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Volumn 3, Issue 5, 2004, Pages 921-929

Proteomics and leukocytes: An approach to understanding potential molecular mechanisms of inflammatory responses

Author keywords

Human; Inflammation; Leukocytes; Organ injury; Proteans profiles; Proteomics

Indexed keywords

ANNEXIN; CALGRANULIN; CELL ADHESION MOLECULE; CELL PROTEIN; CHITOTRIOSIDASE; GLYCOPROTEIN GP 39; IMMUNOSUPPRESSIVE AGENT; IONOMYCIN; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE P38; RAPAMYCIN; RECEPTOR; UNCLASSIFIED DRUG;

EID: 7044223154     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr0499601     Document Type: Review
Times cited : (29)

References (91)
  • 1
    • 0029980760 scopus 로고    scopus 로고
    • MODS/SIRS: Result of an overwhelming inflammatory response?
    • Goris, R. J. MODS/SIRS: result of an overwhelming inflammatory response? World J. Surg. 1996, 20, 418-421.
    • (1996) World J. Surg. , vol.20 , pp. 418-421
    • Goris, R.J.1
  • 2
    • 0142179163 scopus 로고    scopus 로고
    • The epidemiology of severe sepsis syndrome and its treatment with recombinant human activated protein
    • Doig, C. J.; Laupland, K. B.; Zygun, D. A.; Manns, B. J. The epidemiology of severe sepsis syndrome and its treatment with recombinant human activated protein. C. Expert Opin. Pharmacother. 2003, 4, 1789-1799.
    • (2003) C. Expert Opin. Pharmacother. , vol.4 , pp. 1789-1799
    • Doig, C.J.1    Laupland, K.B.2    Zygun, D.A.3    Manns, B.J.4
  • 3
    • 0033590515 scopus 로고    scopus 로고
    • Treating patients with severe sepsis
    • Wheeler, A. P.; Bernard, G. R. Treating patients with severe sepsis. N. Engl. J. Med. 1999, 340, 207-214.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 207-214
    • Wheeler, A.P.1    Bernard, G.R.2
  • 4
    • 0034913320 scopus 로고    scopus 로고
    • Immunodepression in sepsis and SIRS assessed by ex vivo cytokine production is not a generalized phenomenon: A review
    • Cavaillon, J. M.; Adib-Conquy, M.; Cloez-Tayarani, I.; Fitting, C. Immunodepression in sepsis and SIRS assessed by ex vivo cytokine production is not a generalized phenomenon: a review. J. Endotoxin. Res. 2001, 7, 85-93.
    • (2001) J. Endotoxin. Res. , vol.7 , pp. 85-93
    • Cavaillon, J.M.1    Adib-Conquy, M.2    Cloez-Tayarani, I.3    Fitting, C.4
  • 5
    • 0042196164 scopus 로고    scopus 로고
    • Science review: Cell membrane expression (connectivity) regulates neutrophil delivery, function and clearance
    • Seely, A. J.; Pascual, J. L.; Christou, N. V. Science review: Cell membrane expression (connectivity) regulates neutrophil delivery, function and clearance. Crit. Care 2003, 7, 291-307.
    • (2003) Crit. Care , vol.7 , pp. 291-307
    • Seely, A.J.1    Pascual, J.L.2    Christou, N.V.3
  • 6
    • 0038405020 scopus 로고    scopus 로고
    • Understanding exocytosis in immune and inflammatory cells: The molecular basis of mediator secretion
    • Logan, M. R.; Odemuyiwa, S. O.; Moqbel, R. Understanding exocytosis in immune and inflammatory cells: the molecular basis of mediator secretion. J. Allergy Clin. Immunol. 2003, 111, 923-933.
    • (2003) J. Allergy Clin. Immunol. , vol.111 , pp. 923-933
    • Logan, M.R.1    Odemuyiwa, S.O.2    Moqbel, R.3
  • 7
    • 0037829843 scopus 로고    scopus 로고
    • Oxidative stress promotes blood cell-endothelial cell interactions in the microcirculation
    • Cooper, D.; Stokes, K. Y.; Tailor, A.; Granger, D. N. Oxidative stress promotes blood cell-endothelial cell interactions in the microcirculation. Cardiovasc. Toxicol. 2002, 2, 165-180.
    • (2002) Cardiovasc. Toxicol. , vol.2 , pp. 165-180
    • Cooper, D.1    Stokes, K.Y.2    Tailor, A.3    Granger, D.N.4
  • 8
    • 0037460126 scopus 로고    scopus 로고
    • The role of innate cytokines in inflammatory response
    • Liew, F. Y. The role of innate cytokines in inflammatory response. Immunol. Lett. 2003, 85, 131-134.
    • (2003) Immunol. Lett. , vol.85 , pp. 131-134
    • Liew, F.Y.1
  • 9
    • 0037300378 scopus 로고    scopus 로고
    • Chemokines: Attractive mediators of the immune response
    • Wong, M. M.; Fish, E. N. Chemokines: attractive mediators of the immune response. Semin. Immunol. 2003, 15, 5-14.
