메뉴 건너뛰기




Volumn 44, Issue 3, 2014, Pages 831-841

Calpains promote neutrophil recruitment and bacterial clearance in an acute bacterial peritonitis model

Author keywords

Bacterial infection; Calpains; Neutrophils; Phagocytosis; Reactive oxygen species

Indexed keywords

CALPAIN; CRE RECOMBINASE; INTERLEUKIN 1ALPHA; SELENOPROTEIN; SELENOPROTEIN K; UNCLASSIFIED DRUG;

EID: 84896040943     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201343757     Document Type: Article
Times cited : (20)

References (63)
  • 1
    • 84858295538 scopus 로고    scopus 로고
    • Innate host responses to enteric bacterial pathogens: a balancing act between resistance and tolerance
    • Bergstrom, K. S., Sham, H. P., Zarepour, M. and Vallance, B. A., Innate host responses to enteric bacterial pathogens: a balancing act between resistance and tolerance. Cell Microbiol. 2012. 14: 475-484.
    • (2012) Cell Microbiol. , vol.14 , pp. 475-484
    • Bergstrom, K.S.1    Sham, H.P.2    Zarepour, M.3    Vallance, B.A.4
  • 2
    • 79960926555 scopus 로고    scopus 로고
    • Mast cell proteases as protective and inflammatory mediators
    • Caughey, G. H., Mast cell proteases as protective and inflammatory mediators. Adv. Exp. Med. Biol. 2011. 716: 212-234.
    • (2011) Adv. Exp. Med. Biol. , vol.716 , pp. 212-234
    • Caughey, G.H.1
  • 3
    • 84874509753 scopus 로고    scopus 로고
    • Current trends in inflammatory and immunomodulatory mediators in sepsis
    • Aziz, M., Jacob, A., Yang, W. L., Matsuda, A. and Wang, P., Current trends in inflammatory and immunomodulatory mediators in sepsis. J. Leukoc. Biol. 2013. 93: 329-342.
    • (2013) J. Leukoc. Biol. , vol.93 , pp. 329-342
    • Aziz, M.1    Jacob, A.2    Yang, W.L.3    Matsuda, A.4    Wang, P.5
  • 4
    • 84861028443 scopus 로고    scopus 로고
    • Pathophysiological changes to the peritoneal membrane during PD-related peritonitis: the role of mesothelial cells
    • Yung, S. and Chan, T. M., Pathophysiological changes to the peritoneal membrane during PD-related peritonitis: the role of mesothelial cells. Mediators Inflamm. 2012. 2012: 484167.
    • (2012) Mediators Inflamm. , vol.2012 , pp. 484167
    • Yung, S.1    Chan, T.M.2
  • 6
    • 84856104734 scopus 로고    scopus 로고
    • Innate immunity in the vasculature: interactions with pathogenic bacteria
    • Harding, M. and Kubes, P., Innate immunity in the vasculature: interactions with pathogenic bacteria. Curr. Opin. Microbiol. 2012. 15: 85-91.
    • (2012) Curr. Opin. Microbiol. , vol.15 , pp. 85-91
    • Harding, M.1    Kubes, P.2
  • 7
    • 84856367507 scopus 로고    scopus 로고
    • Immunology in clinic review series; focus on autoinflammatory diseases: update on monogenic autoinflammatory diseases: the role of interleukin (IL)-1 and an emerging role for cytokines beyond IL-1
    • Goldbach-Mansky, R., Immunology in clinic review series; focus on autoinflammatory diseases: update on monogenic autoinflammatory diseases: the role of interleukin (IL)-1 and an emerging role for cytokines beyond IL-1. Clin. Exp. Immunol. 2012. 167: 391-404.
    • (2012) Clin. Exp. Immunol. , vol.167 , pp. 391-404
    • Goldbach-Mansky, R.1
  • 10
    • 84867270850 scopus 로고    scopus 로고
    • Structure-function relationships in calpains(1)
    • Campbell, R. L. and Davies, P. L., Structure-function relationships in calpains(1). Biochem. J. 2012. 447: 335-351.
