메뉴 건너뛰기




Volumn 15, Issue 5, 2013, Pages 347-364

Response to oxidative stress in Paracoccidioides yeast cells as determined by proteomic analysis

Author keywords

Antioxidant enzymes; Metabolic profile; Oxidative stress; Paracoccidioides; Proteomic analysis

Indexed keywords

BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE; CATALASE; CYTOCHROME C OXIDASE; CYTOCHROME C PEROXIDASE; FUMARATE REDUCTASE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; MALATE DEHYDROGENASE; OXIDOREDUCTASE; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP); PYRUVATE CARBOXYLASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SUPEROXIDE DISMUTASE; THIOREDOXIN;

EID: 84876830869     PISSN: 12864579     EISSN: 1769714X     Source Type: Journal    
DOI: 10.1016/j.micinf.2012.12.002     Document Type: Article
Times cited : (80)

References (49)
  • 1
    • 36749010860 scopus 로고    scopus 로고
    • Biochemistry of oxidative stress
    • Halliwell B. Biochemistry of oxidative stress. Biochem. Soc. Trans. 2007, 35:1147-1150.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1147-1150
    • Halliwell, B.1
  • 2
    • 33745662190 scopus 로고    scopus 로고
    • Reactive species and antioxidants. Redox biology is a fundamental theme of aerobic life
    • Halliwell B. Reactive species and antioxidants. Redox biology is a fundamental theme of aerobic life. Plant Physiol. 2006, 141:312-322.
    • (2006) Plant Physiol. , vol.141 , pp. 312-322
    • Halliwell, B.1
  • 3
    • 33747764829 scopus 로고    scopus 로고
    • Phagocyte-derived reactive species: salvation or suicide?
    • Halliwell B. Phagocyte-derived reactive species: salvation or suicide?. Trends Biochem. Sci. 2006, 31:509-515.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 509-515
    • Halliwell, B.1
  • 4
    • 78650598564 scopus 로고    scopus 로고
    • Adaptive response to oxidative stress: bacteria, fungi, plants and animals
    • Lushchak V.I. Adaptive response to oxidative stress: bacteria, fungi, plants and animals. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2011, 153:175-190.
    • (2011) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.153 , pp. 175-190
    • Lushchak, V.I.1
  • 5
    • 77955419767 scopus 로고    scopus 로고
    • Interaction of pathogenic yeasts with phagocytes: survival, persistence and escape
    • Seider K., Heyken A., Luttich A., Miramon P., Hube B. Interaction of pathogenic yeasts with phagocytes: survival, persistence and escape. Curr. Opin. Microbiol. 2010, 13:392-400.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 392-400
    • Seider, K.1    Heyken, A.2    Luttich, A.3    Miramon, P.4    Hube, B.5
  • 9
    • 0036301549 scopus 로고    scopus 로고
    • Paracoccidioides brasiliensis and paracoccidioidomycosis: molecular approaches to morphogenesis, diagnosis, epidemiology, taxonomy and genetics
    • San-Blas G., Nino-Vega G., Iturriaga T. Paracoccidioides brasiliensis and paracoccidioidomycosis: molecular approaches to morphogenesis, diagnosis, epidemiology, taxonomy and genetics. Med. Mycol. 2002, 40:225-242.
    • (2002) Med. Mycol. , vol.40 , pp. 225-242
    • San-Blas, G.1    Nino-Vega, G.2    Iturriaga, T.3
  • 10
    • 34249715392 scopus 로고    scopus 로고
    • Paracoccidioides brasiliensis killing by IFN-gamma, TNF-alpha and GM-CSF activated human neutrophils: role for oxygen metabolites