    • (2003) Semin. Immunol. , vol.15 , pp. 5-14
    • Wong, M.M.1    Fish, E.N.2
  • 10
    • 0344875464 scopus 로고    scopus 로고
    • Cytokines, Chemokines, and cell adhesion molecules in inflammatory myopathies
    • Figarella-Branger, D.; Civatte, M.; Bartoli, C.; Pellissier, J. F. Cytokines, Chemokines, and cell adhesion molecules in inflammatory myopathies. Muscle Nerve 2003, 28, 659-682.
    • (2003) Muscle Nerve , vol.28 , pp. 659-682
    • Figarella-Branger, D.1    Civatte, M.2    Bartoli, C.3    Pellissier, J.F.4
  • 11
    • 0037280317 scopus 로고    scopus 로고
    • Novel mechanistic concepts for the control of leukocyte transmigration: Specialization of integrins, chemokines, and junctional molecules
    • Weber, C. Novel mechanistic concepts for the control of leukocyte transmigration: specialization of integrins, chemokines, and junctional molecules. J. Mol. Med. 2003, 81, 4-19.
    • (2003) J. Mol. Med. , vol.81 , pp. 4-19
    • Weber, C.1
  • 15
    • 0037251105 scopus 로고    scopus 로고
    • Proteomics and systems biology approaches to signal transduction in sepsis
    • Nguyen, A.; Yaffe, M. B. Proteomics and systems biology approaches to signal transduction in sepsis. Crit. Care Med. 2003, 31, S1-6.
    • (2003) Crit. Care Med. , vol.31
    • Nguyen, A.1    Yaffe, M.B.2
  • 16
    • 0033832306 scopus 로고    scopus 로고
    • Neutrophil migration mechanisms, with an emphasis on the pulmonary vasculature
    • Wagner, J. G.; Roth, R. A. Neutrophil migration mechanisms, with an emphasis on the pulmonary vasculature. Pharmacol. Rev. 2000, 52, 349-374.
    • (2000) Pharmacol. Rev. , vol.52 , pp. 349-374
    • Wagner, J.G.1    Roth, R.A.2
  • 17
    • 0033373335 scopus 로고    scopus 로고
    • Targeted gene disruption demonstrates that P-selectin glycoprotein ligand 1 (PSGL-1) is required for P-selectin-mediated but not E-selectin-mediated neutrophil rolling and migration
    • Yang, J.; Hirata, T.; Croce, K.; Merrill-Skoloff, G.; Tchernychev, B.; Williams, E.; Flaumenhaft, R.; Furie, B. C.; Furie, B. Targeted gene disruption demonstrates that P-selectin glycoprotein ligand 1 (PSGL-1) is required for P-selectin-mediated but not E-selectin-mediated neutrophil rolling and migration. J. Exp. Med. 1999, 190, 1769-1782.
    • (1999) J. Exp. Med. , vol.190 , pp. 1769-1782
    • Yang, J.1    Hirata, T.2    Croce, K.3    Merrill-Skoloff, G.4    Tchernychev, B.5    Williams, E.6    Flaumenhaft, R.7    Furie, B.C.8    Furie, B.9
  • 18
    • 0036931691 scopus 로고    scopus 로고
    • Acute pancreatitis-associated lung injury: Pathophysiological mechanisms and potential future therapies
    • Zhao, X.; Andersson, R.; Wang, X.; Dib, M.; Wang, X. D. Acute pancreatitis-associated lung injury: pathophysiological mechanisms and potential future therapies. Scand. J. Gastroenterol. 2002, 37, 1351-1358.
    • (2002) Scand. J. Gastroenterol. , vol.37 , pp. 1351-1358
    • Zhao, X.1    Andersson, R.2    Wang, X.3    Dib, M.4    Wang, X.D.5
  • 19
    • 0027253760 scopus 로고
    • The chemical structure of bacterial endotoxin in relation to bioactivity
    • Rietschel, E. T.; Kirikae, T.; Schade, U. F.; Ulmer, A. J.; Holst, O.; Brade, H., et al. The chemical structure of bacterial endotoxin in relation to bioactivity. Immunobiol. 1993, 187, 169-190.
    • (1993) Immunobiol. , vol.187 , pp. 169-190
    • Rietschel, E.T.1    Kirikae, T.2    Schade, U.F.3    Ulmer, A.J.4    Holst, O.5    Brade, H.6
  • 20
    • 0033034660 scopus 로고    scopus 로고
    • Bacterial endotoxin is an active component of cigarette smoke
    • Hasday, J. D.; Bascom, R.; Costa, J. J.; Fitzgerald, T.; Dubin, W. Bacterial endotoxin is an active component of cigarette smoke. Chest 1999, 115, 829-835.
    • (1999) Chest , vol.115 , pp. 829-835
    • Hasday, J.D.1    Bascom, R.2    Costa, J.J.3    Fitzgerald, T.4    Dubin, W.5
  • 21
    • 0033861419 scopus 로고    scopus 로고
    • The interleukin-1 receptor/Toll-like receptor superfamily: Signal generators for pro-inflammatory interleukins and microbial products
    • Bowie, A.; O'Neill, L. A. The interleukin-1 receptor/Toll-like receptor superfamily: signal generators for pro-inflammatory interleukins and microbial products. J. Leukoc. Biol. 2000, 67, 508-514.