    • (2012) Biochem. J. , vol.447 , pp. 335-351
    • Campbell, R.L.1    Davies, P.L.2
  • 11
    • 56749172400 scopus 로고    scopus 로고
    • Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin
    • Hanna, R. A., Campbell, R. L. and Davies, P. L., Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin. Nature 2008. 456: 409-412.
    • (2008) Nature , vol.456 , pp. 409-412
    • Hanna, R.A.1    Campbell, R.L.2    Davies, P.L.3
  • 12
    • 56749143763 scopus 로고    scopus 로고
    • Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains
    • Moldoveanu, T., Gehring, K. and Green, D. R., Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Nature 2008. 456: 404-408.
    • (2008) Nature , vol.456 , pp. 404-408
    • Moldoveanu, T.1    Gehring, K.2    Green, D.R.3
  • 13
    • 80053434264 scopus 로고    scopus 로고
    • Selenoprotein K is a novel target of m-calpain, and cleavage is regulated by Toll-like receptor-induced calpastatin in macrophages
    • Huang, Z., Hoffmann, F. W., Norton, R. L., Hashimoto, A. C. and Hoffmann, P. R., Selenoprotein K is a novel target of m-calpain, and cleavage is regulated by Toll-like receptor-induced calpastatin in macrophages. J. Biol. Chem. 2011. 286: 34830-34838.
    • (2011) J. Biol. Chem. , vol.286 , pp. 34830-34838
    • Huang, Z.1    Hoffmann, F.W.2    Norton, R.L.3    Hashimoto, A.C.4    Hoffmann, P.R.5
  • 15
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin, N., Bhatt, A. K., Dutt, P., Greer, P. A., Arthur, J. S., Elce, J. S. and Huttenlocher, A., Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J. Biol. Chem. 2001. 276: 48382-48388.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48382-48388
    • Dourdin, N.1    Bhatt, A.K.2    Dutt, P.3    Greer, P.A.4    Arthur, J.S.5    Elce, J.S.6    Huttenlocher, A.7
  • 18
    • 72949116148 scopus 로고    scopus 로고
    • Calpain inhibition impairs TNF-alpha-mediated neutrophil adhesion, arrest and oxidative burst
    • Wiemer, A. J., Lokuta, M. A., Surfus, J. C., Wernimont, S. A. and Huttenlocher, A., Calpain inhibition impairs TNF-alpha-mediated neutrophil adhesion, arrest and oxidative burst. Mol. Immunol. 2010. 47: 894-902.
    • (2010) Mol. Immunol. , vol.47 , pp. 894-902
    • Wiemer, A.J.1    Lokuta, M.A.2    Surfus, J.C.3    Wernimont, S.A.4    Huttenlocher, A.5
  • 19
    • 79951831744 scopus 로고    scopus 로고
    • Selenoprotein K knockout mice exhibit deficient calcium flux in immune cells and impaired immune responses
    • Verma, S., Hoffmann, F. W., Kumar, M., Huang, Z., Roe, K., Nguyen-Wu, E., Hashimoto, A. S. and Hoffmann, P. R., Selenoprotein K knockout mice exhibit deficient calcium flux in immune cells and impaired immune responses. J. Immunol. 2011. 186: 2127-2137.
    • (2011) J. Immunol. , vol.186 , pp. 2127-2137
    • Verma, S.1    Hoffmann, F.W.2    Kumar, M.3    Huang, Z.4    Roe, K.5    Nguyen-Wu, E.6    Hashimoto, A.S.7    Hoffmann, P.R.8
  • 21
    • 79955977311 scopus 로고    scopus 로고
    • Group B Streptococcus (GBS) disrupts by calpain activation the actin and microtubule cytoskeleton of macrophages
    • Fettucciari, K., Quotadamo, F., Noce, R., Palumbo, C., Modesti, A., Rosati, E., Mannucci, R. et al., Group B Streptococcus (GBS) disrupts by calpain activation the actin and microtubule cytoskeleton of macrophages. Cell Microbiol. 2011. 13: 859-884.