    • Rodrigues D.R., Dias-Melicio L.A., Calvi S.A., Peracoli M.T., Soares A.M. Paracoccidioides brasiliensis killing by IFN-gamma, TNF-alpha and GM-CSF activated human neutrophils: role for oxygen metabolites. Med. Mycol. 2007, 45:27-33.
    • (2007) Med. Mycol. , vol.45 , pp. 27-33
    • Rodrigues, D.R.1    Dias-Melicio, L.A.2    Calvi, S.A.3    Peracoli, M.T.4    Soares, A.M.5
  • 11
    • 46949090953 scopus 로고    scopus 로고
    • Alveolar macrophages from susceptible mice are more competent than those of resistant mice to control initial Paracoccidioides brasiliensis infection
    • Pina A., Bernardino S., Calich V.L. Alveolar macrophages from susceptible mice are more competent than those of resistant mice to control initial Paracoccidioides brasiliensis infection. J. Leukocyte Biol. 2008, 83:1088-1099.
    • (2008) J. Leukocyte Biol. , vol.83 , pp. 1088-1099
    • Pina, A.1    Bernardino, S.2    Calich, V.L.3
  • 17
    • 1242351829 scopus 로고    scopus 로고
    • Monofunctional catalase P of Paracoccidioides brasiliensis: identification, characterization, molecular cloning and expression analysis
    • Moreira S.F., Bailao A.M., Barbosa M.S., Jesuino R.S., Felipe M.S., Pereira M., Soares C.M.A. Monofunctional catalase P of Paracoccidioides brasiliensis: identification, characterization, molecular cloning and expression analysis. Yeast 2004, 21:173-182.
    • (2004) Yeast , vol.21 , pp. 173-182
    • Moreira, S.F.1    Bailao, A.M.2    Barbosa, M.S.3    Jesuino, R.S.4    Felipe, M.S.5    Pereira, M.6    Soares, C.M.A.7
  • 18
    • 44649090610 scopus 로고    scopus 로고
    • Oxidative stress response in Paracoccidioides brasiliensis: assessing catalase and cytochrome C peroxidase
    • Dantas A.S., Andrade R.V., de Carvalho M.J., Felipe M.S., Campos E.G. Oxidative stress response in Paracoccidioides brasiliensis: assessing catalase and cytochrome C peroxidase. Mycol. Res. 2008, 112:747-756.
    • (2008) Mycol. Res. , vol.112 , pp. 747-756
    • Dantas, A.S.1    Andrade, R.V.2    de Carvalho, M.J.3    Felipe, M.S.4    Campos, E.G.5
  • 21
    • 79960852690 scopus 로고    scopus 로고
    • Proteomic analysis reveals that iron availability alters the metabolic status of the pathogenic fungus Paracoccidioides brasiliensis
    • Parente A.F., Borges C.L., Bailão A.M., Sousa M.V., Ricart C.A., winters M.S., Soares C.M.A. Proteomic analysis reveals that iron availability alters the metabolic status of the pathogenic fungus Paracoccidioides brasiliensis. PLoS One 2011, 6:e22810.
    • (2011) PLoS One , vol.6
    • Parente, A.F.1    Borges, C.L.2    Bailão, A.M.3    Sousa, M.V.4    Ricart, C.A.5    Winters, M.S.6    Soares, C.M.A.7
  • 23
    • 15944376183 scopus 로고    scopus 로고
    • The antigenic and catalytically active formamidase of Paracoccidioides brasiliensis: protein characterization, cDNA and gene cloning, heterologous expression and functional analysis of the recombinant protein
    • Borges C.L., Pereira M., Felipe M.S., de Faria F.P., Gomez F.J., Deepe G.S., Soares C.M.A. The antigenic and catalytically active formamidase of Paracoccidioides brasiliensis: protein characterization, cDNA and gene cloning, heterologous expression and functional analysis of the recombinant protein. Microbes. Infect. 2005, 7:66-77.
    • (2005) Microbes. Infect. , vol.7 , pp. 66-77
    • Borges, C.L.1    Pereira, M.2    Felipe, M.S.3    de Faria, F.P.4    Gomez, F.J.5    Deepe, G.S.6    Soares, C.M.A.7
  • 25
