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Volumn 75, Issue 15, 2012, Pages 4734-4746

Sub-proteomic study on macrophage response to Candida albicans unravels new proteins involved in the host defense against the fungus

Author keywords

Candida albicans; Galectin 3; Inflammation; Macrophages; Oxidative stress; Subcellular

Indexed keywords

CELL PROTEIN; ENDOPLASMIC RETICULUM PROTEIN; GALECTIN 3; MEMBRANE RECEPTOR; MITOCHONDRIAL PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 84864097735     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.01.037     Document Type: Article
Times cited : (22)

References (73)
  • 1
    • 0035217138 scopus 로고    scopus 로고
    • Antifungal susceptibility testing. New technology and clinical applications
    • Pfaller M.A., Yu W.L. Antifungal susceptibility testing. New technology and clinical applications. Infect Dis Clin North Am 2001, 15:1227-1261.
    • (2001) Infect Dis Clin North Am , vol.15 , pp. 1227-1261
    • Pfaller, M.A.1    Yu, W.L.2
  • 2
    • 33846466508 scopus 로고    scopus 로고
    • Epidemiology of invasive candidiasis: a persistent public health problem
    • Pfaller M.A., Diekema D.J. Epidemiology of invasive candidiasis: a persistent public health problem. Clin Microbiol Rev 2007, 20:133-163.
    • (2007) Clin Microbiol Rev , vol.20 , pp. 133-163
    • Pfaller, M.A.1    Diekema, D.J.2
  • 3
    • 0033869563 scopus 로고    scopus 로고
    • Flucytosine: a review of its pharmacology, clinical indications, pharmacokinetics, toxicity and drug interactions
    • Vermes A., Guchelaar H.J., Dankert J. Flucytosine: a review of its pharmacology, clinical indications, pharmacokinetics, toxicity and drug interactions. J Antimicrob Chemother 2000, 46:171-179.
    • (2000) J Antimicrob Chemother , vol.46 , pp. 171-179
    • Vermes, A.1    Guchelaar, H.J.2    Dankert, J.3
  • 4
    • 0035282477 scopus 로고    scopus 로고
    • Mortality and costs of acute renal failure associated with amphotericin B therapy
    • Bates D.W., Su L., Yu D.T., Chertow G.M., Seger D.L., Gomes D.R., et al. Mortality and costs of acute renal failure associated with amphotericin B therapy. Clin Infect Dis 2001, 32:686-693.
    • (2001) Clin Infect Dis , vol.32 , pp. 686-693
    • Bates, D.W.1    Su, L.2    Yu, D.T.3    Chertow, G.M.4    Seger, D.L.5    Gomes, D.R.6
  • 6
    • 0028223193 scopus 로고
    • Elimination of mouse splenic macrophages correlates with increased susceptibility to experimental disseminated candidiasis
    • Qian Q., Jutila M.A., van Rooijen N., Cutler J.E. Elimination of mouse splenic macrophages correlates with increased susceptibility to experimental disseminated candidiasis. J Immunol 1994, 152:5000-5008.
    • (1994) J Immunol , vol.152 , pp. 5000-5008
    • Qian, Q.1    Jutila, M.A.2    van Rooijen, N.3    Cutler, J.E.4
  • 7
    • 66749114259 scopus 로고    scopus 로고
    • Host responses to a versatile commensal: PAMPs and PRRs interplay leading to tolerance or infection by Candida albicans
    • Jouault T., Sarazin A., Martinez-Esparza M., Fradin C., Sendid B., Poulain D. Host responses to a versatile commensal: PAMPs and PRRs interplay leading to tolerance or infection by Candida albicans. Cell Microbiol 2009, 11:1007-1015.
    • (2009) Cell Microbiol , vol.11 , pp. 1007-1015
    • Jouault, T.1    Sarazin, A.2    Martinez-Esparza, M.3    Fradin, C.4    Sendid, B.5    Poulain, D.6
  • 8
    • 77956185307 scopus 로고    scopus 로고
    • Innate immune mechanisms for recognition and uptake of Candida species
    • Netea M.G., Marodi L. Innate immune mechanisms for recognition and uptake of Candida species. Trends Immunol 2010, 31:346-353.