    • (2011) Cell Microbiol. , vol.13 , pp. 859-884
    • Fettucciari, K.1    Quotadamo, F.2    Noce, R.3    Palumbo, C.4    Modesti, A.5    Rosati, E.6    Mannucci, R.7
  • 22
    • 84876284629 scopus 로고    scopus 로고
    • Regulation of interleukin 1alpha secretion by inflammasomes
    • Yazdi, A. S. and Drexler, S. K., Regulation of interleukin 1alpha secretion by inflammasomes. Ann. Rheum. Dis. 2013. 72(Suppl 2): ii96-ii99.
    • (2013) Ann. Rheum. Dis. , vol.72 , Issue.SUPPL. 2
    • Yazdi, A.S.1    Drexler, S.K.2
  • 23
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes
    • Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K. et al., A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 1992. 356: 768-774.
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1    Bull, H.G.2    Calaycay, J.R.3    Chapman, K.T.4    Howard, A.D.5    Kostura, M.J.6    Miller, D.K.7
  • 24
    • 0025871386 scopus 로고
    • Involvement of a calpain-like protease in the processing of the murine interleukin 1 alpha precursor
    • Carruth, L. M., Demczuk, S. and Mizel, S. B., Involvement of a calpain-like protease in the processing of the murine interleukin 1 alpha precursor. J. Biol. Chem. 1991. 266: 12162-12167.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12162-12167
    • Carruth, L.M.1    Demczuk, S.2    Mizel, S.B.3
  • 25
    • 84858761335 scopus 로고    scopus 로고
    • Inflammasome activators induce interleukin-1alpha secretion via distinct pathways with differential requirement for the protease function of caspase-1
    • Gross, O., Yazdi, A. S., Thomas, C. J., Masin, M., Heinz, L. X., Guarda, G., Quadroni, M. et al., Inflammasome activators induce interleukin-1alpha secretion via distinct pathways with differential requirement for the protease function of caspase-1. Immunity 2012. 36: 388-400.
    • (2012) Immunity , vol.36 , pp. 388-400
    • Gross, O.1    Yazdi, A.S.2    Thomas, C.J.3    Masin, M.4    Heinz, L.X.5    Guarda, G.6    Quadroni, M.7
  • 27
    • 58249092789 scopus 로고    scopus 로고
    • TLR2-induced calpain cleavage of epithelial junctional proteins facilitates leukocyte transmigration
    • Chun, J. and Prince, A., TLR2-induced calpain cleavage of epithelial junctional proteins facilitates leukocyte transmigration. Cell Host Microbe 2009. 5: 47-58.
    • (2009) Cell Host Microbe , vol.5 , pp. 47-58
    • Chun, J.1    Prince, A.2
  • 28
    • 84858411647 scopus 로고    scopus 로고
    • Calpain activation by the Shigella flexneri effector VirA regulates key steps in the formation and life of the bacterium's epithelial niche
    • Bergounioux, J., Elisee, R., Prunier, A. L., Donnadieu, F., Sperandio, B., Sansonetti, P. and Arbibe, L., Calpain activation by the Shigella flexneri effector VirA regulates key steps in the formation and life of the bacterium's epithelial niche. Cell Host Microbe 2012. 11: 240-252.
    • (2012) Cell Host Microbe , vol.11 , pp. 240-252
    • Bergounioux, J.1    Elisee, R.2    Prunier, A.L.3    Donnadieu, F.4    Sperandio, B.5    Sansonetti, P.6    Arbibe, L.7
  • 29
    • 67349170024 scopus 로고    scopus 로고
    • Calpain-1 induces apoptosis in pulmonary microvascular endothelial cells under septic conditions
    • Hu, H., Li, X., Li, Y., Wang, L., Mehta, S., Feng, Q., Chen, R. and Peng, T., Calpain-1 induces apoptosis in pulmonary microvascular endothelial cells under septic conditions. Microvasc. Res. 2009. 78: 33-39.
