Proteomic Analysis of Human U937 Cell Line Activation Mediated by Haemophilus influenzae Type b P2 Porin and Its Surface-Exposed Loop (535 views)
J Proteome Res (ISSN: 1535-3893), 2010 Feb; 9(2): 1050-1062.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.46, 5-year impact factor: 5.617
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-76149115883&partnerID=40&md5=9187146c8c50952df789f53113e232ac
Keywords: Haemophilus Influenzae Type B, Immune Response, Pathogen-Host Interaction, Porin, Proteomic Profiling, Loop 7 Peptide, P2 Porin, Unclassified Drug, Article, Cell Activation, Cell Strain U937, Controlled Study, Cytoskeleton, Disease Course, Host Pathogen Interaction, Human, Human Cell, Inflammation, Mass Spectrometry, Metabolism, Nucleotide Sequence, Priority Journal, Protein Analysis, Protein Expression, Signal Transduction, Stress, Two Dimensional Electrophoresis, Bacterial Proteins, Blotting, Western, Two-Dimensional, Matrix-Assisted Laser Desorption-Ionization, U937 Cells, Bacteria (microorganisms), Haemophilus Influenzae Serotype B,
Affiliations:
*** IBB - CNR ***
Department of Life Science, Second University of Naples, Via Vivaldi 43, I-81100 Caserta, Italy
Department of Experimental Medicine, Second University of Naples, Via De Crecchio 7, I-80138 Napoli, Italy
Department of Biological Sciences, University of Naples Federico II, Via Mezzocannone 16, I-80134, Napoli, Italy
Institute of Biostructure and Bioimaging, C.N.R., Via Mezzocannone 16, I-80134, Napoli, Italy
Proteomic and Biomolecular Mass Spectrometry Center, Institute of Food Science and Technology, C.N.R., Via Roma 52 A-C, I-83100 Avellino, Italy
References:
Watt, J.P., Wolfson, L.J., O'Brien, K.L., Henkle, E., Deloria-Knoll, M., McCall, N., Lee, E., Cherian, T., Burden of disease caused by Haemophilus influenzae type b in children younger than 5 years: Global estimates (2009) Lancet, 374 (9693), pp. 903-91
Dufrene, Y.F., Using nanotechniques to explore microbial surfaces (2004) Nat. Rev. Microbiol, 2 (6), pp. 451-460
McDonald, P.P., Bald, A., Cassatella, M.A., Activation of the NF-κB pathway by inflammatory stimuli in human neutrophils (1997) Blood, 89 (9), pp. 3421-3433
Cassatella, M.A., The production of cytokines by polymorphonuclear neutrophils (1995) Immunol. Today, 16 (1), pp. 21-26
Fessler, 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 (2002) J. Biol. Chem, 277 (35), pp. 31291-31302
Gadgil, H.S., Pabst, K.M., Giorgianni, F., Umstot, E.S., Desiderio, D.M., Beranova-Giorgianni, S., Gerling, I.C., Pabst, M.J., Proteome of monocytes primed with lipopolysaccharide: Analysis of the abundant proteins (2003) Proteomics, 3 (9), pp. 1767-1780
Zhang, X., Kuramitsu, Y., Fujimoto, M., Hayashi, E., Yuan, X., Nakamura, K., Proteomic analysis of macrophages stimulated by lipopolysaccharide: Lipopolysaccharide inhibits the cleavage of nucleophosmin (2006) Electrophoresis, 27 (8), pp. 1659-1668
Achouak, W., Heulin, T., Pages, J.M., Multiple facets of bacterial porins (2001) FEMS Microbiol. Lett, 199 (1), pp. 1-7
Galdiero, F., de L'ero, G.C., Benedetto, N., Galdiero, M., Tufano, M.A., Release of cytokines induced by Salmonella typhimurium porins (1993) Infect. Immun, 61 (1), pp. 155-161
Galdiero, M., Cipollaro de L'ero, G., Donnarumma, G., Marcatili, A., Galdiero, F., Interleukin-1 and interleukin-6 gene expression in human monocytes stimulated with Salmonella typhimurium porins (1995) Immunology, 86 (4), pp. 612-619
Galdiero, M., Vitiello, M., Galdiero, S., Eukaryotic cell signaling and transcriptional activation induced by bacterial porins (2003) FEMS Microbiol. Lett, 226 (1), pp. 57-64
Galdiero, M., D'Isanto, M., Vitiello, M., Finamore, E., Peluso, L., Galdiero, M., Monocytic activation of protein tyrosine kinase, protein kinase A and protein kinase C induced by porins isolated from Salmonella enterica serovar Typhimurium (2003) J. Infect, 46 (2), pp. 111-119
