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Volumn 27, Issue 6, 2013, Pages 2132-2144

Candida albicans secreted aspartic proteases 4-6 induce apoptosis of epithelial cells by a novel Trojan horse mechanism

Author keywords

Infectious diseases; Integrins; Lysosome membrane; Virulence factors

Indexed keywords

ACRIDINE ORANGE; ASPARTIC PROTEINASE; ASPARTIC PROTEINASE 4; ASPARTIC PROTEINASE 5; ASPARTIC PROTEINASE 6; CASPASE; UNCLASSIFIED DRUG;

EID: 84878749300     PISSN: None     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.12-214353     Document Type: Article
Times cited : (59)

References (43)
  • 1
    • 0242323689 scopus 로고    scopus 로고
    • Epidemiology of Candida species infections in critically ill non-immunosuppressed patients
    • Eggimann, P., Garbino, J., and Pittet, D. (2003) Epidemiology of Candida species infections in critically ill non-immunosuppressed patients. Lancet Infect. Dis. 3, 685-7022
    • (2003) Lancet Infect. Dis , vol.3 , pp. 685-702
    • Eggimann, P.1    Garbino, J.2    Pittet, D.3
  • 2
    • 0027511893 scopus 로고
    • Secular trends in the epidemiology of nosocomial fungal infections in the United States, 1980-1990 National Nosocomial Infections Surveillance System
    • Beck-Sague, C., and Jarvis, W. R. (1993) Secular trends in the epidemiology of nosocomial fungal infections in the United States, 1980-1990. National Nosocomial Infections Surveillance System. J. Infect. Dis. 167, 1247-12511
    • (1993) J. Infect. Dis , vol.167 , pp. 1247-1251
    • Beck-Sague, C.1    Jarvis, W.R.2
  • 3
    • 0141789642 scopus 로고    scopus 로고
    • Candida albicans secreted aspartyl proteinases in virulence and pathogenesis
    • Naglik, J. R., Challacombe, S. J., and Hube, B. (2003) Candida albicans secreted aspartyl proteinases in virulence and pathogenesis. Microbiol. Mol. Biol. Rev. 67, 400-4288
    • (2003) Microbiol. Mol. Biol. Rev , vol.67 , pp. 400-428
    • Naglik, J.R.1    Challacombe, S.J.2    Hube, B.3
  • 4
    • 84878768768 scopus 로고    scopus 로고
    • Fungal aspartic proteases as possible therapeutic targets
    • (Ghosh, A. K., ed.), Wiley-VCH Verlag, Weinheim, Germany
    • Monod, M., Staib, P., Reichard, U., Jousson, O. (2010) Fungal aspartic proteases as possible therapeutic targets. In: Aspartic Acid Proteases as Therapeutic Targets (Ghosh, A. K., ed.), pp. 573-606, Wiley-VCH Verlag, Weinheim, Germanyy
    • (2010) Aspartic Acid Proteases As Therapeutic Targets , pp. 573-606
    • Monod, M.1    Staib, P.2    Reichard, U.3    Jousson, O.4
  • 5
    • 0032728881 scopus 로고    scopus 로고
    • HIV-Protease inhibitors reduce cell adherence of Candida albicans strains by inhibition of yeast secreted aspartic proteases
    • Borg-von Zepelin, M., Meyer, I., Thomssen, R., Wurzner, R., Sanglard, D., Telenti, A., and Monod, M. (1999) HIV-Protease inhibitors reduce cell adherence of Candida albicans strains by inhibition of yeast secreted aspartic proteases. J. Invest. Dermatol. 113, 747-7511
    • (1999) J. Invest. Dermatol , vol.113 , pp. 747-751
    • Borg-Von Zepelin, M.1    Meyer, I.2    Thomssen, R.3    Wurzner, R.4    Sanglard, D.5    Telenti, A.6    Monod, M.7
  • 6
  • 8
    • 80053474775 scopus 로고    scopus 로고
    • Comprehensive characterization of secreted aspartic proteases encoded by a virulence gene family in Candida albicans
    • Aoki, W., Kitahara, N., Miura, N., Morisaka, H., Yamamoto, Y., Kuroda, K., and Ueda, M. (2011) Comprehensive characterization of secreted aspartic proteases encoded by a virulence gene family in Candida albicans. J. Biochem. 150, 431-4388
    • (2011) J. Biochem , vol.150 , pp. 431-438
    • Aoki, W.1    Kitahara, N.2    Miura, N.3    Morisaka, H.4    Yamamoto, Y.5    Kuroda, K.6    Ueda, M.7
  • 9
    • 0029645880 scopus 로고