    • (2009) Microvasc. Res. , vol.78 , pp. 33-39
    • Hu, H.1    Li, X.2    Li, Y.3    Wang, L.4    Mehta, S.5    Feng, Q.6    Chen, R.7    Peng, T.8
  • 32
    • 84856401404 scopus 로고    scopus 로고
    • Protein metabolism and gene expression in skeletal muscle of critically ill patients with sepsis
    • Klaude, M., Mori, M., Tjader, I., Gustafsson, T., Wernerman, J. and Rooyackers, O., Protein metabolism and gene expression in skeletal muscle of critically ill patients with sepsis. Clin. Sci. (Lond) 2012. 122: 133-142.
    • (2012) Clin. Sci. (Lond) , vol.122 , pp. 133-142
    • Klaude, M.1    Mori, M.2    Tjader, I.3    Gustafsson, T.4    Wernerman, J.5    Rooyackers, O.6
  • 33
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division
    • Arthur, J. S., Elce, J. S., Hegadorn, C., Williams, K. and Greer, P. A., Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol. Cell Biol. 2000. 20: 4474-4481.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 34
    • 0033788531 scopus 로고    scopus 로고
    • The calpain small subunit gene is essential: its inactivation results in embryonic lethality
    • Zimmerman, U. J., Boring, L., Pak, J. H., Mukerjee, N. and Wang, K. K., The calpain small subunit gene is essential: its inactivation results in embryonic lethality. IUBMB Life 2000. 50: 63-68.
    • (2000) IUBMB Life , vol.50 , pp. 63-68
    • Zimmerman, U.J.1    Boring, L.2    Pak, J.H.3    Mukerjee, N.4    Wang, K.K.5
  • 35
    • 33745686005 scopus 로고    scopus 로고
    • Conditional disruption of ubiquitous calpains in the mouse
    • Tan, Y., Dourdin, N., Wu, C., De Veyra, T., Elce, J. S. and Greer, P. A., Conditional disruption of ubiquitous calpains in the mouse. Genesis 2006. 44: 297-303.
    • (2006) Genesis , vol.44 , pp. 297-303
    • Tan, Y.1    Dourdin, N.2    Wu, C.3    De Veyra, T.4    Elce, J.S.5    Greer, P.A.6
  • 36
    • 0035801698 scopus 로고    scopus 로고
    • FES-Cre targets phosphatidylinositol glycan class A (PIGA) inactivation to hematopoietic stem cells in the bone marrow
    • Keller, P., Payne, J. L., Tremml, G., Greer, P. A., Gaboli, M., Pandolfi, P. P. and Bessler, M., FES-Cre targets phosphatidylinositol glycan class A (PIGA) inactivation to hematopoietic stem cells in the bone marrow. J. Exp. Med. 2001. 194: 581-589.
    • (2001) J. Exp. Med. , vol.194 , pp. 581-589
    • Keller, P.1    Payne, J.L.2    Tremml, G.3    Greer, P.A.4    Gaboli, M.5    Pandolfi, P.P.6    Bessler, M.7
  • 37
    • 0025353696 scopus 로고
    • Myeloid expression of the human c-fps/fes proto-oncogene in transgenic mice
    • Greer, P., Maltby, V., Rossant, J., Bernstein, A. and Pawson, T., Myeloid expression of the human c-fps/fes proto-oncogene in transgenic mice. Mol. Cell Biol. 1990. 10: 2521-2527.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 2521-2527
    • Greer, P.1    Maltby, V.2    Rossant, J.3    Bernstein, A.4    Pawson, T.5
  • 38
    • 0029804948 scopus 로고    scopus 로고
    • The fps/fes tyrosine kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells and is localized in the trans-golgi network
    • Haigh, J., McVeigh, J. and Greer, P., The fps/fes tyrosine kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells and is localized in the trans-golgi network. Cell Growth Differ. 1996. 7: 931-944.