Galdiero, M., Tortora, A., Damiano, N., Vitiello, M., Longanella, A., Galdiero, E., Induction of cytokine mRNA expression in U937 cells by Salmonella typhimurium porins is regulated by different phosphorylation pathways (2005) Med. Microbiol. Immunol, 194 (1-2), pp. 13-23
Galdiero, M., D'Amico, M., Gorga, F., Di Filippo, C., D'Isanto, M., Vitiello, M., Longanella, A., Tortora, A., Haemophilus influenzae porin contributes to signaling of the inflammatory cascade in rat brain (2001) Infect. Immun, 69 (1), pp. 221-227
Galdiero, S., Capasso, D., Vitiello, M., D'Isanto, M., Pedone, C., Galdiero, M., Role of surface-exposed loops of Haemophilus influenzae protein P2 in the mitogen-activated protein kinase cascade (2003) Infect. Immun, 71 (5), pp. 2798-2809
Galdiero, S., Vitiello, M., Amodeo, P., D'Isanto, M., Cantisani, M., Pedone, C., Galdiero, M., Structural requirements for proinflammatory activity of porin P2 Loop 7 from Haemophilus influenzae (2006) Biochemistry, 45 (14), pp. 4491-4501
Coulton, J.W., Wan, D.T., The outer membrane of Haemophilus influenzae type b: Cell envelope associations of major proteins (1983) Can. J. Microbiol, 29 (2), pp. 280-287
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., Protein measurement with the Folin phenol reagent (1951) J. Biol. Chem, 193 (1), pp. 265-275
Yin, E.T., Galanos, C., Kinsky, S., Bradshaw, R.A., Wessler, S., Luderitz, O., Sarmiento, M.E., Picogram-sensitive assay for endotoxin: Gelation of Limulus polyphemus blood cell lysate induced by purified lipopolysaccharides and lipid A from Gram-negative bacteria (1972) Biochim. Biophys. Acta, 261 (1), pp. 284-289
Nikaido, H., Rosenberg, E.Y., Porin channels in Escherichia coli: Studies with liposomes reconstituted from purified proteins (1983) J. Bacteriol, 153 (1), pp. 241-252
Galanos, C., Luderitz, O., Westphal, O., A new method for the extraction of R lipopolysaccharides (1969) Eur. J. Biochem, 9 (2), pp. 245-249
Chambery, A., Farina, A., Di Maro, A., Rossi, M., Abbondanza, C., Moncharmont, B., Malorni, L., Parente, A., Proteomic analysis of MCF-7 cell lines expressing the zinc-finger or the proline-rich domain of retinoblastoma-interacting-zinc-finger protein (2006) J. Proteome Res, 5 (5), pp. 1176-1185
Zhang, B., Kirov, S., Snoddy, J., WebGestalt: An integrated system for exploring gene sets in various biological contexts (2005) Nucleic Acids Res, 33. , Web Server issue, W741-8
Mendelsohn, B.A., Malone, J.P., Townsend, R., Gitlin, J., Proteomic analysis of anoxia tolerance in the developing zebrafish embryo (2009) Comp. Biochem. Physiol., Part D, 4 (1), pp. 21-31
Tsan, M.F., Gao, B., Cytokine function of heat shock proteins (2004) Am. J. Physiol.: Cell Physiol, 286 (4), pp. C739-C744
Jaattela, M., Heat shock proteins as cellular lifeguards (1999) Ann. Med, 31 (4), pp. 261-271
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Engel, K., Ahlers, A., Brach, M.A., Herrmann, F., Gaestel, M., MAPKAP kinase 2 is activated by heat shock and TNF-alpha: In vivo phosphorylation of small heat shock protein results from stimulation of the MAP kinase cascade (1995) J. Cell Biochem, 57 (2), pp. 321-330
Jaattela, M., Wissing, D., Heat-shock proteins protect cells from monocyte cytotoxicity: Possible mechanism of self-protection (1993) J. Exp. Med, 177 (1), pp. 231-236
Haddad, J.J., Land, S.C., Redox/ROS regulation of lipopolysaccharide- induced mitogen-activated protein kinase (MAPK) activation and MAPK-mediated TNF-alpha biosynthesis (2002) Br. J. Pharmacol, 135 (2), pp. 520-536
Lavoie, J.N., Hickey, E., Weber, L.A., Landry, J., Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27 (1993) J. Biol. Chem, 268 (32), pp. 24210-24214
Sancho, D., Vicente-Manzanares, M., Mittelbrunn, M., Montoya, M.C., Gordon-Alonso, M., Serrador, J.M., Sanchez-Madrid, F., Regulation of microtubule-organizing center orientation and actomyosin cytoskeleton rearrangement during immune interactions (2002) Immunol. Rev, 189, pp. 84-97