    • (2000) J. Leukoc. Biol. , vol.67 , pp. 508-514
    • Bowie, A.1    O'Neill, L.A.2
  • 22
    • 0033844166 scopus 로고    scopus 로고
    • Toll-like receptors: A growing family of immune receptors that are differentially expressed and regulated by different leukocytes
    • Muzio, M.; Polentarutti, N.; Bosisio, D.; Prahladan, M. K.; Mantovani, A. Toll-like receptors: a growing family of immune receptors that are differentially expressed and regulated by different leukocytes. J. Leukoc. Biol. 2000, 67, 450-456.
    • (2000) J. Leukoc. Biol. , vol.67 , pp. 450-456
    • Muzio, M.1    Polentarutti, N.2    Bosisio, D.3    Prahladan, M.K.4    Mantovani, A.5
  • 24
    • 0037200031 scopus 로고    scopus 로고
    • A genomic and proteomic analysis of activation of the human neutrophil by lipopolysaccharide and its mediation by p38 mitogen-activated protein kinase
    • Fessier, M. B.; Malcolm, K. C.; Duncan, M. W.; Worthen, G. S. A genomic and proteomic analysis of activation of the human neutrophil by lipopolysaccharide and its mediation by p38 mitogen-activated protein kinase. J Biol Chem 2002, 277, 31 291-31 302.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31291-31302
    • Fessier, M.B.1    Malcolm, K.C.2    Duncan, M.W.3    Worthen, G.S.4
  • 25
    • 0036126413 scopus 로고    scopus 로고
    • Lipopolysaccharide stimulation of the human neutrophil: An analysis of changes in gene transcription and protein expression by oligonucleotide microarrays and proteomics
    • Fessler, M. B.; Malcolm, K. C.; Duncan, M. W.; Worthen, G. S. Lipopolysaccharide stimulation of the human neutrophil: an analysis of changes in gene transcription and protein expression by oligonucleotide microarrays and proteomics. Chest 2002; 121: 75S-76S.
    • (2002) Chest , vol.121
    • Fessler, M.B.1    Malcolm, K.C.2    Duncan, M.W.3    Worthen, G.S.4
  • 26
    • 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.; Huttenlocher, A. Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J. Biol. Chem. 2001, 276, 48 382-48 388.
    • (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
  • 27
    • 0027174208 scopus 로고
    • Control of exocytosis in early neutrophil activation
    • Sengelov, H.; Kjeldsen, L.; Borregaard, N. Control of exocytosis in early neutrophil activation. J. Immunol. 1993, 150, 1535-1543.
    • (1993) J. Immunol. , vol.150 , pp. 1535-1543
    • Sengelov, H.1    Kjeldsen, L.2    Borregaard, N.3
  • 28
    • 0033998727 scopus 로고    scopus 로고
    • Calcium-dependent secretion in human neutrophils: A proteomic approach
    • Boussac, M.; Garin, J. Calcium-dependent secretion in human neutrophils: a proteomic approach. Electrophoresis 2000, 21, 665-672.
    • (2000) Electrophoresis , vol.21 , pp. 665-672
    • Boussac, M.1    Garin, J.2
  • 29
    • 0034660481 scopus 로고    scopus 로고
    • Differential mitogen-activated protein kinase stimulation by Fc gamma receptor IIa and Fc gamma receptor IIIb determines the activation phenotype of human neutrophils
    • Coxon, P. Y.; Rane, M. J.; Powell, D. W.; Klein, J. B.; McLeish, K. R. Differential mitogen-activated protein kinase stimulation by Fc gamma receptor IIa and Fc gamma receptor IIIb determines the activation phenotype of human neutrophils. J. Immunol. 2000, 164, 6530-6537.
    • (2000) J. Immunol. , vol.164 , pp. 6530-6537
    • Coxon, P.Y.1    Rane, M.J.2    Powell, D.W.3    Klein, J.B.4    McLeish, K.R.5
  • 30
    • 0034711296 scopus 로고    scopus 로고
    • Priming of the neutrophil respiratory burst involves p38 mitogen-activated protein kinase-dependent exocytosis of flavocytochrome b558-containing granules
    • Ward, R. A.; Nakamura, M.; McLeish, K. R. Priming of the neutrophil respiratory burst involves p38 mitogen-activated protein kinase-dependent exocytosis of flavocytochrome b558-containing granules. J. Biol. Chem. 2000, 275, 36 713-36 719.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36713-36719
    • Ward, R.A.1    Nakamura, M.2    McLeish, K.R.3
  • 33
    • 0029890991 scopus 로고    scopus 로고
    • Activation of MAP kinase-activated protein kinase 2 in human neutrophils after phorbol ester or fMLP peptide stimulation
    • Zu, Y. L.; Ai, Y.; Gilchrist, A.; Labadia, M. E.; Sha'afi, R. I.; Huang, C. K. Activation of MAP kinase-activated protein kinase 2 in human neutrophils after phorbol ester or fMLP peptide stimulation. Blood 1996, 87, 5287-5296.