    • (2010) Trends Immunol , vol.31 , pp. 346-353
    • Netea, M.G.1    Marodi, L.2
  • 9
    • 77955415951 scopus 로고    scopus 로고
    • Fungal attacks on mammalian hosts: pathogen elimination requires sensing and tasting
    • Bourgeois C., Majer O., Frohner I.E., Tierney L., Kuchler K. Fungal attacks on mammalian hosts: pathogen elimination requires sensing and tasting. Curr Opin Microbiol 2010, 13:401-408.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 401-408
    • Bourgeois, C.1    Majer, O.2    Frohner, I.E.3    Tierney, L.4    Kuchler, K.5
  • 10
    • 11844275910 scopus 로고    scopus 로고
    • Ligand recognition by antigen-presenting cell C-type lectin receptors
    • McGreal E.P., Miller J.L., Gordon S. Ligand recognition by antigen-presenting cell C-type lectin receptors. Curr Opin Immunol 2005, 17:18-24.
    • (2005) Curr Opin Immunol , vol.17 , pp. 18-24
    • McGreal, E.P.1    Miller, J.L.2    Gordon, S.3
  • 11
    • 0033035316 scopus 로고    scopus 로고
    • Candida albicans suppresses nitric oxide (NO) production by interferon-gamma (IFN-gamma) and lipopolysaccharide (LPS)-stimulated murine peritoneal macrophages
    • Chinen T., Qureshi M.H., Koguchi Y., Kawakami K. Candida albicans suppresses nitric oxide (NO) production by interferon-gamma (IFN-gamma) and lipopolysaccharide (LPS)-stimulated murine peritoneal macrophages. Clin Exp Immunol 1999, 115:491-497.
    • (1999) Clin Exp Immunol , vol.115 , pp. 491-497
    • Chinen, T.1    Qureshi, M.H.2    Koguchi, Y.3    Kawakami, K.4
  • 13
    • 0025772031 scopus 로고
    • Mechanisms of host defense against Candida species. I. Phagocytosis by monocytes and monocyte-derived macrophages
    • Marodi L., Korchak H.M., Johnston R.B. Mechanisms of host defense against Candida species. I. Phagocytosis by monocytes and monocyte-derived macrophages. J Immunol 1991, 146:2783-2789.
    • (1991) J Immunol , vol.146 , pp. 2783-2789
    • Marodi, L.1    Korchak, H.M.2    Johnston, R.B.3
  • 14
    • 0025857228 scopus 로고
    • Mechanisms of host defense against Candida species. II. Biochemical basis for the killing of Candida by mononuclear phagocytes
    • Marodi L., Forehand J.R., Johnston R.B. Mechanisms of host defense against Candida species. II. Biochemical basis for the killing of Candida by mononuclear phagocytes. J Immunol 1991, 146:2790-2794.
    • (1991) J Immunol , vol.146 , pp. 2790-2794
    • Marodi, L.1    Forehand, J.R.2    Johnston, R.B.3
  • 15
    • 12844262948 scopus 로고    scopus 로고
    • Enhanced killing of Candida albicans by human macrophages adherent to type 1 collagen matrices via induction of phagolysosomal fusion
    • Newman S.L., Bhugra B., Holly A., Morris R.E. Enhanced killing of Candida albicans by human macrophages adherent to type 1 collagen matrices via induction of phagolysosomal fusion. Infect Immun 2005, 73:770-777.
    • (2005) Infect Immun , vol.73 , pp. 770-777
    • Newman, S.L.1    Bhugra, B.2    Holly, A.3    Morris, R.E.4
  • 16
    • 0028953653 scopus 로고
    • Nitric oxide production does not directly increase macrophage candidacidal activity
    • Vázquez-Torres A., Jones-Carson J., Balish E. Nitric oxide production does not directly increase macrophage candidacidal activity. Infect Immun 1995, 63:1142-1144.
    • (1995) Infect Immun , vol.63 , pp. 1142-1144
    • Vázquez-Torres, A.1    Jones-Carson, J.2    Balish, E.3
  • 17
    • 34147130534 scopus 로고    scopus 로고
    • Differential protein expression of murine macrophages upon interaction with Candida albicans
    • Martínez-Solano L., Nombela C., Molero G., Gil C. Differential protein expression of murine macrophages upon interaction with Candida albicans. Proteomics 2006, 6(Suppl 1):S133-S144.
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 1
    • Martínez-Solano, L.1    Nombela, C.2    Molero, G.3    Gil, C.4
  • 18
    • 67649158210 scopus 로고    scopus 로고
    • Proteomics of RAW 264.7 macrophages upon interaction with heat-inactivated Candida albicans cells unravel an anti-inflammatory response
    • Martínez-Solano L., Reales-Calderón J.A., Nombela C., Molero G., Gil C. Proteomics of RAW 264.7 macrophages upon interaction with heat-inactivated Candida albicans cells unravel an anti-inflammatory response. Proteomics 2009, 9:2995-3010.