Yin, H.L., Hartwig, J.H., The structure of the macrophage actin skeleton (1988) J. Cell Sci. Suppl, 9, pp. 169-184
Eswarappa, S.M., Pareek, V., Chakravortty, D., Role of actin cytoskeleton in LPS-induced NF-kappaB activation and nitric oxide production in murine macrophages (2008) Innate Immun, 14 (5), pp. 309-318
De Martino, L., Nazzaro, C., Concilio, S., Galdiero, M., Morphological changes induced in HEp-2 cells by Salmonella typhimurium porins (1995) J. Submicrosc. Cytol. Pathol, 27 (4), pp. 445-449
Galdiero, M., Palomba, E., De, L., Vitiello, M., Pagnini, P., Effects of the major Pasteurella multocida porin on bovine neutrophils (1998) Am. J. Vet. Res, 59 (10), pp. 1270-1274
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Vabulas, R.M., Ahmad-Nejad, P., da Costa, C., Miethke, T., Kirschning, C.J., Hacker, H., Wagner, H., Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells (2001) J. Biol. Chem, 276 (33), pp. 31332-31339
Cohen-Sfady, M., Nussbaum, G., Pevsner-Fischer, M., Mor, F., Carmi, P., Zanin-Zhorov, A., Lider, O., Cohen, I.R., Heat shock protein 60 activates B cells via the TLR4-MyD88 pathway (2005) J. Immunol, 175 (6), pp. 3594-3602
Kim, Y.S., Koh, J.M., Lee, Y.S., Kim, B.J., Lee, S.H., Lee, K.U., Kim, G.S., Increased circulating heat shock protein 60 induced by menopause, stimulates apoptosis of osteoblast-lineage cells via upregulation of toll-like receptors (2009) Bone, 45 (1), pp. 68-76
Zhao, Y., Yokota, K., Ayada, K., Yamamoto, Y., Okada, T., Shen, L., Oguma, K., Helicobacter pylori heat-shock protein 60 induces interleukin-8 via a Toll-like receptor (TLR)2 and mitogen-activated protein (MAP) kinase pathway in human monocytes (2007) J. Med. Microbiol, 56 (2), pp. 154-164
Habich, C., Kempe, K., van der Zee, R., Rumenapf, R., Akiyama, H., Kolb, H., Burkart, V., Heat shock protein 60: Specific binding of lipopolysaccharide (2005) J. Immunol, 174 (3), pp. 1298-1305
Zhou, M., Jacob, A., Ho, N., Miksa, M., Wu, R., Maitra, S.R., Wang, P., Downregulation of protein disulfide isomerase in sepsis and its role in tumor necrosis factor-alpha release (2008) Crit. Care, 12 (4), pp. R100
Ghebrehiwet, B., Peerschke, E.I., cC1q-R (calreticulin) and gC1q-R/p33: Ubiquitously expressed multi-ligand binding cellular proteins involved in inflammation and infection (2004) Mol. Immunol, 41 (2-3), pp. 173-183
Vertessy, B.G., Toth, J., Keeping uracil out of DNA: Physiological role, structure and catalytic mechanism of dUTPases (2009) Acc. Chem. Res, 42 (1), pp. 97-106
Sire, J., Querat, G., Esnault, C., Priet, S., Uracil within DNA: An actor of antiviral immunity (2008) Retrovirology, 5, p. 45
Ariza, M.E., Glaser, R., Kaumaya, P.T., Jones, C., Williams, M.V., The EBV-encoded dUTPase activates NF-kappa B through the TLR2 and MyD88-dependent signaling pathway (2009) J. Immunol, 182 (2), pp. 851-859
Glaser, R., Padgett, D.A., Litsky, M.L., Baiocchi, R.A., Yang, E.V., Chen, M., Yeh, P.E., Williams, M.V., Stress-associated changes in the steady-state expression of latent Epstein-Barr virus: Implications for chronic fatigue syndrome and cancer (2005) Brain Behav. Immun, 19 (2), pp. 91-103
Waldman, W.J., Williams Jr., M.V., Lemeshow, S., Binkley, P., Guttridge, D., Kiecolt-Glaser, J.K., Knight, D.A., Glaser, R., Epstein-Barr virus-encoded dUTPase enhances proin-flammatory cytokine production by macrophages in contact with endothelial cells: Evidence for depression-induced atherosclerotic risk (2008) Brain Behav. Immun, 22 (2), pp. 215-223
Jung, H., Seong, H.A., Ha, H., Direct interaction between NM23-H1 and macrophage migration inhibitory factor (MIF) is critical for alleviation of MIF-mediated suppression of p53 activity (2008) J. Biol. Chem, 283 (47), pp. 32669-32679
