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Volumn 3, Issue 10, 2009, Pages 1236-1246

Impact of incomplete DNase I treatment on human macrophage proteome analysis

Author keywords

2 D DIGE; Deoxyribonuclease I; Macrophage; MALDI TOF; Proteome

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 3; ALPHA ENOLASE; ALPHA TROPOMYOSIN; BETA TUBULIN; DEOXYRIBONUCLEASE I; ELONGATION FACTOR 2; FILAMIN A; FRUCTOSE 1,6 BISPHOSPHATE; FRUCTOSE BISPHOSPHATE ALDOLASE; GELSOLIN; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE TRANSFERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN 90; LIPOCORTIN 2; MOESIN; PEROXIREDOXIN 1; PHOSPHOGLUCONATE DEHYDROGENASE; PHOSPHOGLYCERATE MUTASE; PROTEIN DISULFIDE ISOMERASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PYRUVATE KINASE; QUERCETIN; RAP1 PROTEIN;

EID: 70350749905     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200900113     Document Type: Article
Times cited : (9)

References (29)
  • 1
    • 34547662422 scopus 로고    scopus 로고
    • In vitro transcription and translation coupled to two-dimensional electrophoresis for bacterial proteome analysis
    • Norais, N., Garaguso, I., Ferrari, G., Grandi, G., In vitro transcription and translation coupled to two-dimensional electrophoresis for bacterial proteome analysis. Methods Mol. Biol. 2007, 375, 183-209.
    • (2007) Methods Mol. Biol , vol.375 , pp. 183-209
    • Norais, N.1    Garaguso, I.2    Ferrari, G.3    Grandi, G.4
  • 2
    • 44449149860 scopus 로고    scopus 로고
    • Isolation and solubilization of gram-positive bacterial cell wall-associated proteins
    • Cole, J. N., Djordjevic, S. P., Walker, M. J., Isolation and solubilization of gram-positive bacterial cell wall-associated proteins. Methods Mol. Biol. 2008, 425, 295-311.
    • (2008) Methods Mol. Biol , vol.425 , pp. 295-311
    • Cole, J.N.1    Djordjevic, S.P.2    Walker, M.J.3
  • 3
    • 0034761973 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis of selenized yeast and autoradiography of 75Se-containing proteins
    • Chéry, C. C., Dumont, E., Cornelis, R., Moens, L., Two-dimensional gel electrophoresis of selenized yeast and autoradiography of 75Se-containing proteins. Fresenius J. Anal. Chem. 2001, 371, 775-781.
    • (2001) Fresenius J. Anal. Chem , vol.371 , pp. 775-781
    • Chéry, C.C.1    Dumont, E.2    Cornelis, R.3    Moens, L.4
  • 4
    • 55249105481 scopus 로고    scopus 로고
    • Comparative proteomic analysis of matched primary and metastatic melanoma cell lines
    • Al-Ghoul, M., Br. uck, T. B., Lauer-Fields, J. L., Asirvatham, V. S. et al., Comparative proteomic analysis of matched primary and metastatic melanoma cell lines. J. Proteome Res. 2008, 7, 4107-4118.
    • (2008) J. Proteome Res , vol.7 , pp. 4107-4118
    • Al-Ghoul, M.1    Br2    uck, T.B.3    Lauer-Fields, J.L.4    Asirvatham, V.S.5
  • 5
    • 34548316688 scopus 로고    scopus 로고
    • Depletion of high-abundance proteins in plasma by immunoaffinity subtraction for two-dimensional difference gel electrophoresis analysis
    • Dardé, V.M., Barderas, M. G., Vivanco, F., Depletion of high-abundance proteins in plasma by immunoaffinity subtraction for two-dimensional difference gel electrophoresis analysis. Methods Mol. Biol. 2007, 357, 351-364.
    • (2007) Methods Mol. Biol , vol.357 , pp. 351-364
    • Dardé, V.M.1    Barderas, M.G.2    Vivanco, F.3
  • 6
    • 40549088497 scopus 로고    scopus 로고
    • Protein profiling of human plasma samples by two-dimensional electrophoresis