    • (1996) Blood , vol.87 , pp. 5287-5296
    • Zu, Y.L.1    Ai, Y.2    Gilchrist, A.3    Labadia, M.E.4    Sha'afi, R.I.5    Huang, C.K.6
  • 34
    • 0141741538 scopus 로고    scopus 로고
    • MAPK-activated protein kinase-2 participates in p38 MAPK-dependent and ERK-dependent functions in human neutrophils
    • Coxon, P. Y.; Rane, M. J.; Uriarte, S.; Powell, D. W.; Singh, S.; Butt, W.; Chen, Q.; McLeish, K. R. MAPK-activated protein kinase-2 participates in p38 MAPK-dependent and ERK-dependent functions in human neutrophils. Cell Signal 2003, 15, 993-1001.
    • (2003) Cell Signal , vol.15 , pp. 993-1001
    • Coxon, P.Y.1    Rane, M.J.2    Uriarte, S.3    Powell, D.W.4    Singh, S.5    Butt, W.6    Chen, Q.7    McLeish, K.R.8
  • 35
    • 0141480959 scopus 로고    scopus 로고
    • Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis
    • Singh, S.; Powell, D. W.; Rane, M. J.; Millard, T. H.; Trent, J. O. Pierce, W. M.; Klein, J. B.; Machesky, L. M.; McLeish, K. R. Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis. J. Biol. Chem. 2003, 278, 36 410-36 417.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36410-36417
    • Singh, S.1    Powell, D.W.2    Rane, M.J.3    Millard, T.H.4    Trent, J.O.5    Pierce, W.M.6    Klein, J.B.7    Machesky, L.M.8    McLeish, K.R.9
  • 36
    • 0032512546 scopus 로고    scopus 로고
    • MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase
    • Ni, H.; Wang, X. S.; Diener, K.; Yao, Z. MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase. Biochem. Biophys. Res. Commun. 1998, 243, 492-496.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 492-496
    • Ni, H.1    Wang, X.S.2    Diener, K.3    Yao, Z.4
  • 37
    • 0037044735 scopus 로고    scopus 로고
    • Cytoskeletal changes in hypoxic pulmonary endothelial cells are dependent on MAPK-activated protein kinase MK2
    • Kayyali, U. S.; Pennella, C. M.; Trujillo, C.; Villa, O.; Gaestel, M.; Hassoun, P. M. Cytoskeletal changes in hypoxic pulmonary endothelial cells are dependent on MAPK-activated protein kinase MK2. J. Biol. Chem. 2002, 277, 42 596-42 602.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42596-42602
    • Kayyali, U.S.1    Pennella, C.M.2    Trujillo, C.3    Villa, O.4    Gaestel, M.5    Hassoun, P.M.6
  • 38
    • 0032789927 scopus 로고    scopus 로고
    • The polarization of the motile cell
    • Nabi, I. R. The polarization of the motile cell. J. Cell. Sci. 1999, 112, 1803-1811.
    • (1999) J. Cell. Sci. , vol.112 , pp. 1803-1811
    • Nabi, I.R.1
  • 39
    • 0033755860 scopus 로고    scopus 로고
    • Cellular signaling in macrophage migration and chemotaxis
    • Jones, G. E. Cellular signaling in macrophage migration and chemotaxis. J. Leukoc. Biol. 2000, 68, 593-602.
    • (2000) J. Leukoc. Biol. , vol.68 , pp. 593-602
    • Jones, G.E.1
  • 40
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues
    • Bennett, V.; Baines, A. J. Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol. Rev. 2001, 81, 1353-1392.
    • (2001) Physiol. Rev. , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 41
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic Analysis of a Detergent-resistant Membrane Skeleton from Neutrophil Plasma Membranes
    • Nebl, T.; Pestonjamasp, K. N.; Leszyk, J. D.; Crowley, J. L.; Oh, S. W.; Luna, E. J. Proteomic Analysis of a Detergent-resistant Membrane Skeleton from Neutrophil Plasma Membranes. J. Biol. Chem. 2002, 277, 43 399-43 409.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43399-43409
    • Nebl, T.1    Pestonjamasp, K.N.2    Leszyk, J.D.3    Crowley, J.L.4    Oh, S.W.5    Luna, E.J.6
  • 42
    • 0036180136 scopus 로고    scopus 로고
    • Proteome analysis of rat polymorphonuclear leukocytes: A two-dimensional electrophoresis/mass spectrometry approach
    • Piubelli, C.; Galvani, M.; Hamdan, M.; Domenici, E.; Righetti, P. G. Proteome analysis of rat polymorphonuclear leukocytes: a two-dimensional electrophoresis/mass spectrometry approach. Electrophoresis 2002, 23, 298-310.
    • (2002) Electrophoresis , vol.23 , pp. 298-310
    • Piubelli, C.1    Galvani, M.2    Hamdan, M.3    Domenici, E.4    Righetti, P.G.5
  • 44
    • 0036839597 scopus 로고    scopus 로고
    • Genomic and proteomic analysis of the myeloid differentiation program: Global analysis of gene expression during induced differentiation in the MPRO cell line
    • Lian, Z.; Kluger, Y.; Greenbaum, D. S.; Tuck, D.; Gerstein, M.; Berliner, N.; Weissman, S. M.; Newburger, P. E. Genomic and proteomic analysis of the myeloid differentiation program: global analysis of gene expression during induced differentiation in the MPRO cell line. Blood 2002, 100, 3209-3220.