Nawa, Y., Kawahara, K.I., Tancharoen, S., Meng, X., Sameshima, H., Ito, T., Masuda, Y., Maruyama, I., Nucleophosmin may act as an alarmin: Implications for severe sepsis (2009) J. Leukocyte Biol, 86 (3), pp. 645-653
Arora, K., Gwinn, W.M., Bower, M.A., Watson, A., Okwumabua, I., MacDonald, H.R., Bukrinsky, M.I., Constant, S.L., Extracellular cyclophilins contribute to the regulation of inflammatory responses (2005) J. Immunol, 175 (1), pp. 517-522
Kim, H., Kim, W.J., Jeon, S.T., Koh, E.M., Cha, H.S., Ahn, K.S., Lee, W.H., Cyclophilin A may contribute to the inflammatory processes in rheumatoid arthritis through induction of matrix degrading enzymes and inflammatory cytokines from macrophages (2005) Clin. Immunol, 116 (3), pp. 217-224
Jin, Z.G., Lungu, A.O., Xie, L., Wang, M., Wong, C., Berk, B.C., Cyclophilin A is a proinflammatory cytokine that activates endothelial cells (2004) Arterioscler., Thromb., Vasc. Biol, 24 (7), pp. 1186-1191
Watt, J. P., Wolfson, L. J., O'Brien, K. L., Henkle, E., Deloria-Knoll, M., McCall, N., Lee, E., Cherian, T., Burden of disease caused by Haemophilus influenzae type b in children younger than 5 years: Global estimates (2009) Lancet, 374 (9693), pp. 903-91
Dufrene, Y. F., Using nanotechniques to explore microbial surfaces (2004) Nat. Rev. Microbiol, 2 (6), pp. 451-460
McDonald, P. P., Bald, A., Cassatella, M. A., Activation of the NF- B pathway by inflammatory stimuli in human neutrophils (1997) Blood, 89 (9), pp. 3421-3433
Cassatella, M. A., The production of cytokines by polymorphonuclear neutrophils (1995) Immunol. Today, 16 (1), pp. 21-26
Fessler, 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 (2002) J. Biol. Chem, 277 (35), pp. 31291-31302
Gadgil, H. S., Pabst, K. M., Giorgianni, F., Umstot, E. S., Desiderio, D. M., Beranova-Giorgianni, S., Gerling, I. C., Pabst, M. J., Proteome of monocytes primed with lipopolysaccharide: Analysis of the abundant proteins (2003) Proteomics, 3 (9), pp. 1767-1780
Coulton, J. W., Wan, D. T., The outer membrane of Haemophilus influenzae type b: Cell envelope associations of major proteins (1983) Can. J. Microbiol, 29 (2), pp. 280-287
Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J., Protein measurement with the Folin phenol reagent (1951) J. Biol. Chem, 193 (1), pp. 265-275
Yin, E. T., Galanos, C., Kinsky, S., Bradshaw, R. A., Wessler, S., Luderitz, O., Sarmiento, M. E., Picogram-sensitive assay for endotoxin: Gelation of Limulus polyphemus blood cell lysate induced by purified lipopolysaccharides and lipid A from Gram-negative bacteria (1972) Biochim. Biophys. Acta, 261 (1), pp. 284-289
Mendelsohn, B. A., Malone, J. P., Townsend, R., Gitlin, J., Proteomic analysis of anoxia tolerance in the developing zebrafish embryo (2009) Comp. Biochem. Physiol., Part D, 4 (1), pp. 21-31
Tsan, M. F., Gao, B., Cytokine function of heat shock proteins (2004) Am. J. Physiol.: Cell Physiol, 286 (4), pp. C739-C744
Haddad, J. J., Land, S. C., Redox/ROS regulation of lipopolysaccharide- induced mitogen-activated protein kinase (MAPK) activation and MAPK-mediated TNF-alpha biosynthesis (2002) Br. J. Pharmacol, 135 (2), pp. 520-536
Lavoie, J. N., Hickey, E., Weber, L. A., Landry, J., Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27 (1993) J. Biol. Chem, 268 (32), pp. 24210-24214
Yin, H. L., Hartwig, J. H., The structure of the macrophage actin skeleton (1988) J. Cell Sci. Suppl, 9, pp. 169-184
Eswarappa, S. M., Pareek, V., Chakravortty, D., Role of actin cytoskeleton in LPS-induced NF-kappaB activation and nitric oxide production in murine macrophages (2008) Innate Immun, 14 (5), pp. 309-318
Vabulas, R. M., Ahmad-Nejad, P., da Costa, C., Miethke, T., Kirschning, C. J., Hacker, H., Wagner, H., Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells (2001) J. Biol. Chem, 276 (33), pp. 31332-31339
Kim, Y. S., Koh, J. M., Lee, Y. S., Kim, B. J., Lee, S. H., Lee, K. U., Kim, G. S., Increased circulating heat shock protein 60 induced by menopause, stimulates apoptosis of osteoblast-lineage cells via upregulation of toll-like receptors (2009) Bone, 45 (1), pp. 68-76