    • (1996) Cell Growth Differ. , vol.7 , pp. 931-944
    • Haigh, J.1    McVeigh, J.2    Greer, P.3
  • 39
    • 84858843244 scopus 로고    scopus 로고
    • FES/FER kinase signaling in hematopoietic cells and leukemias
    • Craig, A. W., FES/FER kinase signaling in hematopoietic cells and leukemias. Front Biosci. 2012. 17: 861-875.
    • (2012) Front Biosci. , vol.17 , pp. 861-875
    • Craig, A.W.1
  • 40
    • 58849112217 scopus 로고    scopus 로고
    • Alveolar macrophages from septic mice promote polymorphonuclear leukocyte transendothelial migration via an endothelial cell Src kinase/NADPH oxidase pathway
    • Wang, Z., Rui, T., Yang, M., Valiyeva, F. and Kvietys, P. R., Alveolar macrophages from septic mice promote polymorphonuclear leukocyte transendothelial migration via an endothelial cell Src kinase/NADPH oxidase pathway. J. Immunol. 2008. 181: 8735-8744.
    • (2008) J. Immunol. , vol.181 , pp. 8735-8744
    • Wang, Z.1    Rui, T.2    Yang, M.3    Valiyeva, F.4    Kvietys, P.R.5
  • 41
    • 84874248044 scopus 로고    scopus 로고
    • Intracellular interleukin-1 receptor 2 binding prevents cleavage and activity of interleukin-1alpha, controlling necrosis-induced sterile inflammation
    • Zheng, Y., Humphry, M., Maguire, J. J., Bennett, M. R. and Clarke, M. C., Intracellular interleukin-1 receptor 2 binding prevents cleavage and activity of interleukin-1alpha, controlling necrosis-induced sterile inflammation. Immunity 2013. 38: 285-295.
    • (2013) Immunity , vol.38 , pp. 285-295
    • Zheng, Y.1    Humphry, M.2    Maguire, J.J.3    Bennett, M.R.4    Clarke, M.C.5
  • 42
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth, J. D., NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 2004. 4: 181-189.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 45
    • 62649139025 scopus 로고    scopus 로고
    • Immunological and inflammatory functions of the interleukin-1 family
    • Dinarello, C. A., Immunological and inflammatory functions of the interleukin-1 family. Annu. Rev. Immunol. 2009. 27: 519-550.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 519-550
    • Dinarello, C.A.1
  • 46
    • 84876284629 scopus 로고    scopus 로고
    • Regulation of interleukin 1alpha secretion by inflammasomes
    • Yazdi, A. S. and Drexler, S. K., Regulation of interleukin 1alpha secretion by inflammasomes. Ann. Rheum. Dis. 2013. 72(Suppl 2): ii96-ii99.
    • (2013) Ann. Rheum. Dis. , vol.72 , Issue.SUPPL. 2 , pp. 296-299
    • Yazdi, A.S.1    Drexler, S.K.2
  • 47
    • 34447116244 scopus 로고    scopus 로고
    • Identification of a key pathway required for the sterile inflammatory response triggered by dying cells
    • Chen, C. J., Kono, H., Golenbock, D., Reed, G., Akira, S. and Rock, K. L., Identification of a key pathway required for the sterile inflammatory response triggered by dying cells. Nat. Med. 2007. 13: 851-856.