    • (2002) Blood , vol.100 , pp. 3209-3220
    • Lian, Z.1    Kluger, Y.2    Greenbaum, D.S.3    Tuck, D.4    Gerstein, M.5    Berliner, N.6    Weissman, S.M.7    Newburger, P.E.8
  • 46
    • 0032849641 scopus 로고    scopus 로고
    • Dendritic cells: Expansion and differentiation with hematopoietic growth factors
    • Young, J. W. Dendritic cells: expansion and differentiation with hematopoietic growth factors. Curr. Opin. Hematol. 1999, 6, 135-144.
    • (1999) Curr. Opin. Hematol. , vol.6 , pp. 135-144
    • Young, J.W.1
  • 47
    • 0035947669 scopus 로고    scopus 로고
    • Profiling changes in gene expression during differentiation and maturation of monocyte-derived dendritic cells using both oligonucleotide microarrays and proteomics
    • Le Naour, F.; Hohenkirk, L.; Grolleau, A.; Misek, D. E.; Lescure, P.; Geiger, J. D.; Hanash, S.; Beretta, L. Profiling changes in gene expression during differentiation and maturation of monocyte-derived dendritic cells using both oligonucleotide microarrays and proteomics. J. Biol. Chem. 2001, 276, 17 920-17 931.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17920-17931
    • Le Naour, F.1    Hohenkirk, L.2    Grolleau, A.3    Misek, D.E.4    Lescure, P.5    Geiger, J.D.6    Hanash, S.7    Beretta, L.8
  • 48
    • 0036960169 scopus 로고    scopus 로고
    • Integrated genomic and proteomic analysis of signaling pathways in dendritic cell differentiation and maturation
    • Richards, J.; Le Naour, F.; Hanash, S.; Beretta, L. Integrated genomic and proteomic analysis of signaling pathways in dendritic cell differentiation and maturation. Ann. N.Y. Acad. Sci. 2002, 975, 91-100.
    • (2002) Ann. N.Y. Acad. Sci. , vol.975 , pp. 91-100
    • Richards, J.1    Le Naour, F.2    Hanash, S.3    Beretta, L.4
  • 50
    • 0033179274 scopus 로고    scopus 로고
    • Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake
    • Todryk, S.; Melcher, A. A.; Hardwick, N.; Linardakis, E.; Bateman, A.; Colombo, M. P.; Stoppacciaro, A.; Vile, R. G. Heat shock protein 70 induced during tumor cell killing induces Th1 cytokines and targets immature dendritic cell precursors to enhance antigen uptake. J. Immunol. 1999, 163, 1398-1408.
    • (1999) J. Immunol. , vol.163 , pp. 1398-1408
    • Todryk, S.1    Melcher, A.A.2    Hardwick, N.3    Linardakis, E.4    Bateman, A.5    Colombo, M.P.6    Stoppacciaro, A.7    Vile, R.G.8
  • 51
    • 0030041936 scopus 로고    scopus 로고
    • Heat shock proteins increase resistance to apoptosis
    • Samali, A.; Cotter, T. G. Heat shock proteins increase resistance to apoptosis. Exp. Cell. Res. 1996, 223, 163-170.
    • (1996) Exp. Cell. Res. , vol.223 , pp. 163-170
    • Samali, A.1    Cotter, T.G.2
  • 52
    • 0034734639 scopus 로고    scopus 로고
    • Treatment of solid tumours in children with tumour-lysate-pulsed dendritic cells
    • Geiger, J.; Hutchinson, R.; Hohenkirk, L.; McKenna, E.; Chang, A. Mule J. Treatment of solid tumours in children with tumour-lysate-pulsed dendritic cells. Lancet 2000, 356, 1163-1165.
    • (2000) Lancet , vol.356 , pp. 1163-1165
    • Geiger, J.1    Hutchinson, R.2    Hohenkirk, L.3    McKenna, E.4    Chang, A.5    Mule, J.6
  • 53
    • 0034733807 scopus 로고    scopus 로고
    • Redox-dependent signal transduction
    • Finkel, T. Redox-dependent signal transduction. FBBS Lett. 2000, 476, 52-54.
    • (2000) FBBS Lett. , vol.476 , pp. 52-54
    • Finkel, T.1
  • 54
    • 0036829699 scopus 로고    scopus 로고
    • Oxidative stress in septic shock and disseminated intravascular coagulation
    • Salvemini, D.; Cuzzocrea, S. Oxidative stress in septic shock and disseminated intravascular coagulation. Free Radical Biol. Med. 2002, 33, 1173-1185.