    • Cho, S. Y., Lee, E. Y., Kim, H. Y., Kang, M. J. et al., Protein profiling of human plasma samples by two-dimensional electrophoresis. Methods Mol. Biol. 2008, 428, 57-75.
    • (2008) Methods Mol. Biol , vol.428 , pp. 57-75
    • Cho, S.Y.1    Lee, E.Y.2    Kim, H.Y.3    Kang, M.J.4
  • 7
    • 61349198132 scopus 로고    scopus 로고
    • A 2-DE MALDI-TOF study to identify disease regulated serum proteins in lung cancer of c-myc transgenic mice
    • Chatterji, B., Borlak, J., A 2-DE MALDI-TOF study to identify disease regulated serum proteins in lung cancer of c-myc transgenic mice. Proteomics 2009, 9, 1044-1056.
    • (2009) Proteomics , vol.9 , pp. 1044-1056
    • Chatterji, B.1    Borlak, J.2
  • 8
    • 67049095500 scopus 로고    scopus 로고
    • Proteomic Analysis of Mature Soybean Seeds from the Chernobyl Area Suggests Plant Adaptation to the Contaminated Environment
    • Danchenko, M., Skultety, L., Rashydov, N., Berezhna, V. V. et al., Proteomic Analysis of Mature Soybean Seeds from the Chernobyl Area Suggests Plant Adaptation to the Contaminated Environment. J. Proteome Res. 2009, 8, 2915-2922.
    • (2009) J. Proteome Res , vol.8 , pp. 2915-2922
    • Danchenko, M.1    Skultety, L.2    Rashydov, N.3    Berezhna, V.V.4
  • 9
    • 61849108192 scopus 로고    scopus 로고
    • Leaf proteome analysis of transgenic plants expressing antiviral antibodies
    • Di Carli, M., Villani, E., Renzone, G., Nardi, L. et al., Leaf proteome analysis of transgenic plants expressing antiviral antibodies. J. Proteome Res. 2009, 8, 838-848.
    • (2009) J. Proteome Res , vol.8 , pp. 838-848
    • Di Carli, M.1    Villani, E.2    Renzone, G.3    Nardi, L.4
  • 10
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlü, 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
    • Unlü, M.1    Morgan, M.E.2    Minden, J.S.3
  • 11
    • 0035289178 scopus 로고    scopus 로고
    • Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology
    • Tonge, R., Shaw, J., Middleton,B., Rowlinson, R. et al., Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics 2001, 1, 377-396.
    • (2001) Proteomics , vol.1 , pp. 377-396
    • Tonge, R.1    Shaw, J.2    Middleton, B.3    Rowlinson, R.4
  • 12
    • 34147161968 scopus 로고    scopus 로고
    • Application of highly sensitive fluorescent dyes (CyDye DIGE Fluor saturation dyes) to laser microdissection and two-dimensional difference gel electrophoresis (2D-DIGE) for cancer proteomics
    • Kondo, T., Hirohashi, S., Application of highly sensitive fluorescent dyes (CyDye DIGE Fluor saturation dyes) to laser microdissection and two-dimensional difference gel electrophoresis (2D-DIGE) for cancer proteomics. Nat. Protoc. 2006, 1, 2940-2956.
    • (2006) Nat. Protoc , vol.1 , pp. 2940-2956
    • Kondo, T.1    Hirohashi, S.2
  • 13
    • 57649242758 scopus 로고    scopus 로고
    • Proteomic analysis reveals protein changes within layer 2 of the insular cortex in schizophrenia
    • Pennington, K., Dicker, P., Dunn, M. J., Cotter, D. R., Proteomic analysis reveals protein changes within layer 2 of the insular cortex in schizophrenia. Proteomics 2008, 8, 5097-5107.
    • (2008) Proteomics , vol.8 , pp. 5097-5107
    • Pennington, K.1    Dicker, P.2    Dunn, M.J.3    Cotter, D.R.4
  • 14
    • 44449136554 scopus 로고    scopus 로고
    • Application of fluorescence dye saturation labeling for differential proteome analysis of 1,000 microdissected cells from pancreatic ductal adenocarcinoma precursor lesions