    • (2009) Proteomics , vol.9 , pp. 2995-3010
    • Martínez-Solano, L.1    Reales-Calderón, J.A.2    Nombela, C.3    Molero, G.4    Gil, C.5
  • 19
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: a single gel method for detecting changes in protein extracts
    • Unlu M., Morgan M.E., Minden J.S. Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18:2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 20
    • 27944456827 scopus 로고    scopus 로고
    • Development and application of proteomics technologies in Saccharomyces cerevisiae
    • Kolkman A., Slijper M., Heck A.J. Development and application of proteomics technologies in Saccharomyces cerevisiae. Trends Biotechnol 2005, 23:598-604.
    • (2005) Trends Biotechnol , vol.23 , pp. 598-604
    • Kolkman, A.1    Slijper, M.2    Heck, A.J.3
  • 21
    • 0021742042 scopus 로고
    • Isolation of the Candida albicans gene for orotidine-5'-phosphate decarboxylase by complementation of S. cerevisiae ura3 and E. coli pyrF mutations
    • Gillum A.M., Tsay E.Y., Kirsch D.R. Isolation of the Candida albicans gene for orotidine-5'-phosphate decarboxylase by complementation of S. cerevisiae ura3 and E. coli pyrF mutations. Mol Gen Genet 1984, 198:179-182.
    • (1984) Mol Gen Genet , vol.198 , pp. 179-182
    • Gillum, A.M.1    Tsay, E.Y.2    Kirsch, D.R.3
  • 22
    • 34548409217 scopus 로고    scopus 로고
    • Experimental and statistical considerations to avoid false conclusions in proteomics studies using differential in-gel electrophoresis
    • Karp N.A., McCormick P.S., Russell M.R., Lilley K.S. Experimental and statistical considerations to avoid false conclusions in proteomics studies using differential in-gel electrophoresis. Mol Cell Proteomics 2007, 6:1354-1364.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1354-1364
    • Karp, N.A.1    McCormick, P.S.2    Russell, M.R.3    Lilley, K.S.4
  • 23
    • 0032535467 scopus 로고    scopus 로고
    • Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification
    • Sechi S., Chait B.T. Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification. Anal Chem Dec 15 1998, 70(24):5150-5158.
    • (1998) Anal Chem , vol.70 , Issue.24 , pp. 5150-5158
    • Sechi, S.1    Chait, B.T.2
  • 24
    • 70350238654 scopus 로고    scopus 로고
    • Proteopathogen, a protein database for studying Candida albicans-host interaction
    • Vialás V., Nogales-Cadenas R., Nombela C., Pascual-Montano A., Gil C. Proteopathogen, a protein database for studying Candida albicans-host interaction. Proteomics 2009, 9:4664-4668.
    • (2009) Proteomics , vol.9 , pp. 4664-4668
    • Vialás, V.1    Nogales-Cadenas, R.2    Nombela, C.3    Pascual-Montano, A.4    Gil, C.5
  • 25
    • 0347154004 scopus 로고    scopus 로고
    • Two different NO-dependent mechanisms account for the low virulence of a non-mycelial morphological mutant of Candida albicans
    • Diez-Orejas R., Molero G., Moro M.A., Gil C., Nombela C., Sánchez-Pérez M. Two different NO-dependent mechanisms account for the low virulence of a non-mycelial morphological mutant of Candida albicans. Med Microbiol Immunol (Berl) 2001, 189:153-160.
    • (2001) Med Microbiol Immunol (Berl) , vol.189 , pp. 153-160
    • Diez-Orejas, R.1    Molero, G.2    Moro, M.A.3    Gil, C.4    Nombela, C.5    Sánchez-Pérez, M.6
  • 26
    • 2542462280 scopus 로고    scopus 로고
    • Reductions in linker histone levels are tolerated in developing spermatocytes but cause changes in specific gene expression
    • Lin Q., Inselman A., Han X., Xu H., Zhang W., Handel M.A., et al. Reductions in linker histone levels are tolerated in developing spermatocytes but cause changes in specific gene expression. J Biol Chem 2004, 279:23525-23535.
    • (2004) J Biol Chem , vol.279 , pp. 23525-23535
    • Lin, Q.1    Inselman, A.2    Han, X.3    Xu, H.4    Zhang, W.5    Handel, M.A.6
  • 28
    • 0032714092 scopus 로고    scopus 로고
    • Secretion of the galectin family of mammalian carbohydrate-binding proteins
    • Hughes R.C. Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim Biophys Acta 1999, 1473:172-185.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 172-185
    • Hughes, R.C.1
  • 29
    • 0033572093 scopus 로고    scopus 로고
    • The NH2 terminus of galectin-3 governs cellular compartmentalization and functions in cancer cells
    • Gong H.C., Honjo Y., Nangia-Makker P., Hogan V., Mazurak N., Bresalier R.S., et al. The NH2 terminus of galectin-3 governs cellular compartmentalization and functions in cancer cells. Cancer Res 1999, 59:6239-6245.