    • (2002) Free Radical Biol. Med. , vol.33 , pp. 1173-1185
    • Salvemini, D.1    Cuzzocrea, S.2
  • 55
  • 56
    • 0037202908 scopus 로고    scopus 로고
    • Proteomic analysis of the cellular proteins induced by adaptive concentrations of hydrogen peroxide in human U937 cells
    • Seong, J. K.; Kim, do K.; Choi, K. H.; Oh, S. H.; Kim, K. S.; Lee, S. S.; Um, H. D. Proteomic analysis of the cellular proteins induced by adaptive concentrations of hydrogen peroxide in human U937 cells. Exp. Mol. Med. 2002, 34, 374-378.
    • (2002) Exp. Mol. Med. , vol.34 , pp. 374-378
    • Seong, J.K.1    Kim Do, K.2    Choi, K.H.3    Oh, S.H.4    Kim, K.S.5    Lee, S.S.6    Um, H.D.7
  • 58
    • 0036668520 scopus 로고    scopus 로고
    • Proteomic analysis of human lysosomes: Application to monocytic and breast cancer cells
    • Journet, A.; Chapel, A.; Kieffer, S.; Roux, F.; Garin, J. Proteomic analysis of human lysosomes: application to monocytic and breast cancer cells. Proteomics 2002, 2, 1026-1040.
    • (2002) Proteomics , vol.2 , pp. 1026-1040
    • Journet, A.1    Chapel, A.2    Kieffer, S.3    Roux, F.4    Garin, J.5
  • 60
    • 32344441627 scopus 로고    scopus 로고
    • Proteomic approaches to the analysis of early events in colony-stimulating factor-1 signal transduction
    • Yeung, Y. G., Stanley, E. R. Proteomic approaches to the analysis of early events in colony-stimulating factor-1 signal transduction. Mol. Cell. Proteomics 2003, 2, 1143-1155.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1143-1155
    • Yeung, Y.G.1    Stanley, E.R.2
  • 61
    • 0036668059 scopus 로고    scopus 로고
    • Biomic study of human myeloid leukemia cells differentiation to macrophages using DNA array, proteomic, and bioinformatic analytical methods
    • Juan, H. F.; Lin, J. Y.; Chang, W. H.; Wu, C. Y.; Pan, T. L.; Tseng, M. J.; Khoo, K. H.; Chen, S. T. Biomic study of human myeloid leukemia cells differentiation to macrophages using DNA array, proteomic, and bioinformatic analytical methods. Electrophoresis 2002, 23, 2490-2504.
    • (2002) Electrophoresis , vol.23 , pp. 2490-2504
    • Juan, H.F.1    Lin, J.Y.2    Chang, W.H.3    Wu, C.Y.4    Pan, T.L.5    Tseng, M.J.6    Khoo, K.H.7    Chen, S.T.8
  • 62
    • 0036204066 scopus 로고    scopus 로고
    • Development of improved cell lysis, solubilization and imaging approaches for proteomic analyses
    • Leimgruber, R. M.; Malone, J. P.; Radabaugh, M. R.; LaPorte, M. L.; Violand, B. N.; Monahan, J. B. Development of improved cell lysis, solubilization and imaging approaches for proteomic analyses. Proteomics 2002, 2, 135-144.
    • (2002) Proteomics , vol.2 , pp. 135-144
    • Leimgruber, R.M.1    Malone, J.P.2    Radabaugh, M.R.3    Laporte, M.L.4    Violand, B.N.5    Monahan, J.B.6
  • 64
    • 0035823537 scopus 로고    scopus 로고
    • Novel intra-and intermolecular sulfinamide bonds in S100A8 produced by hypochlorite oxidation
    • Raftery, M. J.; Yang, Z.; Valenzuela, S. M.; Geczy, C. L. Novel intra-and intermolecular sulfinamide bonds in S100A8 produced by hypochlorite oxidation. J. Biol. Chem. 2001, 276, 33 393-33 401.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33393-33401
    • Raftery, M.J.1    Yang, Z.2    Valenzuela, S.M.3    Geczy, C.L.4
  • 65
    • 0034792227 scopus 로고    scopus 로고
    • Changes in gene expression in macrophages infected with Mycobacterium tuberculosis: A combined transcriptomic and proteomic approach
    • Ragno, S.; Romano, M.; Howell, S.; Pappin, D. J.; Jenner, P. J.; Colston, M. J. Changes in gene expression in macrophages infected with Mycobacterium tuberculosis: a combined transcriptomic and proteomic approach. Immunology 2001, 104, 99-108.
    • (2001) Immunology , vol.104 , pp. 99-108
    • Ragno, S.1    Romano, M.2    Howell, S.3    Pappin, D.J.4    Jenner, P.J.5    Colston, M.J.6
  • 67
    • 0026511987 scopus 로고
    • Environmental signals controlling expression of virulence determinants in bacteria
    • Mekalanos, J. J. Environmental signals controlling expression of virulence determinants in bacteria. J. Bacteriol. 1992, 174, 1-7.
    • (1992) J. Bacteriol. , vol.174 , pp. 1-7
    • Mekalanos, J.J.1
  • 68
    • 0028792234 scopus 로고
    • The role of endothelial cells in the systemic inflammatory response syndrome and multiple system organ failure
    • Wang, X. D.; Andersson, R. The role of endothelial cells in the systemic inflammatory response syndrome and multiple system organ failure. Eur. J. Surg. 1995, 161, 703-713.