    • (2007) Nat. Med. , vol.13 , pp. 851-856
    • Chen, C.J.1    Kono, H.2    Golenbock, D.3    Reed, G.4    Akira, S.5    Rock, K.L.6
  • 49
    • 82455175456 scopus 로고    scopus 로고
    • Granzyme B-dependent proteolysis acts as a switch to enhance the proinflammatory activity of IL-1alpha
    • Afonina, I. S., Tynan, G. A., Logue, S. E., Cullen, S. P., Bots, M., Luthi, A. U., Reeves, E. P. et al., Granzyme B-dependent proteolysis acts as a switch to enhance the proinflammatory activity of IL-1alpha. Mol. Cell 2011. 44: 265-278.
    • (2011) Mol. Cell , vol.44 , pp. 265-278
    • Afonina, I.S.1    Tynan, G.A.2    Logue, S.E.3    Cullen, S.P.4    Bots, M.5    Luthi, A.U.6    Reeves, E.P.7
  • 50
    • 30444459066 scopus 로고    scopus 로고
    • MyD88 mediates neutrophil recruitment initiated by IL-1R but not TLR2 activation in immunity against Staphylococcus aureus
    • Miller, L. S., O'Connell, R. M., Gutierrez, M. A., Pietras, E. M., Shahangian, A., Gross, C. E., Thirumala, A. et al., MyD88 mediates neutrophil recruitment initiated by IL-1R but not TLR2 activation in immunity against Staphylococcus aureus. Immunity 2006. 24: 79-91.
    • (2006) Immunity , vol.24 , pp. 79-91
    • Miller, L.S.1    O'Connell, R.M.2    Gutierrez, M.A.3    Pietras, E.M.4    Shahangian, A.5    Gross, C.E.6    Thirumala, A.7
  • 52
    • 67649303340 scopus 로고    scopus 로고
    • Over-expression of calpastatin inhibits calpain activation and attenuates myocardial dysfunction during endotoxaemia
    • Li, X., Li, Y., Shan, L., Shen, E., Chen, R. and Peng, T., Over-expression of calpastatin inhibits calpain activation and attenuates myocardial dysfunction during endotoxaemia. Cardiovasc. Res. 2009. 83: 72-79.
    • (2009) Cardiovasc. Res. , vol.83 , pp. 72-79
    • Li, X.1    Li, Y.2    Shan, L.3    Shen, E.4    Chen, R.5    Peng, T.6
  • 53
    • 0029553849 scopus 로고
    • Cellular and molecular mechanisms of TNF protection in septic peritonitis
    • Echtenacher, B., Hultner, L. and Mannel, D. N., Cellular and molecular mechanisms of TNF protection in septic peritonitis. J. Inflamm. 1995. 47: 85-89.
    • (1995) J. Inflamm. , vol.47 , pp. 85-89
    • Echtenacher, B.1    Hultner, L.2    Mannel, D.N.3
  • 54
    • 0029892080 scopus 로고    scopus 로고
    • Critical protective role of mast cells in a model of acute septic peritonitis
    • Echtenacher, B., Mannel, D. N. and Hultner, L., Critical protective role of mast cells in a model of acute septic peritonitis. Nature 1996. 381: 75-77.
    • (1996) Nature , vol.381 , pp. 75-77
    • Echtenacher, B.1    Mannel, D.N.2    Hultner, L.3
  • 55
    • 0027080131 scopus 로고
    • Neutrophil recruitment by tumor necrosis factor from mast cells in immune complex peritonitis
    • Zhang, Y., Ramos, B. F. and Jakschik, B. A., Neutrophil recruitment by tumor necrosis factor from mast cells in immune complex peritonitis. Science 1992. 258: 1957-1959.
    • (1992) Science , vol.258 , pp. 1957-1959
    • Zhang, Y.1    Ramos, B.F.2    Jakschik, B.A.3
  • 57
    • 84864299611 scopus 로고    scopus 로고
    • Widespread immunological functions of mast cells: fact or fiction?
    • Rodewald, H. R. and Feyerabend, T. B., Widespread immunological functions of mast cells: fact or fiction? Immunity 2012. 37: 13-24.