    • (1999) Cancer Res , vol.59 , pp. 6239-6245
    • Gong, H.C.1    Honjo, Y.2    Nangia-Makker, P.3    Hogan, V.4    Mazurak, N.5    Bresalier, R.S.6
  • 30
    • 33749125248 scopus 로고    scopus 로고
    • Galectin-3 induces death of Candida species expressing specific beta-1,2-linked mannans
    • Kohatsu L., Hsu D.K., Jegalian A.G., Liu F.T., Baum L.G. Galectin-3 induces death of Candida species expressing specific beta-1,2-linked mannans. J Immunol 2006, 177:4718-4726.
    • (2006) J Immunol , vol.177 , pp. 4718-4726
    • Kohatsu, L.1    Hsu, D.K.2    Jegalian, A.G.3    Liu, F.T.4    Baum, L.G.5
  • 31
    • 17644423479 scopus 로고    scopus 로고
    • Peroxiredoxins, oxidative stress, and cell proliferation
    • Immenschuh S., Baumgart-Vogt E. Peroxiredoxins, oxidative stress, and cell proliferation. Antioxid Redox Signal 2005, 7:768-777.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 768-777
    • Immenschuh, S.1    Baumgart-Vogt, E.2
  • 32
    • 77953703114 scopus 로고    scopus 로고
    • Induction of peroxiredoxin I gene expression by LPS involves the Src/PI3K/JNK signalling pathway
    • Bast A., Fischer K., Erttmann S.F., Walther R. Induction of peroxiredoxin I gene expression by LPS involves the Src/PI3K/JNK signalling pathway. Biochim Biophys Acta 2010, 1799:402-410.
    • (2010) Biochim Biophys Acta , vol.1799 , pp. 402-410
    • Bast, A.1    Fischer, K.2    Erttmann, S.F.3    Walther, R.4
  • 33
    • 0027325603 scopus 로고
    • Cloning and characterization of a 23-kDa stress-induced mouse peritoneal macrophage protein
    • Ishii T., Yamada M., Sato H., Matsue M., Taketani S., Nakayama K., et al. Cloning and characterization of a 23-kDa stress-induced mouse peritoneal macrophage protein. J Biol Chem 1993, 268:18633-18636.
    • (1993) J Biol Chem , vol.268 , pp. 18633-18636
    • Ishii, T.1    Yamada, M.2    Sato, H.3    Matsue, M.4    Taketani, S.5    Nakayama, K.6
  • 34
    • 0027252064 scopus 로고
    • Induction of a 23kDa stress protein by oxidative and sulfhydryl-reactive agents in mouse peritoneal macrophages
    • Sato H., Ishii T., Sugita Y., Tateishi N., Bannai S. Induction of a 23kDa stress protein by oxidative and sulfhydryl-reactive agents in mouse peritoneal macrophages. Biochim Biophys Acta 1993, 1148:127-132.
    • (1993) Biochim Biophys Acta , vol.1148 , pp. 127-132
    • Sato, H.1    Ishii, T.2    Sugita, Y.3    Tateishi, N.4    Bannai, S.5
  • 35
    • 19544387788 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies protein disulfide isomerase and peroxiredoxin 1 as new players involved in embryonic interdigital cell death
    • Shan S.W., Tang M.K., Cai D.Q., Chui Y.L., Chow P.H., Grotewold L., et al. Comparative proteomic analysis identifies protein disulfide isomerase and peroxiredoxin 1 as new players involved in embryonic interdigital cell death. Dev Dyn 2005, 233:266-281.
    • (2005) Dev Dyn , vol.233 , pp. 266-281
    • Shan, S.W.1    Tang, M.K.2    Cai, D.Q.3    Chui, Y.L.4    Chow, P.H.5    Grotewold, L.6
  • 36
    • 53649097254 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae infection induces reactive oxygen species and DNA damage in A549 human lung carcinoma cells
    • Sun G., Xu X., Wang Y., Shen X., Chen Z., Yang J. Mycoplasma pneumoniae infection induces reactive oxygen species and DNA damage in A549 human lung carcinoma cells. Infect Immun 2008, 76:4405-4413.
    • (2008) Infect Immun , vol.76 , pp. 4405-4413
    • Sun, G.1    Xu, X.2    Wang, Y.3    Shen, X.4    Chen, Z.5    Yang, J.6
  • 37
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • Rhee S.G., Kang S.W., Jeong W., Chang T.S., Yang K.S., Woo H.A. Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr Opin Cell Biol 2005, 17:183-189.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.S.4    Yang, K.S.5    Woo, H.A.6
  • 39
    • 1942471909 scopus 로고    scopus 로고
    • Protein disulfide isomerase suppresses the transcriptional activity of NF-kappaB
    • Higuchi T., Watanabe Y., Waga I. Protein disulfide isomerase suppresses the transcriptional activity of NF-kappaB. Biochem Biophys Res Commun 2004, 318:46-52.