    • The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors
    • Cutfield, S. M., Dodson, E. J., Anderson, B. F., Moody, P. C., Marshall, C. J., Sullivan, P. A., and Cutfield, J. F. (1995) The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors. Structure 3, 1261-12711
    • (1995) Structure , vol.3 , pp. 1261-1271
    • Cutfield, S.M.1    Dodson, E.J.2    Anderson, B.F.3    Moody, P.C.4    Marshall, C.J.5    Sullivan, P.A.6    Cutfield, J.F.7
  • 10
    • 34447525518 scopus 로고    scopus 로고
    • The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A
    • Borelli, C., Ruge, E., Schaller, M., Monod, M., Korting, H. C., Huber, R., and Maskos, K. (2007) The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A. Proteins 68, 738-7488
    • (2007) Proteins , vol.68 , pp. 738-748
    • Borelli, C.1    Ruge, E.2    Schaller, M.3    Monod, M.4    Korting, H.C.5    Huber, R.6    Maskos, K.7
  • 11
    • 51349144006 scopus 로고    scopus 로고
    • X-ray structures of Sap1 and Sap5: Structural comparison of the secreted aspartic proteinases from Candida albicans
    • Borelli, C., Ruge, E., Lee, J. H., Schaller, M., Vogelsang, A., Monod, M., Korting, H. C., Huber, R., and Maskos, K. (2008) X-ray structures of Sap1 and Sap5: structural comparison of the secreted aspartic proteinases from Candida albicans. Proteins 72, 1308-13199
    • (2008) Proteins , vol.72 , pp. 1308-1319
    • Borelli, C.1    Ruge, E.2    Lee, J.H.3    Schaller, M.4    Vogelsang, A.5    Monod, M.6    Korting, H.C.7    Huber, R.8    Maskos, K.9
  • 15
    • 0030884478 scopus 로고    scopus 로고
    • Disruption of each of the secreted aspartyl proteinase genes SAP1, SAP2, and SAP3 of Candida albicans attenuates virulence
    • Hube, B., Sanglard, D., Odds, F. C., Hess, D., Monod, M., Schafer, W., Brown, A. J., and Gow, N. A. (1997) Disruption of each of the secreted aspartyl proteinase genes SAP1, SAP2, and SAP3 of Candida albicans attenuates virulence. Infect. Immun. 65, 3529-35388
    • (1997) Infect. Immun , vol.65 , pp. 3529-3538
    • Hube, B.1    Sanglard, D.2    Odds, F.C.3    Hess, D.4    Monod, M.5    Schafer, W.6    Brown, A.J.7    Gow, N.A.8
  • 16
    • 0030884697 scopus 로고    scopus 로고
    • A triple deletion of the secreted aspartyl proteinase genes SAP4, SAP5, and SAP6 of Candida albicans causes attenuated virulence
    • Sanglard, D., Hube, B., Monod, M., Odds, F. C., and Gow, N. A. (1997) A triple deletion of the secreted aspartyl proteinase genes SAP4, SAP5, and SAP6 of Candida albicans causes attenuated virulence. Infect. Immun. 65, 3539-35466
    • (1997) Infect. Immun , vol.65 , pp. 3539-3546
    • Sanglard, D.1    Hube, B.2    Monod, M.3    Odds, F.C.4    Gow, N.A.5
  • 17
    • 78049434544 scopus 로고    scopus 로고
    • Limited role of secreted aspartyl proteinases Sap1 to Sap6 in Candida albicans virulence and host immune response in murine hematogenously disseminated candidiasis
    • Correia, A., Lermann, U., Teixeira, L., Cerca, F., Botelho, S., da Costa, R. M., Sampaio, P., Gartner, F., Morschhauser, J., Vilanova, M., and Pais, C. (2010) Limited role of secreted aspartyl proteinases Sap1 to Sap6 in Candida albicans virulence and host immune response in murine hematogenously disseminated candidiasis. Infect. Immun. 78, 4839-48499
    • (2010) Infect. Immun , vol.78 , pp. 4839-4849
    • Correia, A.1    Lermann, U.2    Teixeira, L.3    Cerca, F.4    Botelho, S.5    Da Costa, R.M.6    Sampaio, P.7    Gartner, F.8    Morschhauser, J.9    Vilanova, M.10    Pais, C.11
  • 18
    • 57349131646 scopus 로고    scopus 로고
    • Secreted aspartic proteases are not required for invasion of reconstituted human epithelia by Candida albicans