    • Sitek, B., Sipos, B., Klöppel, G., Schmiegel, W. et al., Application of fluorescence dye saturation labeling for differential proteome analysis of 1,000 microdissected cells from pancreatic ductal adenocarcinoma precursor lesions. Methods Mol. Biol. 2008, 425, 1-14.
    • (2008) Methods Mol. Biol , vol.425 , pp. 1-14
    • Sitek, B.1    Sipos, B.2    Klöppel, G.3    Schmiegel, W.4
  • 15
    • 12444315072 scopus 로고    scopus 로고
    • Global quantitative phosphoprotein analysis using Multiplexed Proteomics technology
    • Steinberg, T. H., Agnew, B. J., Gee, K. R., Leung, W. Y., Global quantitative phosphoprotein analysis using Multiplexed Proteomics technology. Proteomics 2003, 3, 1128-1144.
    • (2003) Proteomics , vol.3 , pp. 1128-1144
    • Steinberg, T.H.1    Agnew, B.J.2    Gee, K.R.3    Leung, W.Y.4
  • 16
    • 2942560843 scopus 로고    scopus 로고
    • Two-dimensional maps and databases of the human macrophage proteome and secretome
    • Dupont, A., Tokarski, C., Dekeyzer, O., Guihot, A. L. et al., Two-dimensional maps and databases of the human macrophage proteome and secretome. Proteomics 2004, 4, 1761-1778.
    • (2004) Proteomics , vol.4 , pp. 1761-1778
    • Dupont, A.1    Tokarski, C.2    Dekeyzer, O.3    Guihot, A.L.4
  • 17
    • 2942617959 scopus 로고    scopus 로고
    • Morphology, homogeneity and functionality of human monocytes-derived macrophages
    • Pinet, F., Dupont, A., Bencherif, N., Guihot, A. L. et al., Morphology, homogeneity and functionality of human monocytes-derived macrophages. Cell. Mol. Biol. (Noisy-legrand) 2003, 49, 899-905.
    • (2003) Cell. Mol. Biol. (Noisy-legrand) , vol.49 , pp. 899-905
    • Pinet, F.1    Dupont, A.2    Bencherif, N.3    Guihot, A.L.4
  • 18
    • 53049100000 scopus 로고    scopus 로고
    • Application of saturation dye 2D-DIGE proteomics to characterize proteins modulated by oxidized low density lipoprotein treatment of human macrophages
    • Dupont, A., Chwastyniak, M., Beseme, O., Guihot, A. L. et al., Application of saturation dye 2D-DIGE proteomics to characterize proteins modulated by oxidized low density lipoprotein treatment of human macrophages. J. Proteome Res. 2008, 7, 3572-3582.
    • (2008) J. Proteome Res , vol.7 , pp. 3572-3582
    • Dupont, A.1    Chwastyniak, M.2    Beseme, O.3    Guihot, A.L.4
  • 19
    • 34047209848 scopus 로고    scopus 로고
    • Clinical proteomics: A need to define the field and to begin to set adequate standards
    • Mischak, H., Apweiler, R., Banks, R. E., Conaway, M. et al., Clinical proteomics: a need to define the field and to begin to set adequate standards. Proteomics Clin. Appl. 2007, 1, 148-156.
    • (2007) Proteomics Clin. Appl , vol.1 , pp. 148-156
    • Mischak, H.1    Apweiler, R.2    Banks, R.E.3    Conaway, M.4
  • 20
    • 0014385564 scopus 로고
    • Isolation of mononuclear cells and granulocytes from human blood. Isolation of monuclear cells by one centrifugation, and of granulocytes by combining centrifugation and sedimentation at 1 g
    • Böyum, A., Isolation of mononuclear cells and granulocytes from human blood. Isolation of monuclear cells by one centrifugation, and of granulocytes by combining centrifugation and sedimentation at 1 g. Scand. J. Clin. Lab. Invest. Suppl. 1968, 97, 77-89.
    • (1968) Scand. J. Clin. Lab. Invest. Suppl , vol.97 , pp. 77-89
    • Böyum, A.1
  • 21
    • 0016361516 scopus 로고
    • Actin is the naturally occurring inhibitor of deoxyribonuclease I
    • Lazarides, E., Lindberg, U., Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc. Natl. Acad. Sci. USA 1974, 71, 4742-4746.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4742-4746