    • (2004) Biochem Biophys Res Commun , vol.318 , pp. 46-52
    • Higuchi, T.1    Watanabe, Y.2    Waga, I.3
  • 40
    • 34250825393 scopus 로고    scopus 로고
    • Nuclear and cytoplasmic peroxiredoxin-1 differentially regulate NF-kappaB activities
    • Hansen J.M., Moriarty-Craige S., Jones D.P. Nuclear and cytoplasmic peroxiredoxin-1 differentially regulate NF-kappaB activities. Free Radic Biol Med 2007, 43:282-288.
    • (2007) Free Radic Biol Med , vol.43 , pp. 282-288
    • Hansen, J.M.1    Moriarty-Craige, S.2    Jones, D.P.3
  • 42
    • 33749638414 scopus 로고    scopus 로고
    • Comparative proteomic studies on the pathogenesis of human ulcerative colitis
    • Hsieh S.Y., Shih T.C., Yeh C.Y., Lin C.J., Chou Y.Y., Lee Y.S. Comparative proteomic studies on the pathogenesis of human ulcerative colitis. Proteomics 2006, 6:5322-5331.
    • (2006) Proteomics , vol.6 , pp. 5322-5331
    • Hsieh, S.Y.1    Shih, T.C.2    Yeh, C.Y.3    Lin, C.J.4    Chou, Y.Y.5    Lee, Y.S.6
  • 43
    • 42549172433 scopus 로고    scopus 로고
    • Colonization of mice by Candida albicans is promoted by chemically induced colitis and augments inflammatory responses through galectin-3
    • Jawhara S., Thuru X., Standaert-Vitse A., Jouault T., Mordon S., Sendid B., et al. Colonization of mice by Candida albicans is promoted by chemically induced colitis and augments inflammatory responses through galectin-3. J Infect Dis 2008, 197:972-980.
    • (2008) J Infect Dis , vol.197 , pp. 972-980
    • Jawhara, S.1    Thuru, X.2    Standaert-Vitse, A.3    Jouault, T.4    Mordon, S.5    Sendid, B.6
  • 44
    • 0028874589 scopus 로고
    • Expression and function of galectin-3, a beta-galactoside-binding lectin, in human monocytes and macrophages
    • Liu F.T., Hsu D.K., Zuberi R.I., Kuwabara I., Chi E.Y., Henderson W.R. Expression and function of galectin-3, a beta-galactoside-binding lectin, in human monocytes and macrophages. Am J Pathol 1995, 147:1016-1028.
    • (1995) Am J Pathol , vol.147 , pp. 1016-1028
    • Liu, F.T.1    Hsu, D.K.2    Zuberi, R.I.3    Kuwabara, I.4    Chi, E.Y.5    Henderson, W.R.6
  • 46
    • 58149502606 scopus 로고    scopus 로고
    • Modulation of macrophage infiltration and inflammatory activity by the phosphatase SHP-1 in virus-induced demyelinating disease
    • Christophi G.P., Hudson C.A., Panos M., Gruber R.C., Massa P.T. Modulation of macrophage infiltration and inflammatory activity by the phosphatase SHP-1 in virus-induced demyelinating disease. J Virol 2009, 83:522-539.
    • (2009) J Virol , vol.83 , pp. 522-539
    • Christophi, G.P.1    Hudson, C.A.2    Panos, M.3    Gruber, R.C.4    Massa, P.T.5
  • 47
    • 33846056990 scopus 로고    scopus 로고
    • Cardioprotective effects of cerium oxide nanoparticles in a transgenic murine model of cardiomyopathy
    • Niu J., Azfer A., Rogers L.M., Wang X., Kolattukudy P.E. Cardioprotective effects of cerium oxide nanoparticles in a transgenic murine model of cardiomyopathy. Cardiovasc Res 2007, 73:549-559.
    • (2007) Cardiovasc Res , vol.73 , pp. 549-559
    • Niu, J.1    Azfer, A.2    Rogers, L.M.3    Wang, X.4    Kolattukudy, P.E.5
  • 48
    • 79954418920 scopus 로고    scopus 로고
    • Involvement of the constitutive prostaglandin E synthase cPGES/p23 in expression of an initial prostaglandin E2 inactivating enzyme, 15-PGDH
    • Nakatani Y., Hokonohara Y., Tajima Y., Kudo I., Hara S. Involvement of the constitutive prostaglandin E synthase cPGES/p23 in expression of an initial prostaglandin E2 inactivating enzyme, 15-PGDH. Prostaglandins Other Lipid Mediat 2011, 94:112-117.