Vertessy, B. G., Toth, J., Keeping uracil out of DNA: Physiological role, structure and catalytic mechanism of dUTPases (2009) Acc. Chem. Res, 42 (1), pp. 97-106
Ariza, M. E., Glaser, R., Kaumaya, P. T., Jones, C., Williams, M. V., The EBV-encoded dUTPase activates NF-kappa B through the TLR2 and MyD88-dependent signaling pathway (2009) J. Immunol, 182 (2), pp. 851-859
Waldman, W. J., Williams Jr., M. V., Lemeshow, S., Binkley, P., Guttridge, D., Kiecolt-Glaser, J. K., Knight, D. A., Glaser, R., Epstein-Barr virus-encoded dUTPase enhances proin-flammatory cytokine production by macrophages in contact with endothelial cells: Evidence for depression-induced atherosclerotic risk (2008) Brain Behav. Immun, 22 (2), pp. 215-223
Kim, H., Kim, W. J., Jeon, S. T., Koh, E. M., Cha, H. S., Ahn, K. S., Lee, W. H., Cyclophilin A may contribute to the inflammatory processes in rheumatoid arthritis through induction of matrix degrading enzymes and inflammatory cytokines from macrophages (2005) Clin. Immunol, 116 (3), pp. 217-224
Jin, Z. G., Lungu, A. O., Xie, L., Wang, M., Wong, C., Berk, B. C., Cyclophilin A is a proinflammatory cytokine that activates endothelial cells (2004) Arterioscler., Thromb., Vasc. Biol, 24 (7), pp. 1186-1191
J Proteome Res (ISSN: 1535-3893), 2010 Feb; 9(2): 1050-1062.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.46, 5-year impact factor: 5.617
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-76149115883&partnerID=40&md5=9187146c8c50952df789f53113e232ac
Keywords: Haemophilus Influenzae Type B, Immune Response, Pathogen-Host Interaction, Porin, Proteomic Profiling, Loop 7 Peptide, P2 Porin, Unclassified Drug, Article, Cell Activation, Cell Strain U937, Controlled Study, Cytoskeleton, Disease Course, Host Pathogen Interaction, Human, Human Cell, Inflammation, Mass Spectrometry, Metabolism, Nucleotide Sequence, Priority Journal, Protein Analysis, Protein Expression, Signal Transduction, Stress, Two Dimensional Electrophoresis, Bacterial Proteins, Blotting, Western, Two-Dimensional, Matrix-Assisted Laser Desorption-Ionization, U937 Cells, Bacteria (microorganisms), Haemophilus Influenzae Serotype B,
Affiliations:
*** IBB - CNR ***
Department of Life Science, Second University of Naples, Via Vivaldi 43, I-81100 Caserta, Italy
Department of Experimental Medicine, Second University of Naples, Via De Crecchio 7, I-80138 Napoli, Italy
Department of Biological Sciences, University of Naples Federico II, Via Mezzocannone 16, I-80134, Napoli, Italy
Institute of Biostructure and Bioimaging, C.N.R., Via Mezzocannone 16, I-80134, Napoli, Italy
Proteomic and Biomolecular Mass Spectrometry Center, Institute of Food Science and Technology, C.N.R., Via Roma 52 A-C, I-83100 Avellino, Italy
References:
Watt, J.P., Wolfson, L.J., O'Brien, K.L., Henkle, E., Deloria-Knoll, M., McCall, N., Lee, E., Cherian, T., Burden of disease caused by Haemophilus influenzae type b in children younger than 5 years: Global estimates (2009) Lancet, 374 (9693), pp. 903-91
Dufrene, Y.F., Using nanotechniques to explore microbial surfaces (2004) Nat. Rev. Microbiol, 2 (6), pp. 451-460
McDonald, P.P., Bald, A., Cassatella, M.A., Activation of the NF-κB pathway by inflammatory stimuli in human neutrophils (1997) Blood, 89 (9), pp. 3421-3433
Cassatella, M.A., The production of cytokines by polymorphonuclear neutrophils (1995) Immunol. Today, 16 (1), pp. 21-26
Fessler, 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 (2002) J. Biol. Chem, 277 (35), pp. 31291-31302
Gadgil, H.S., Pabst, K.M., Giorgianni, F., Umstot, E.S., Desiderio, D.M., Beranova-Giorgianni, S., Gerling, I.C., Pabst, M.J., Proteome of monocytes primed with lipopolysaccharide: Analysis of the abundant proteins (2003) Proteomics, 3 (9), pp. 1767-1780
