219426 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induced by surfactant protein C BRICHOS mutants promotes proinflammatory signaling by epithelial cells
    • Maguire, J. A., Mulugeta, S., and Beers, M. F. (2011) Endoplasmic reticulum stress induced by surfactant protein C BRICHOS mutants promotes proinflammatory signaling by epithelial cells. Am. J. Respir. Cell Mol. Biol. 44, 404-414
    • (2011) Am. J. Respir. Cell Mol. Biol. , vol.44 , pp. 404-414
    • Maguire, J.A.1    Mulugeta, S.2    Beers, M.F.3
  • 36
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman, B. D., Hendershot, L. M., and Johnson, A. E. (1998) BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92, 747-758
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 38
    • 35549006797 scopus 로고    scopus 로고
    • 2+ signaling and cell survival
    • 2+ signaling and cell survival. Cell 131, 596-610
    • (2007) Cell , vol.131 , pp. 596-610
    • Hayashi, T.1    Su, T.P.2
  • 39
    • 79251508006 scopus 로고    scopus 로고
    • Assays for detecting the unfolded protein response
    • Cawley, K., Deegan, S., Samali, A., and Gupta, S. (2011) Assays for detecting the unfolded protein response. Methods Enzymol. 490, 31-51
    • (2011) Methods Enzymol. , vol.490 , pp. 31-51
    • Cawley, K.1    Deegan, S.2    Samali, A.3    Gupta, S.4
  • 40
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D., and Walter, P. (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519-529
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 42
    • 2442542312 scopus 로고    scopus 로고
    • PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress
    • Cullinan, S. B., and Diehl, J. A. (2004) PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress. J. Biol. Chem. 279, 20108-20117
    • (2004) J. Biol. Chem. , vol.279 , pp. 20108-20117
    • Cullinan, S.B.1    Diehl, J.A.2
  • 46
    • 33748178875 scopus 로고    scopus 로고
    • Apoptotic cells promote macrophage survival by releasing the antiapoptotic mediator sphingosine-1-phosphate
    • Weigert, A., Johann, A. M., von Knethen, A., Schmidt, H., Geisslinger, G., and Brüne, B. (2006) Apoptotic cells promote macrophage survival by releasing the antiapoptotic mediator sphingosine-1-phosphate. Blood 108, 1635-1642
    • (2006) Blood , vol.108 , pp. 1635-1642
    • Weigert, A.1    Johann, A.M.2    Von Knethen, A.3    Schmidt, H.4    Geisslinger, G.5    Brüne, B.6
  • 47
    • 77954961992 scopus 로고    scopus 로고
    • Macrophages: Master regulators of inflammation and fibrosis
    • Wynn, T. A., and Barron, L. (2010) Macrophages: master regulators of inflammation and fibrosis. Semin. Liver Dis. 30, 245-257
    • (2010) Semin. Liver Dis. , vol.30 , pp. 245-257
    • Wynn, T.A.1    Barron, L.2
  • 49
    • 84859505076 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress controls M2 macrophage differentiation and foam cell formation
    • Oh, J., Riek, A. E., Weng, S., Petty, M., Kim, D., Colonna, M., Cella, M., and Bernal-Mizrachi, C. (2012) Endoplasmic reticulum stress controls M2 macrophage differentiation and foam cell formation. J. Biol. Chem. 287, 11629-11641
    • (2012) J. Biol. Chem. , vol.287 , pp. 11629-11641
    • Oh, J.1    Riek, A.E.2    Weng, S.3    Petty, M.4    Kim, D.5    Colonna, M.6    Cella, M.7    Bernal-Mizrachi, C.8
  • 50
    • 20444461628 scopus 로고    scopus 로고
    • Free cholesterol-loaded macrophages are an abundant source of tumor necrosis factor-α and interleukin-6: Model of NF-κB- and map kinase-dependent inflammation in advanced atherosclerosis
    • Li, Y., Schwabe, R. F., DeVries-Seimon, T., Yao, P. M., Gerbod-Giannone, M. C., Tall, A. R., Davis, R. J., Flavell, R., Brenner, D. A., and Tabas, I. (2005) Free cholesterol-loaded macrophages are an abundant source of tumor necrosis factor-α and interleukin-6: model of NF-κB- and map kinase-dependent inflammation in advanced atherosclerosis. J. Biol. Chem. 280, 21763-21772
    • (2005) J. Biol. Chem. , vol.280 , pp. 21763-21772
    • Li, Y.1    Schwabe, R.F.2    DeVries-Seimon, T.3    Yao, P.M.4    Gerbod-Giannone, M.C.5    Tall, A.R.6    Davis, R.J.7    Flavell, R.8    Brenner, D.A.9    Tabas, I.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.