    • (2011) Prostaglandins Other Lipid Mediat , vol.94 , pp. 112-117
    • Nakatani, Y.1    Hokonohara, Y.2    Tajima, Y.3    Kudo, I.4    Hara, S.5
  • 49
    • 0038306849 scopus 로고    scopus 로고
    • Candida albicans phospholipomannan promotes survival of phagocytosed yeasts through modulation of bad phosphorylation and macrophage apoptosis
    • Ibata-Ombetta S., Idziorek T., Trinel P.A., Poulain D., Jouault T. Candida albicans phospholipomannan promotes survival of phagocytosed yeasts through modulation of bad phosphorylation and macrophage apoptosis. J Biol Chem 2003, 278:13086-13093.
    • (2003) J Biol Chem , vol.278 , pp. 13086-13093
    • Ibata-Ombetta, S.1    Idziorek, T.2    Trinel, P.A.3    Poulain, D.4    Jouault, T.5
  • 50
    • 0033870111 scopus 로고    scopus 로고
    • Targeted disruption of the galectin-3 gene results in attenuated peritoneal inflammatory responses
    • Hsu D.K., Yang R.Y., Pan Z., Yu L., Salomon D.R., Fung-Leung W.P., et al. Targeted disruption of the galectin-3 gene results in attenuated peritoneal inflammatory responses. Am J Pathol 2000, 156:1073-1083.
    • (2000) Am J Pathol , vol.156 , pp. 1073-1083
    • Hsu, D.K.1    Yang, R.Y.2    Pan, Z.3    Yu, L.4    Salomon, D.R.5    Fung-Leung, W.P.6
  • 51
    • 0032803128 scopus 로고    scopus 로고
    • Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl-2 action
    • Morishima N. Changes in nuclear morphology during apoptosis correlate with vimentin cleavage by different caspases located either upstream or downstream of Bcl-2 action. Genes Cells 1999, 4:401-414.
    • (1999) Genes Cells , vol.4 , pp. 401-414
    • Morishima, N.1
  • 52
    • 0035798645 scopus 로고    scopus 로고
    • Identification of a caspase-9 substrate and detection of its cleavage in programmed cell death during mouse development
    • Nakanishi K., Maruyama M., Shibata T., Morishima N. Identification of a caspase-9 substrate and detection of its cleavage in programmed cell death during mouse development. J Biol Chem 2001, 276:41237-41244.
    • (2001) J Biol Chem , vol.276 , pp. 41237-41244
    • Nakanishi, K.1    Maruyama, M.2    Shibata, T.3    Morishima, N.4
  • 53
    • 0035370484 scopus 로고    scopus 로고
    • Caspase-resistant vimentin suppresses apoptosis after photodynamic treatment with a silicon phthalocyanine in Jurkat cells
    • Belichenko I., Morishima N., Separovic D. Caspase-resistant vimentin suppresses apoptosis after photodynamic treatment with a silicon phthalocyanine in Jurkat cells. Arch Biochem Biophys 2001, 390:57-63.
    • (2001) Arch Biochem Biophys , vol.390 , pp. 57-63
    • Belichenko, I.1    Morishima, N.2    Separovic, D.3
  • 54
    • 3442885352 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer protein alpha regulates growth and apoptosis of NIH3T3 cells: involvement of a cannabinoid 1-like receptor
    • Schenning M., van Tiel C.M., Van Manen D., Stam J.C., Gadella B.M., Wirtz K.W., et al. Phosphatidylinositol transfer protein alpha regulates growth and apoptosis of NIH3T3 cells: involvement of a cannabinoid 1-like receptor. J Lipid Res 2004, 45:1555-1564.
    • (2004) J Lipid Res , vol.45 , pp. 1555-1564
    • Schenning, M.1    van Tiel, C.M.2    Van Manen, D.3    Stam, J.C.4    Gadella, B.M.5    Wirtz, K.W.6
  • 55
    • 79958016253 scopus 로고    scopus 로고
    • Proteomic evaluation and validation of cathepsin D regulated proteins in macrophages exposed to Streptococcus pneumoniae
    • M111.008193
    • Bewley M.A., Pham T.K., Marriott H.M., Noirel J., Chu H.P., Ow S.Y., et al. Proteomic evaluation and validation of cathepsin D regulated proteins in macrophages exposed to Streptococcus pneumoniae. Mol Cell Proteomics 2011, 10. M111.008193.