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi H. Catalase in vitro. Methods Enzymol. 1984, 105:121-126.
    • (1984) Methods Enzymol. , vol.105 , pp. 121-126
    • Aebi, H.1
  • 28
    • 71049141836 scopus 로고    scopus 로고
    • The malate synthase of Paracoccidioides brasiliensis Pb01 is required in the glyoxylate cycle and in the allantoin degradation pathway
    • Zambuzzi-Carvalho P.F., Cruz A.H., Santos-Silva L.K., Goes A.M., Soares C.M.A., Pereira M. The malate synthase of Paracoccidioides brasiliensis Pb01 is required in the glyoxylate cycle and in the allantoin degradation pathway. Med. Mycol. 2009, 47:734-744.
    • (2009) Med. Mycol. , vol.47 , pp. 734-744
    • Zambuzzi-Carvalho, P.F.1    Cruz, A.H.2    Santos-Silva, L.K.3    Goes, A.M.4    Soares, C.M.A.5    Pereira, M.6
  • 29
    • 39149106038 scopus 로고    scopus 로고
    • High-throughput real-time quantitative reverse transcription PCR
    • John Wiley and Sons, Hoboken NJ, F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, K. Struhl (Eds.)
    • Bookout A.L., Cummins C.L., Mangelsdorf D.J., Pesola J.M., Kramer M.F. High-throughput real-time quantitative reverse transcription PCR. Current Protocols in Molecular Biology 2006, 1581-1628. John Wiley and Sons, Hoboken NJ. F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, K. Struhl (Eds.).
    • (2006) Current Protocols in Molecular Biology , pp. 1581-1628
    • Bookout, A.L.1    Cummins, C.L.2    Mangelsdorf, D.J.3    Pesola, J.M.4    Kramer, M.F.5
  • 30
    • 0037044847 scopus 로고    scopus 로고
    • Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase
    • Messner K.R., Imlay J.A. Mechanism of superoxide and hydrogen peroxide formation by fumarate reductase, succinate dehydrogenase, and aspartate oxidase. J. Biol. Chem. 2002, 277:42563-42571.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42563-42571
    • Messner, K.R.1    Imlay, J.A.2
  • 31
    • 84859510110 scopus 로고    scopus 로고
    • Aconitase B is required for optimal growth of Xanthomonas campestris pv. vesicatoria in pepper plants
    • Kirchberg J., Buttner D., Thiemer B., Sawers R.G. Aconitase B is required for optimal growth of Xanthomonas campestris pv. vesicatoria in pepper plants. PLoS One 2012, 7:e34941.
    • (2012) PLoS One , vol.7
    • Kirchberg, J.1    Buttner, D.2    Thiemer, B.3    Sawers, R.G.4
  • 32
    • 68049143143 scopus 로고    scopus 로고
    • Nitrosative and oxidative stress responses in fungal pathogenicity
    • Brown A.J., Haynes K., Quinn J. Nitrosative and oxidative stress responses in fungal pathogenicity. Curr. Opin. Microbiol. 2009, 12:384-391.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 384-391
    • Brown, A.J.1    Haynes, K.2    Quinn, J.3
  • 35
    • 43149093576 scopus 로고    scopus 로고
    • Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes
    • Perez J.M., Arenas F.A., Pradenas G.A., Sandoval J.M., Vasquez C.C. Escherichia coli YqhD exhibits aldehyde reductase activity and protects from the harmful effect of lipid peroxidation-derived aldehydes. J. Biol. Chem. 2008, 283:7346-7353.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7346-7353
    • Perez, J.M.1    Arenas, F.A.2    Pradenas, G.A.3    Sandoval, J.M.4    Vasquez, C.C.5
  • 36
    • 1542335652 scopus 로고    scopus 로고
    • Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth
    • Cha M.K., Kim W.C., Lim C.J., Kim K., Kim I.H. Escherichia coli periplasmic thiol peroxidase acts as lipid hydroperoxide peroxidase and the principal antioxidative function during anaerobic growth. J. Biol. Chem. 2004, 279:8769-8778.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8769-8778
    • Cha, M.K.1    Kim, W.C.2    Lim, C.J.3    Kim, K.4    Kim, I.H.5
  • 37
  • 38
    • 50349101772 scopus 로고    scopus 로고
    • Oxidative stress-associated impairment of glucose and ammonia metabolism in the filamentous fungus, Aspergillus niger B1-D
    • Li Q., Abrashev R., Harvey L.M., McNeil B. Oxidative stress-associated impairment of glucose and ammonia metabolism in the filamentous fungus, Aspergillus niger B1-D. Mycol. Res. 2008, 112:1049-1055.
    • (2008) Mycol. Res. , vol.112 , pp. 1049-1055
    • Li, Q.1    Abrashev, R.2    Harvey, L.M.3    McNeil, B.4
  • 41
  • 43
    • 33745252231 scopus 로고    scopus 로고
    • Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress
    • Tretter L., Adam-Vizi V. Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress. Philos. Trans. R Soc. Lond B Biol. Sci. 2005, 360:2335-2345.
    • (2005) Philos. Trans. R Soc. Lond B Biol. Sci. , vol.360 , pp. 2335-2345
    • Tretter, L.1    Adam-Vizi, V.2
  • 44
    • 0022386564 scopus 로고
    • Pyruvate and related alpha-ketoacids protect mammalian cells in culture against hydrogen peroxide-induced cytotoxicity
    • Andrae U., Singh J., Ziegler-Skylakakis K. Pyruvate and related alpha-ketoacids protect mammalian cells in culture against hydrogen peroxide-induced cytotoxicity. Toxicol. Lett. 1985, 28:93-98.
    • (1985) Toxicol. Lett. , vol.28 , pp. 93-98
    • Andrae, U.1    Singh, J.2    Ziegler-Skylakakis, K.3
  • 45
    • 0037237973 scopus 로고    scopus 로고
    • Antioxidants, oxidative damage and oxygen deprivation stress: a review
    • Spec No
    • Blokhina O., Virolainen E., Fagerstedt K.V. Antioxidants, oxidative damage and oxygen deprivation stress: a review. Ann. Bot. 2003, 91:179-194. Spec No.
    • (2003) Ann. Bot. , vol.91 , pp. 179-194
    • Blokhina, O.1    Virolainen, E.2    Fagerstedt, K.V.3
  • 47
    • 38149044175 scopus 로고    scopus 로고
    • Adaptive response to oxidative stress in the filamentous fungus Aspergillus niger B1-D
    • Li Q., McNeil B., Harvey L.M. Adaptive response to oxidative stress in the filamentous fungus Aspergillus niger B1-D. Free Radical Biol. Med. 2008, 44:394-402.
    • (2008) Free Radical Biol. Med. , vol.44 , pp. 394-402
    • Li, Q.1    McNeil, B.2    Harvey, L.M.3
  • 48
    • 80955158010 scopus 로고    scopus 로고
    • Adaptive stress response to menadione-induced oxidative stress in Saccharomyces cerevisiae KNU5377
    • Kim I.S., Sohn H.Y., Jin I. Adaptive stress response to menadione-induced oxidative stress in Saccharomyces cerevisiae KNU5377. J. Microbiol. 2011, 49:816-823.
    • (2011) J. Microbiol. , vol.49 , pp. 816-823
    • Kim, I.S.1    Sohn, H.Y.2    Jin, I.3
  • 49
    • 34548563918 scopus 로고    scopus 로고
    • Oxidative stress evokes a metabolic adaptation that favors increased NADPH synthesis and decreased NADH production in Pseudomonas fluorescens
    • Singh R., Mailloux R.J., Puiseux-Dao S., Appanna V.D. Oxidative stress evokes a metabolic adaptation that favors increased NADPH synthesis and decreased NADH production in Pseudomonas fluorescens. J. Bacteriol. 2007, 189:6665-6675.
    • (2007) J. Bacteriol. , vol.189 , pp. 6665-6675
    • Singh, R.1    Mailloux, R.J.2    Puiseux-Dao, S.3    Appanna, V.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.