Zhang, X., Kuramitsu, Y., Fujimoto, M., Hayashi, E., Yuan, X., Nakamura, K., Proteomic analysis of macrophages stimulated by lipopolysaccharide: Lipopolysaccharide inhibits the cleavage of nucleophosmin (2006) Electrophoresis, 27 (8), pp. 1659-1668
Achouak, W., Heulin, T., Pages, J.M., Multiple facets of bacterial porins (2001) FEMS Microbiol. Lett, 199 (1), pp. 1-7
Galdiero, F., de L'ero, G.C., Benedetto, N., Galdiero, M., Tufano, M.A., Release of cytokines induced by Salmonella typhimurium porins (1993) Infect. Immun, 61 (1), pp. 155-161
Galdiero, M., Cipollaro de L'ero, G., Donnarumma, G., Marcatili, A., Galdiero, F., Interleukin-1 and interleukin-6 gene expression in human monocytes stimulated with Salmonella typhimurium porins (1995) Immunology, 86 (4), pp. 612-619
Galdiero, M., Vitiello, M., Galdiero, S., Eukaryotic cell signaling and transcriptional activation induced by bacterial porins (2003) FEMS Microbiol. Lett, 226 (1), pp. 57-64
Galdiero, M., D'Isanto, M., Vitiello, M., Finamore, E., Peluso, L., Galdiero, M., Monocytic activation of protein tyrosine kinase, protein kinase A and protein kinase C induced by porins isolated from Salmonella enterica serovar Typhimurium (2003) J. Infect, 46 (2), pp. 111-119
Galdiero, M., Tortora, A., Damiano, N., Vitiello, M., Longanella, A., Galdiero, E., Induction of cytokine mRNA expression in U937 cells by Salmonella typhimurium porins is regulated by different phosphorylation pathways (2005) Med. Microbiol. Immunol, 194 (1-2), pp. 13-23
Galdiero, M., D'Amico, M., Gorga, F., Di Filippo, C., D'Isanto, M., Vitiello, M., Longanella, A., Tortora, A., Haemophilus influenzae porin contributes to signaling of the inflammatory cascade in rat brain (2001) Infect. Immun, 69 (1), pp. 221-227
Galdiero, S., Capasso, D., Vitiello, M., D'Isanto, M., Pedone, C., Galdiero, M., Role of surface-exposed loops of Haemophilus influenzae protein P2 in the mitogen-activated protein kinase cascade (2003) Infect. Immun, 71 (5), pp. 2798-2809
Galdiero, S., Vitiello, M., Amodeo, P., D'Isanto, M., Cantisani, M., Pedone, C., Galdiero, M., Structural requirements for proinflammatory activity of porin P2 Loop 7 from Haemophilus influenzae (2006) Biochemistry, 45 (14), pp. 4491-4501
Coulton, J.W., Wan, D.T., The outer membrane of Haemophilus influenzae type b: Cell envelope associations of major proteins (1983) Can. J. Microbiol, 29 (2), pp. 280-287
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., Protein measurement with the Folin phenol reagent (1951) J. Biol. Chem, 193 (1), pp. 265-275
Yin, E.T., Galanos, C., Kinsky, S., Bradshaw, R.A., Wessler, S., Luderitz, O., Sarmiento, M.E., Picogram-sensitive assay for endotoxin: Gelation of Limulus polyphemus blood cell lysate induced by purified lipopolysaccharides and lipid A from Gram-negative bacteria (1972) Biochim. Biophys. Acta, 261 (1), pp. 284-289
Nikaido, H., Rosenberg, E.Y., Porin channels in Escherichia coli: Studies with liposomes reconstituted from purified proteins (1983) J. Bacteriol, 153 (1), pp. 241-252
Galanos, C., Luderitz, O., Westphal, O., A new method for the extraction of R lipopolysaccharides (1969) Eur. J. Biochem, 9 (2), pp. 245-249
Chambery, A., Farina, A., Di Maro, A., Rossi, M., Abbondanza, C., Moncharmont, B., Malorni, L., Parente, A., Proteomic analysis of MCF-7 cell lines expressing the zinc-finger or the proline-rich domain of retinoblastoma-interacting-zinc-finger protein (2006) J. Proteome Res, 5 (5), pp. 1176-1185
Zhang, B., Kirov, S., Snoddy, J., WebGestalt: An integrated system for exploring gene sets in various biological contexts (2005) Nucleic Acids Res, 33. , Web Server issue, W741-8
Mendelsohn, B.A., Malone, J.P., Townsend, R., Gitlin, J., Proteomic analysis of anoxia tolerance in the developing zebrafish embryo (2009) Comp. Biochem. Physiol., Part D, 4 (1), pp. 21-31