    • (2011) Mol Cell Proteomics , vol.10
    • Bewley, M.A.1    Pham, T.K.2    Marriott, H.M.3    Noirel, J.4    Chu, H.P.5    Ow, S.Y.6
  • 56
    • 0035145592 scopus 로고    scopus 로고
    • HnRNP F influences binding of a 64-kilodalton subunit of cleavage stimulation factor to mRNA precursors in mouse B cells
    • Veraldi K.L., Arhin G.K., Martincic K., Chung-Ganster L.H., Wilusz J., Milcarek C. hnRNP F influences binding of a 64-kilodalton subunit of cleavage stimulation factor to mRNA precursors in mouse B cells. Mol Cell Biol 2001, 21:1228-1238.
    • (2001) Mol Cell Biol , vol.21 , pp. 1228-1238
    • Veraldi, K.L.1    Arhin, G.K.2    Martincic, K.3    Chung-Ganster, L.H.4    Wilusz, J.5    Milcarek, C.6
  • 57
    • 77954759427 scopus 로고    scopus 로고
    • Knockdown of NAPA using short-hairpin RNA sensitizes cancer cells to cisplatin: implications to overcome chemoresistance
    • Wu Z.Z., Chao C.C. Knockdown of NAPA using short-hairpin RNA sensitizes cancer cells to cisplatin: implications to overcome chemoresistance. Biochem Pharmacol 2010, 80:827-837.
    • (2010) Biochem Pharmacol , vol.80 , pp. 827-837
    • Wu, Z.Z.1    Chao, C.C.2
  • 58
    • 22144474008 scopus 로고    scopus 로고
    • Up-regulation of GRP78 and antiapoptotic signaling in murine peritoneal macrophages exposed to insulin
    • Misra U.K., Pizzo S.V. Up-regulation of GRP78 and antiapoptotic signaling in murine peritoneal macrophages exposed to insulin. J Leukoc Biol 2005, 78:187-194.
    • (2005) J Leukoc Biol , vol.78 , pp. 187-194
    • Misra, U.K.1    Pizzo, S.V.2
  • 59
    • 0034013539 scopus 로고    scopus 로고
    • Stress protein GRP78 prevents apoptosis induced by calcium ionophore, ionomycin, but not by glycosylation inhibitor, tunicamycin, in human prostate cancer cells
    • Miyake H., Hara I., Arakawa S., Kamidono S. Stress protein GRP78 prevents apoptosis induced by calcium ionophore, ionomycin, but not by glycosylation inhibitor, tunicamycin, in human prostate cancer cells. J Cell Biochem 2000, 77:396-408.
    • (2000) J Cell Biochem , vol.77 , pp. 396-408
    • Miyake, H.1    Hara, I.2    Arakawa, S.3    Kamidono, S.4
  • 60
    • 77953227279 scopus 로고    scopus 로고
    • The Arabidopsis thaliana Myo-inositol 1-phosphate synthase1 gene is required for Myo-inositol synthesis and suppression of cell death
    • Donahue J.L., Alford S.R., Torabinejad J., Kerwin R.E., Nourbakhsh A., Ray W.K., et al. The Arabidopsis thaliana Myo-inositol 1-phosphate synthase1 gene is required for Myo-inositol synthesis and suppression of cell death. Plant Cell 2010, 22:888-903.
    • (2010) Plant Cell , vol.22 , pp. 888-903
    • Donahue, J.L.1    Alford, S.R.2    Torabinejad, J.3    Kerwin, R.E.4    Nourbakhsh, A.5    Ray, W.K.6
  • 61
    • 0037100508 scopus 로고    scopus 로고
    • Src homology region 2 domain-containing phosphatase 1 positively regulates B cell receptor-induced apoptosis by modulating association of B cell linker protein with Nck and activation of c-Jun NH2-terminal kinase
    • Mizuno K., Tagawa Y., Mitomo K., Watanabe N., Katagiri T., Ogimoto M., et al. Src homology region 2 domain-containing phosphatase 1 positively regulates B cell receptor-induced apoptosis by modulating association of B cell linker protein with Nck and activation of c-Jun NH2-terminal kinase. J Immunol 2002, 169:778-786.
    • (2002) J Immunol , vol.169 , pp. 778-786
    • Mizuno, K.1    Tagawa, Y.2    Mitomo, K.3    Watanabe, N.4    Katagiri, T.5    Ogimoto, M.6
  • 62
    • 77954759427 scopus 로고    scopus 로고
    • Knockdown of NAPA using short-hairpin RNA sensitizes cancer cells to cisplatin: implications to overcome chemoresistance
    • Wu Z.Z., Chao C.C. Knockdown of NAPA using short-hairpin RNA sensitizes cancer cells to cisplatin: implications to overcome chemoresistance. Biochem Pharmacol 2010, 80(6):827-837.