    • Lermann, U., and Morschhauser, J. (2008) Secreted aspartic proteases are not required for invasion of reconstituted human epithelia by Candida albicans. Microbiology 154, 3281-32955
    • (2008) Microbiology , vol.154 , pp. 3281-3295
    • Lermann, U.1    Morschhauser, J.2
  • 19
    • 0013803179 scopus 로고
    • Serum-proteins as nitrogen source for yeastlike fungi
    • Staib, F. (1965) Serum-proteins as nitrogen source for yeastlike fungi. Sabouraudia 4, 187-1933
    • (1965) Sabouraudia , vol.4 , pp. 187-193
    • Staib, F.1
  • 20
    • 0029961316 scopus 로고    scopus 로고
    • Evidence for degradation of gastrointestinal mucin by Candida albicans secretory aspartyl proteinase
    • Colina, A. R., Aumont, F., Deslauriers, N., Belhumeur, P., and de Repentigny, L. (1996) Evidence for degradation of gastrointestinal mucin by Candida albicans secretory aspartyl proteinase. Infect. Immun. 64, 4514-45199
    • (1996) Infect. Immun , vol.64 , pp. 4514-4519
    • Colina, A.R.1    Aumont, F.2    Deslauriers, N.3    Belhumeur, P.4    De Repentigny, L.5
  • 21
    • 17144474933 scopus 로고    scopus 로고
    • Degradation of human subendothelial extracellular matrix by proteinase-secreting Candida albicans
    • Morschhauser, J., Virkola, R., Korhonen, T. K., and Hacker, J. (1997) Degradation of human subendothelial extracellular matrix by proteinase-secreting Candida albicans. FEMS Microbiol. Lett. 153, 349-3555
    • (1997) FEMS Microbiol. Lett , vol.153 , pp. 349-355
    • Morschhauser, J.1    Virkola, R.2    Korhonen, T.K.3    Hacker, J.4
  • 22
    • 0019503111 scopus 로고
    • Properties of a purified proteinase from the yeast Candida albicans
    • Ruchel, R. (1981) Properties of a purified proteinase from the yeast Candida albicans. Biochim. Biophys. Acta 659, 99-1133
    • (1981) Biochim. Biophys. Acta , vol.659 , pp. 99-1133
    • Ruchel, R.1
  • 24
    • 34248370072 scopus 로고    scopus 로고
    • Mucosal tissue invasion by Candida albicans is associated with E-cadherin degradation, mediated by transcription factor Rim101p and protease Sap5p
    • Villar, C. C., Kashleva, H., Nobile, C. J., Mitchell, A. P., and Dongari-Bagtzoglou, A. (2007) Mucosal tissue invasion by Candida albicans is associated with E-cadherin degradation, mediated by transcription factor Rim101p and protease Sap5p. Infect. Immun. 75, 2126-21355
    • (2007) Infect. Immun , vol.75 , pp. 2126-2135
    • Villar, C.C.1    Kashleva, H.2    Nobile, C.J.3    Mitchell, A.P.4    Dongari-Bagtzoglou, A.5
  • 25
    • 0031971193 scopus 로고    scopus 로고
    • The expression of the secreted aspartyl proteinases Sap4 to Sap6 from Candida albicans in murine macrophages
    • Borg-von Zepelin, M., Beggah, S., Boggian, K., Sanglard, D., and Monod, M. (1998) The expression of the secreted aspartyl proteinases Sap4 to Sap6 from Candida albicans in murine macrophages. Mol. Microbiol. 28, 543-5544
    • (1998) Mol. Microbiol , vol.28 , pp. 543-554
    • Borg-Von Zepelin, M.1    Beggah, S.2    Boggian, K.3    Sanglard, D.4    Monod, M.5
  • 26
    • 0015523287 scopus 로고
    • Kinetics and mechanism of pepsinogen activation
    • al-Janabi, J., Hartsuck, J. A., and Tang, J. (1972) Kinetics and mechanism of pepsinogen activation. J. Biol. Chem. 247, 4628-46322
    • (1972) J. Biol. Chem , vol.247 , pp. 4628-4632
    • Al-Janabi, J.1    Hartsuck, J.A.2    Tang, J.3
  • 28
    • 43049152912 scopus 로고    scopus 로고
    • TNF- induces two distinct caspase-8 activation pathways
    • Wang, L., Du, F., and Wang, X. (2008) TNF- induces two distinct caspase-8 activation pathways. Cell 133, 693-7033
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 29
    • 70549101138 scopus 로고    scopus 로고
    • Integrins: Masters and slaves of endocytic transport
    • Caswell, P. T., Vadrevu, S., and Norman, J. C. (2009) Integrins: masters and slaves of endocytic transport. Nat. Rev. Mol. Cell Biol. 10, 843-8533