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Tsan, M. F., Gao, B., Cytokine function of heat shock proteins (2004) Am. J. Physiol.: Cell Physiol, 286 (4), pp. C739-C744
Haddad, J. J., Land, S. C., Redox/ROS regulation of lipopolysaccharide- induced mitogen-activated protein kinase (MAPK) activation and MAPK-mediated TNF-alpha biosynthesis (2002) Br. J. Pharmacol, 135 (2), pp. 520-536
Lavoie, J. N., Hickey, E., Weber, L. A., Landry, J., Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27 (1993) J. Biol. Chem, 268 (32), pp. 24210-24214
Yin, H. L., Hartwig, J. H., The structure of the macrophage actin skeleton (1988) J. Cell Sci. Suppl, 9, pp. 169-184
Eswarappa, S. M., Pareek, V., Chakravortty, D., Role of actin cytoskeleton in LPS-induced NF-kappaB activation and nitric oxide production in murine macrophages (2008) Innate Immun, 14 (5), pp. 309-318
Vabulas, R. M., Ahmad-Nejad, P., da Costa, C., Miethke, T., Kirschning, C. J., Hacker, H., Wagner, H., Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells (2001) J. Biol. Chem, 276 (33), pp. 31332-31339
Kim, Y. S., Koh, J. M., Lee, Y. S., Kim, B. J., Lee, S. H., Lee, K. U., Kim, G. S., Increased circulating heat shock protein 60 induced by menopause, stimulates apoptosis of osteoblast-lineage cells via upregulation of toll-like receptors (2009) Bone, 45 (1), pp. 68-76
Vertessy, B. G., Toth, J., Keeping uracil out of DNA: Physiological role, structure and catalytic mechanism of dUTPases (2009) Acc. Chem. Res, 42 (1), pp. 97-106
Ariza, M. E., Glaser, R., Kaumaya, P. T., Jones, C., Williams, M. V., The EBV-encoded dUTPase activates NF-kappa B through the TLR2 and MyD88-dependent signaling pathway (2009) J. Immunol, 182 (2), pp. 851-859
Waldman, W. J., Williams Jr., M. V., Lemeshow, S., Binkley, P., Guttridge, D., Kiecolt-Glaser, J. K., Knight, D. A., Glaser, R., Epstein-Barr virus-encoded dUTPase enhances proin-flammatory cytokine production by macrophages in contact with endothelial cells: Evidence for depression-induced atherosclerotic risk (2008) Brain Behav. Immun, 22 (2), pp. 215-223
Kim, H., Kim, W. J., Jeon, S. T., Koh, E. M., Cha, H. S., Ahn, K. S., Lee, W. H., Cyclophilin A may contribute to the inflammatory processes in rheumatoid arthritis through induction of matrix degrading enzymes and inflammatory cytokines from macrophages (2005) Clin. Immunol, 116 (3), pp. 217-224
Jin, Z. G., Lungu, A. O., Xie, L., Wang, M., Wong, C., Berk, B. C., Cyclophilin A is a proinflammatory cytokine that activates endothelial cells (2004) Arterioscler., Thromb., Vasc. Biol, 24 (7), pp. 1186-1191
Proteomic Analysis of Human U937 Cell Line Activation Mediated by Haemophilus influenzae Type b P2 Porin and Its Surface-Exposed Loop
The virulence of Haemophilus influenzae type b (Hib) has been attributed to a variety of potential factors associated with its cell surface, including lipopolysaccharides (LPS) and major outer membrane proteins (OMPs). P2 porin, one of the best-characterized porins in terms of its functional characteristics, is the most abundant OMP in Hib and has also been shown to possess proinflammatory activity. To characterize the role played by bacterial surface components in disease onset and development, the proteomic profiling of human U937 cell line activated by H. influenzae type b P2 porin and its most active surface-exposed loop (L7) was performed by means of two-dimensional electrophoresis and mass spectrometry. The study provided a list of candidate proteins with potential relevance in the host immune and inflammatory response. Most of the differentially expressed proteins are involved in metabolic processes, remodelling of cytoskeleton, stress response and signal transduction pathways. The results constitute the basis for dissecting signal transduction cascades activated by P2 stimulation and gain insights into the molecular events involved in the modulation of pathogen-host cell interactions. © 2010 American Chemical Society.