    • (2010) Biochem Pharmacol , vol.80 , Issue.6 , pp. 827-837
    • Wu, Z.Z.1    Chao, C.C.2
  • 63
    • 33847260278 scopus 로고    scopus 로고
    • Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages
    • Yang Y., Liu B., Dai J., Srivastava P.K., Zammit D.J., Lefrancois L., et al. Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages. Immunity 2007, 26:215-226.
    • (2007) Immunity , vol.26 , pp. 215-226
    • Yang, Y.1    Liu, B.2    Dai, J.3    Srivastava, P.K.4    Zammit, D.J.5    Lefrancois, L.6
  • 64
    • 1942485925 scopus 로고    scopus 로고
    • Down-regulation of gp96 by Orientia tsutsugamushi
    • Cho N.H., Choi C.Y., Seong S.Y. Down-regulation of gp96 by Orientia tsutsugamushi. Microbiol Immunol 2004, 48:297-305.
    • (2004) Microbiol Immunol , vol.48 , pp. 297-305
    • Cho, N.H.1    Choi, C.Y.2    Seong, S.Y.3
  • 65
    • 33846044754 scopus 로고    scopus 로고
    • Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes
    • Garbi N., Hammerling G., Tanaka S. Interaction of ERp57 and tapasin in the generation of MHC class I-peptide complexes. Curr Opin Immunol 2007, 19:99-105.
    • (2007) Curr Opin Immunol , vol.19 , pp. 99-105
    • Garbi, N.1    Hammerling, G.2    Tanaka, S.3
  • 66
    • 0034703009 scopus 로고    scopus 로고
    • BiP and PDI cooperate in the oxidative folding of antibodies in vitro
    • Mayer M., Kies U., Kammermeier R., Buchner J. BiP and PDI cooperate in the oxidative folding of antibodies in vitro. J Biol Chem 2000, 275:29421-29425.
    • (2000) J Biol Chem , vol.275 , pp. 29421-29425
    • Mayer, M.1    Kies, U.2    Kammermeier, R.3    Buchner, J.4
  • 67
    • 0034695915 scopus 로고    scopus 로고
    • Live Salmonella recruits N-ethylmaleimide-sensitive fusion protein on phagosomal membrane and promotes fusion with early endosome
    • Mukherjee K., Siddiqi S.A., Hashim S., Raje M., Basu S.K., Mukhopadhyay A. Live Salmonella recruits N-ethylmaleimide-sensitive fusion protein on phagosomal membrane and promotes fusion with early endosome. J Cell Biol 2000, 148:741-753.
    • (2000) J Cell Biol , vol.148 , pp. 741-753
    • Mukherjee, K.1    Siddiqi, S.A.2    Hashim, S.3    Raje, M.4    Basu, S.K.5    Mukhopadhyay, A.6
  • 68
  • 70
    • 0033914833 scopus 로고    scopus 로고
    • Beta-1,2-linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3
    • Fradin C., Poulain D., Jouault T. Beta-1,2-linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3. Infect Immun 2000, 68:4391-4398.
    • (2000) Infect Immun , vol.68 , pp. 4391-4398
    • Fradin, C.1    Poulain, D.2    Jouault, T.3
  • 71
    • 32044459676 scopus 로고    scopus 로고
    • Proteomic analysis of mammalian basic proteins by liquid-based two-dimensional column chromatography
    • Shin Y.K., Lee H.J., Lee J.S., Paik Y.K. Proteomic analysis of mammalian basic proteins by liquid-based two-dimensional column chromatography. Proteomics 2006, 6:1143-1150.
    • (2006) Proteomics , vol.6 , pp. 1143-1150
    • Shin, Y.K.1    Lee, H.J.2    Lee, J.S.3    Paik, Y.K.4
  • 72
    • 33749143645 scopus 로고    scopus 로고
    • Specific recognition of Candida albicans by macrophages requires galectin-3 to discriminate Saccharomyces cerevisiae and needs association with TLR2 for signaling
    • Jouault T., El Abed-El Behi M., Martinez-Esparza M., Breuilh L., Trinel P.A., Chamaillard M., et al. Specific recognition of Candida albicans by macrophages requires galectin-3 to discriminate Saccharomyces cerevisiae and needs association with TLR2 for signaling. J Immunol 2006, 177:4679-4687.
    • (2006) J Immunol , vol.177 , pp. 4679-4687
    • Jouault, T.1    El Abed-El Behi, M.2    Martinez-Esparza, M.3    Breuilh, L.4    Trinel, P.A.5    Chamaillard, M.6
  • 73


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