    • (1995) Eur. J. Surg. , vol.161 , pp. 703-713
    • Wang, X.D.1    Andersson, R.2
  • 69
    • 0029072762 scopus 로고
    • Flow-mediated endothelial mechanotransduction
    • Davies, P. F. Flow-mediated endothelial mechanotransduction. Physiol. Rev. 1995, 75, 519-560.
    • (1995) Physiol. Rev. , vol.75 , pp. 519-560
    • Davies, P.F.1
  • 71
    • 7044284378 scopus 로고    scopus 로고
    • Potential role reactive oxygen speices in pancreatitis-associated multiple organ dysfunction
    • in press
    • Shi, C. B.; Andersson, R.; Zhao, X.; Wang, X. D. Potential role reactive oxygen speices in pancreatitis-associated multiple organ dysfunction. J Pancreatol. 2004; in press.
    • (2004) J. Pancreatol.
    • Shi, C.B.1    Andersson, R.2    Zhao, X.3    Wang, X.D.4
  • 72
    • 0028791184 scopus 로고
    • Antioxidant and calcium channel blockers counteract endothelial barrier injury induced by acute pancreatitis in rats
    • Wang, X. D.; Deng, X. M.; Haraldsen, P.; Andersson, R.; Ihse, I. Antioxidant and calcium channel blockers counteract endothelial barrier injury induced by acute pancreatitis in rats. Scand. J. Gastroenterol. 1995, 30, 1129-1136.
    • (1995) Scand. J. Gastroenterol. , vol.30 , pp. 1129-1136
    • Wang, X.D.1    Deng, X.M.2    Haraldsen, P.3    Andersson, R.4    Ihse, I.5
  • 74
    • 0037013303 scopus 로고    scopus 로고
    • Rapid phosphorylation of heterogeneous nuclear ribonucleoprotein C1/C2 in response to physiologic levels of hydrogen peroxide in human endothelial cells
    • Stone, J. R.; Collins, T. Rapid phosphorylation of heterogeneous nuclear ribonucleoprotein C1/C2 in response to physiologic levels of hydrogen peroxide in human endothelial cells. J. Biol. Chem. 2002, 277, 15 621-15 628.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15621-15628
    • Stone, J.R.1    Collins, T.2
  • 75
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding
    • Schlondorff, J.; Blobel, C. P. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding. J. Cell. Sci. 1999, 112, 3603-3617.
    • (1999) J. Cell. Sci. , vol.112 , pp. 3603-3617
    • Schlondorff, J.1    Blobel, C.P.2
  • 77
    • 0034009976 scopus 로고    scopus 로고
    • Metalloproteolytic release of endothelial cell protein C receptor
    • Xu, J.; Qu, D.; Esmon, N. L.; Esmon, C. T. Metalloproteolytic release of endothelial cell protein C receptor. J. Biol. Chem. 2000, 275, 6038-6044.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6038-6044
    • Xu, J.1    Qu, D.2    Esmon, N.L.3    Esmon, C.T.4
  • 78
    • 0036857628 scopus 로고    scopus 로고
    • Proteomic analysis of human eosinophil activation mediated by mast cells, granulocyte macrophage colony stimulating factor and tumor necrosis factor alpha
    • Levi-Schaffer, F.; Temkin, V.; Simon, H. U.; Kettman, J. R., Frey, J. R.; Lefkovits, I. Proteomic analysis of human eosinophil activation mediated by mast cells, granulocyte macrophage colony stimulating factor and tumor necrosis factor alpha. Proteomics 2002, 2, 1616-1626.
    • (2002) Proteomics , vol.2 , pp. 1616-1626
    • Levi-Schaffer, F.1    Temkin, V.2    Simon, H.U.3    Kettman, J.R.4    Frey, J.R.5    Lefkovits, I.6
  • 79
    • 0023034808 scopus 로고
    • Recombinant human granulocyte-macrophage colony-stimulating factor stimulates in vitro mature human neutrophil and eosinophil function, surface receptor expression, and survival
    • Lopez, A. F.; Williamson, D. J.; Gamble, J. R.; Begley, C. G.; Harlan, J. M.; Klebanoff, S. J.; Waltersdorph, A.; Wong, G.; Clark S. C.; Vadas, M. A. Recombinant human granulocyte-macrophage colony-stimulating factor stimulates in vitro mature human neutrophil and eosinophil function, surface receptor expression, and survival. J. Clin. Invest. 1986, 78, 1220-1228.