The virulence of Haemophilus influenzae type b (Hib) has been attributed to a variety of potential factors associated with its cell surface, including lipopolysaccharides (LPS) and major outer membrane proteins (OMPs). P2 porin, one of the best-characterized porins in terms of its functional characteristics, is the most abundant OMP in Hib and has also been shown to possess proinflammatory activity. To characterize the role played by bacterial surface components in disease onset and development, the proteomic profiling of human U937 cell line activated by H. influenzae type b P2 porin and its most active surface-exposed loop (L7) was performed by means of two-dimensional electrophoresis and mass spectrometry. The study provided a list of candidate proteins with potential relevance in the host immune and inflammatory response. Most of the differentially expressed proteins are involved in metabolic processes, remodelling of cytoskeleton, stress response and signal transduction pathways. The results constitute the basis for dissecting signal transduction cascades activated by P2 stimulation and gain insights into the molecular events involved in the modulation of pathogen-host cell interactions. © 2010 American Chemical Society.
Proteomic Analysis of Human U937 Cell Line Activation Mediated by Haemophilus influenzae Type b P2 Porin and Its Surface-Exposed Loop
Proteomic Analysis of Human U937 Cell Line Activation Mediated by Haemophilus influenzae Type b P2 Porin and Its Surface-Exposed Loop
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* A Structural View at Vaccine Development against M. tuberculosis (2 views)
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Impact Factor: 3.375
View Export to BibTeX Export to EndNote
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Impact Factor: 4.518
View Export to BibTeX Export to EndNote
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Impact Factor: 2.326
View Export to BibTeX Export to EndNote
Cantisani M, Vitiello M, Falanga A, Finamore E, Galdiero M, Galdiero S
* Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity (528 views)
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Impact Factor: 3.463
View Export to BibTeX Export to EndNote
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Impact Factor: 5.132
View Export to BibTeX Export to EndNote
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Impact Factor: 2.801
View Export to BibTeX Export to EndNote
Romano M, Buffolano W, Bisogni R, Russo R, Liuzzi R, Newell ML, Carandente P
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Impact Factor: 2.133
View Export to BibTeX Export to EndNote
Galdiero S, Vitiello M, Amodeo P, D'Isanto M, Cantisani M, Pedone C, Galdiero M
* Structural requirements for proinflammatory activity of porin P2 loop 7 from Haemophilus influenzae (575 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2006 Apr 11; 45(14): 4491-4501.
Impact Factor: 3.633
View Export to BibTeX Export to EndNote
Benedetti E, Pedone C
* Cyclolinopeptide A: inhibitor, immunosuppressor or other? (568 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2005 May; 11(5): 268-272.
Impact Factor: 1.803
View Export to BibTeX Export to EndNote
Galdiero S, Capasso D, Vitiello M, D'Isanto M, Pedone C, Galdiero M
* Protein P2 from Haemophilus influenzae: The role of its surface exposed loops on the mitogen-activated protein kinase cascade (378 views)
Infection And Immunity (ISSN: 0019-9567), 2003 May; 71(5): 2798-2809.
Impact Factor: 3.875
View Export to BibTeX Export to EndNote
Cook JA, Kim SY, Teague D, Krishna MC, Pacelli R, Mitchell JB, Vodovotz Y, Nims RW, Christodoulou D, Miles AM, Grisham MB, Wink DA
Convenient colorimetric and fluorometric assays for S-nitrosothiols (568 views)
Anal Biochem (ISSN: 0003-2697, 1096-0309electronic, 0003-2697linking), 1996 Jul 1; 238(2): 150-158.
Impact Factor: 2.017
View Export to BibTeX Export to EndNote
15 Records (15 excluding Abstracts).
Total impact factor: 56.197 (56.197 excluding Abstracts).
Total 5 year impact factor: 50.332 (50.332 excluding Abstracts).
Total impact factor: 56.197 (56.197 excluding Abstracts).
Total 5 year impact factor: 50.332 (50.332 excluding Abstracts).
535 views. Last view on Tuesday 23 May 2023, 10:41:20
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