    • (2012) Immunity , vol.37 , pp. 13-24
    • Rodewald, H.R.1    Feyerabend, T.B.2
  • 58
    • 79959362680 scopus 로고    scopus 로고
    • Mast cells are key promoters of contact allergy that mediate the adjuvant effects of haptens
    • Dudeck, A., Dudeck, J., Scholten, J., Petzold, A., Surianarayanan, S., Kohler, A., Peschke, K. et al., Mast cells are key promoters of contact allergy that mediate the adjuvant effects of haptens. Immunity 2011. 34: 973-984.
    • (2011) Immunity , vol.34 , pp. 973-984
    • Dudeck, A.1    Dudeck, J.2    Scholten, J.3    Petzold, A.4    Surianarayanan, S.5    Kohler, A.6    Peschke, K.7
  • 59
    • 81955164074 scopus 로고    scopus 로고
    • Cre-mediated cell ablation contests mast cell contribution in models of antibody- and T cell-mediated autoimmunity
    • Feyerabend, T. B., Weiser, A., Tietz, A., Stassen, M., Harris, N., Kopf, M., Radermacher, P. et al., Cre-mediated cell ablation contests mast cell contribution in models of antibody- and T cell-mediated autoimmunity. Immunity 2011. 35: 832-844.
    • (2011) Immunity , vol.35 , pp. 832-844
    • Feyerabend, T.B.1    Weiser, A.2    Tietz, A.3    Stassen, M.4    Harris, N.5    Kopf, M.6    Radermacher, P.7
  • 60
    • 84860370817 scopus 로고    scopus 로고
    • Inhibition of calpain blocks the phagosomal escape of Listeria monocytogenes
    • Lopez-Castejon, G., Corbett, D., Goldrick, M., Roberts, I. S. and Brough, D., Inhibition of calpain blocks the phagosomal escape of Listeria monocytogenes. PLoS One 2012. 7: e35936.
    • (2012) PLoS One , vol.7
    • Lopez-Castejon, G.1    Corbett, D.2    Goldrick, M.3    Roberts, I.S.4    Brough, D.5
  • 61
    • 84861164816 scopus 로고    scopus 로고
    • Reactive oxygen species produced by the NADPH oxidase 2 complex in monocytes protect mice from bacterial infections
    • Pizzolla, A., Hultqvist, M., Nilson, B., Grimm, M. J., Eneljung, T., Jonsson, I. M., Verdrengh, M. et al., Reactive oxygen species produced by the NADPH oxidase 2 complex in monocytes protect mice from bacterial infections. J. Immunol. 2012. 188: 5003-5011.
    • (2012) J. Immunol. , vol.188 , pp. 5003-5011
    • Pizzolla, A.1    Hultqvist, M.2    Nilson, B.3    Grimm, M.J.4    Eneljung, T.5    Jonsson, I.M.6    Verdrengh, M.7
  • 62
    • 33744918550 scopus 로고    scopus 로고
    • Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis
    • Tan, Y., Dourdin, N., Wu, C., De Veyra, T., Elce, J. S. and Greer, P. A., Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis. J. Biol. Chem. 2006. 281: 16016-16024.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16016-16024
    • Tan, Y.1    Dourdin, N.2    Wu, C.3    De Veyra, T.4    Elce, J.S.5    Greer, P.A.6
  • 63
    • 33845433766 scopus 로고    scopus 로고
    • The Fps/Fes kinase regulates the inflammatory response to endotoxin through down-regulation of TLR4, NF-kappaB activation, and TNF-alpha secretion in macrophages
    • Parsons, S. A. and Greer, P. A., The Fps/Fes kinase regulates the inflammatory response to endotoxin through down-regulation of TLR4, NF-kappaB activation, and TNF-alpha secretion in macrophages. J. Leukoc. Biol. 2006. 80: 1522-1528.
    • (2006) J. Leukoc. Biol. , vol.80 , pp. 1522-1528
    • Parsons, S.A.1    Greer, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.