    • Lazarides, E.1    Lindberg, U.2
  • 22
    • 0018827176 scopus 로고
    • The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin
    • Mannherz, H. G., Goody, R. S., Konrad, M., Nowak, E., The interaction of bovine pancreatic deoxyribonuclease I and skeletal muscle actin. Eur. J. Biochem. 1980, 104, 367-379.
    • (1980) Eur. J. Biochem , vol.104 , pp. 367-379
    • Mannherz, H.G.1    Goody, R.S.2    Konrad, M.3    Nowak, E.4
  • 23
    • 34147150069 scopus 로고    scopus 로고
    • A high-throughput assay shows that DNase-I binds actin monomers and polymers with similar affinity
    • Morrison, S. S., Dawson, J. F., A high-throughput assay shows that DNase-I binds actin monomers and polymers with similar affinity. Anal. Biochem. 2007, 364, 159-164.
    • (2007) Anal. Biochem , vol.364 , pp. 159-164
    • Morrison, S.S.1    Dawson, J.F.2
  • 24
    • 0032528848 scopus 로고    scopus 로고
    • Interactions of elongation factor 2 with the cytoskeleton and interference with DNase I binding to actin
    • Bektaş, M., Nurten, R., Sayers, Z., Bermek, E., Interactions of elongation factor 2 with the cytoskeleton and interference with DNase I binding to actin. Eur. J. Biochem. 1998, 256, 142-147.
    • (1998) Eur. J. Biochem , vol.256 , pp. 142-147
    • Bektaş, M.1    Nurten, R.2    Sayers, Z.3    Bermek, E.4
  • 25
    • 0033662118 scopus 로고    scopus 로고
    • The role of ATP, ADP and divalent cations in the formation of binary and ternary complexes of actin, cofilin and DNase I
    • Chhabra, D., Nosworthy, N. J., dos Remedios, C. G., The role of ATP, ADP and divalent cations in the formation of binary and ternary complexes of actin, cofilin and DNase I. Electrophoresis 2000, 21, 3863-3869.
    • (2000) Electrophoresis , vol.21 , pp. 3863-3869
    • Chhabra, D.1    Nosworthy, N.J.2    dos Remedios, C.G.3
  • 26
    • 23844464107 scopus 로고    scopus 로고
    • The N-terminal fragment of gelsolin inhibitis the interaction of DNase I with isolated actin, but not with the cofilin-actin complex
    • Chhabra, D., The N-terminal fragment of gelsolin inhibitis the interaction of DNase I with isolated actin, but not with the cofilin-actin complex. Proteomics 2005, 5, 3131-3136.
    • (2005) Proteomics , vol.5 , pp. 3131-3136
    • Chhabra, D.1
  • 27
    • 0037378124 scopus 로고    scopus 로고
    • Actin binding proteins: Regulation of cytoskeletal microfilaments
    • dos Remedios, C. G., Chhabra, D., Kekic, M., Dedova, I. V. et al., Actin binding proteins: regulation of cytoskeletal microfilaments. Physiol. Rev. 2003, 83, 433-473.
    • (2003) Physiol. Rev , vol.83 , pp. 433-473
    • dos Remedios, C.G.1    Chhabra, D.2    Kekic, M.3    Dedova, I.V.4
  • 28
    • 35748959354 scopus 로고    scopus 로고
    • Actin cytoskeleton architecture and signaling in osmosensing
    • Papakonstanti, E. A., Stournaras, C., Actin cytoskeleton architecture and signaling in osmosensing. Methods Enzymol. 2007, 428, 227-240.
    • (2007) Methods Enzymol , vol.428 , pp. 227-240
    • Papakonstanti, E.A.1    Stournaras, C.2
  • 29
    • 63249097106 scopus 로고    scopus 로고
    • Efficient removal of DNA from proteomic samples prior to two-dimensional map analysis
    • Antonioli, P., Bachi, A., Fasoli, E., Righetti, P. G., Efficient removal of DNA from proteomic samples prior to two-dimensional map analysis. J. Chromatogr. A 2009, 24, 3606-3612.
    • (2009) J. Chromatogr. A , vol.24 , pp. 3606-3612
    • Antonioli, P.1    Bachi, A.2    Fasoli, E.3    Righetti, P.G.4


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