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 843-853
    • Caswell, P.T.1    Vadrevu, S.2    Norman, J.C.3
  • 30
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri, K. F., and Kroemer, G. (2001) Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3, E255-E2633
    • (2001) Nat. Cell Biol , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 33
    • 36248945066 scopus 로고    scopus 로고
    • Oxidative stress causes a decline in lysosomal integrity during hypothermic incubation of rat hepatocytes
    • Arthur, P. G., Niu, X., Rigby, P., Steer, J. H., and Jeffrey, G. P. (2008) Oxidative stress causes a decline in lysosomal integrity during hypothermic incubation of rat hepatocytes. Free Radic. Biol. Med. 44, 24-333
    • (2008) Free Radic. Biol. Med , vol.44 , pp. 24-33
    • Arthur, P.G.1    Niu, X.2    Rigby, P.3    Steer, J.H.4    Jeffrey, G.P.5
  • 34
    • 33644947905 scopus 로고    scopus 로고
    • Cellular adhesion molecules as targets for bacterial infection
    • Hauck, C. R., Agerer, F., Muenzner, P., and Schmitter, T. (2006) Cellular adhesion molecules as targets for bacterial infection. Eur. J. Cell Biol. 85, 235-2422
    • (2006) Eur. J. Cell Biol , vol.85 , pp. 235-242
    • Hauck, C.R.1    Agerer, F.2    Muenzner, P.3    Schmitter, T.4
  • 35
    • 49649095969 scopus 로고    scopus 로고
    • Caveolin-1-dependent -1 integrin endocytosis is a critical regulator of fibronectin turnover
    • Shi, F., and Sottile, J. (2008) Caveolin-1-dependent -1 integrin endocytosis is a critical regulator of fibronectin turnover. J. Cell Sci. 121, 2360-23711
    • (2008) J. Cell Sci , vol.121 , pp. 2360-2371
    • Shi, F.1    Sottile, J.2
  • 37
    • 35148833480 scopus 로고    scopus 로고
    • Commitment to apoptosis in CD4(+) T lymphocytes productively infected with human immunodeficiency virus type 1 is initiated by lysosomal membrane permeabilization, itself induced by the isolated expression of the viral protein Nef
    • Laforge, M., Petit, F., Estaquier, J., and Senik, A. (2007) Commitment to apoptosis in CD4(+) T lymphocytes productively infected with human immunodeficiency virus type 1 is initiated by lysosomal membrane permeabilization, itself induced by the isolated expression of the viral protein Nef. J. Virol. 81, 11426-114400
    • (2007) J. Virol , vol.81 , pp. 11426-11440
    • Laforge, M.1    Petit, F.2    Estaquier, J.3    Senik, A.4
  • 39
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti, E. (1996) RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 12, 697-7155
    • (1996) Annu. Rev. Cell Dev. Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 40
    • 77951950692 scopus 로고    scopus 로고
    • Candida albicans induces early apoptosis followed by secondary necrosis in oral epithelial cells
    • Villar, C. C., and Zhao, X. R. (2010) Candida albicans induces early apoptosis followed by secondary necrosis in oral epithelial cells. Mol. Oral Microbiol. 25, 215-2255
    • (2010) Mol. Oral Microbiol , vol.25 , pp. 215-225
    • Villar, C.C.1    Zhao, X.R.2
  • 43
    • 0004790502 scopus 로고    scopus 로고
    • Evidence that members of the secretory aspartyl proteinase gene family, in particular SAP2, are virulence factors for Candida vaginitis
    • De Bernardis, F., Arancia, S., Morelli, L., Hube, B., Sanglard, D., Schafer, W., and Cassone, A. (1999) Evidence that members of the secretory aspartyl proteinase gene family, in particular SAP2, are virulence factors for Candida vaginitis. J. Infect. Dis. 179, 201-2088
    • (1999) J. Infect. Dis , vol.179 , pp. 201-208
    • De Bernardis, F.1    Arancia, S.2    Morelli, L.3    Hube, B.4    Sanglard, D.5    Schafer, W.6    Cassone, A.7


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