    • (1986) J. Clin. Invest. , vol.78 , pp. 1220-1228
    • Lopez, A.F.1    Williamson, D.J.2    Gamble, J.R.3    Begley, C.G.4    Harlan, J.M.5    Klebanoff, S.J.6    Waltersdorph, A.7    Wong, G.8    Clark, S.C.9    Vadas, M.A.10
  • 80
    • 0035854651 scopus 로고    scopus 로고
    • Proteomic analysis of macrophage differentiation. p46/52(Shc) Tyrosine phosphorylation is required for CSF-1-mediated macrophage differentiation
    • Csar, X. F.; Wilson, N. J.; McMahon, K. A.; Marks, D. C.; Beecroft, T. L.; Ward, A. C.; Whitty, G. A.; Kanangasundarum, V.; Hamilton, J. A. Proteomic analysis of macrophage differentiation. p46/52(Shc) Tyrosine phosphorylation is required for CSF-1-mediated macrophage differentiation. J. Biol. Chem. 2001, 276, 26211-26217.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26211-26217
    • Csar, X.F.1    Wilson, N.J.2    McMahon, K.A.3    Marks, D.C.4    Beecroft, T.L.5    Ward, A.C.6    Whitty, G.A.7    Kanangasundarum, V.8    Hamilton, J.A.9
  • 82
    • 0021139225 scopus 로고
    • Inadequate interleukin 2 production. A fundamental immunological deficiency in patients with major burns
    • Wood, J. J.; Rodrick, M. L.; O'Mahony, J. B.; Palder S. B.,; Saporoschetz, I.' D'Eon, P.; Mannick, J. A. Inadequate interleukin 2 production. A fundamental immunological deficiency in patients with major burns. Ann. Surg. 1984, 200, 311-320.
    • (1984) Ann. Surg. , vol.200 , pp. 311-320
    • Wood, J.J.1    Rodrick, M.L.2    O'Mahony, J.B.3    Palder, S.B.4    Saporoschetz, I.5    D'Eon, P.6    Mannick, J.A.7
  • 84
    • 0034121321 scopus 로고    scopus 로고
    • Proteomic analysis of T cell activation in the presence of cyclosporin A: Immunosuppressor and activator removal induces de novo protein synthesis
    • Truffa-Bachi, P.; Lefkovits, I.; Frey, J. R. Proteomic analysis of T cell activation in the presence of cyclosporin A: immunosuppressor and activator removal induces de novo protein synthesis. Mol. Immunol. 2000, 37, 21-28.
    • (2000) Mol. Immunol. , vol.37 , pp. 21-28
    • Truffa-Bachi, P.1    Lefkovits, I.2    Frey, J.R.3
  • 85
    • 0034721074 scopus 로고    scopus 로고
    • Increased protein synthesis after T cell activation in the presence of cyclosporin A
    • Mascarell, L.; Frey, J. R.; Michel, F.; Lefkovits, I.; Truffa-Bachi, P. Increased protein synthesis after T cell activation in the presence of cyclosporin A. Transplantation 2000, 70, 340-348.
    • (2000) Transplantation , vol.70 , pp. 340-348
    • Mascarell, L.1    Frey, J.R.2    Michel, F.3    Lefkovits, I.4    Truffa-Bachi, P.5
  • 88
    • 0037151120 scopus 로고    scopus 로고
    • Global and specific transtional control by rapamycin in T cells uncovered by microarrays and proteomics
    • Grolleau, A.; Bowman, J.; Pradet-Balade, B.; Puravs, E.; Hanash, S.; Garcia-Sanz, J. A.; Beretta, L. Global and specific transtional control by rapamycin in T cells uncovered by microarrays and proteomics. J. Biol. Chem. 2002, 277, 22 175-22 184.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22175-22184
    • Grolleau, A.1    Bowman, J.2    Pradet-Balade, B.3    Puravs, E.4    Hanash, S.5    Garcia-Sanz, J.A.6    Beretta, L.7
  • 89
    • 0035923582 scopus 로고    scopus 로고
    • Profiling the global tyrosine phosphorylation state by Src homology 2 domain binding
    • Nollau, P.; Mayer, B. J. Profiling the global tyrosine phosphorylation state by Src homology 2 domain binding. PNAS 2001, 98, 13531-13536.
    • (2001) PNAS , vol.98 , pp. 13531-13536
    • Nollau, P.1    Mayer, B.J.2
  • 90
    • 0037349125 scopus 로고    scopus 로고
    • Role of Th2 responses in the development of allergen-induced airway remodelling in a murine model of allergic asthma
    • Komai, M.; Tanaka, H.; Masuda, T.; Nagao, K.; Ishizaki, M.; Sawada, M.; Nagai, H. Role of Th2 responses in the development of allergen-induced airway remodelling in a murine model of allergic asthma. Br. J. Pharmacol. 2003, 138, 912-920.
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 912-920
    • Komai, M.1    Tanaka, H.2    Masuda, T.3    Nagao, K.4    Ishizaki, M.5    Sawada, M.6    Nagai, H.7
  • 91
    • 0034931864 scopus 로고    scopus 로고
    • Fingerprinting of signal transduction pathways using a combination of anti-phosphotyrosine immunoprecipitations and two-dimensional polycrylamide gel electrophoresis
    • Stancato, L. F.; Petricoin, E. F., III Fingerprinting of signal transduction pathways using a combination of anti-phosphotyrosine immunoprecipitations and two-dimensional polycrylamide gel electrophoresis. Electrophoresis 2001, 22, 2120-2124.
    • (2001) Electrophoresis , vol.22 , pp. 2120-2124
    • Stancato, L.F.1    Petricoin III, E.F.2


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