*** IBB - CNR *** Dipto. di Medicina Sperimentale, Sezione Microbiol. Microbiol. Clin., Seconda Univ. degli Studi di Napoli, Via De Crecchio 7, 80138 Naples, Italy Ctro. Interuniversitario Ric. Sui P., Univ. di Napoli 'Federico II', Via Mezzocannone 6-8, 80134 Naples, Italy Dipartimento di Chimica Biologica, Ist. Biostrutture Bioimmagini - CNR, Univ. di Napoli 'Federico II', Via Mezzocannone, 80134 Naples, Italy
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Cory, S., Adams, J. M., The Bcl-2 family: Regulators of the cellular life-or-death switch (2002) Nat. Rev. Cancer, 2, pp. 647-656
Neary, J. M., Yi, K., Karalus, R. J., Murphy, T. F., Antibodies to loop 6 of the P2 porin protein of nontypeable Haemophilus influenzae are bactericidal against multiple strains (2001) Infect. Immun., 69, pp. 773-778
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Merz, A. J., So, M., Interactions of pathogenic Neisseriae with epithelial cell membranes (2000) Annu. Rev. Cell Dev. Biol., 16, pp. 423-457
Evans, D. J., Frank, D. W., Finck-Barbancon, V., Wu, C., Fleiszig, S. M., Pseudomonas aeruginosa invasion and cytotoxicity are independent events, both of which involve protein tyrosine kinase activity (1998) Infect. Immun., 66, pp. 1453-1459
Weinstein, S. L., Sanghera, J. S., Lemke, K., Defranco, A. L., Pelech, S. L., Bacterial lipopolysaccharide induces tyrosine phosphorylation and activation of mitogen-activated protein kinases in macrophages (1992) J. Biol. Chem., 267, pp. 14955-14962
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Davis, R. J., Signal transduction by the JNK group of MAP kinases (2000) Cell, 103, pp. 239-252
Procyk, K. J., Kovarik, P., Von Gabain, A., Baccarini, M., Salmonella typhimurium and lipopolysaccharide stimulate extracellularly regulated kinase activation in macrophages by a mechanism involving phosphatidylinositol 3-kinase and phospholipase D as novel intermediates (1999) Infect. Immun., 67, pp. 1011-1017
Beaty, C. D., Franklin, T. L., Uehara, Y., Wilson, C. B., Lipopolysaccharide-induced cytokine production in human monocytes: Role of tyrosine phosphorylation in transmembrane signal transduction (1994) Eur. J. Immunol., 24, pp. 1278-1284
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The protein composition of the outer membrane of Gram-negative bacteria consists of about 20 immunochemically distinct proteins, termed outer membrane proteins (OMPs). Apart from their structural role, OMPs have been shown to have other functions, particularly with regard to transport, and have been classified as permeases and porins. Porins, during their interaction with the host, are immunogenic and also directly stimulate several cellular functions. Porins work both as molecules present on the bacterial surface and as molecules released by bacteria. Lipopolysaccharide and OMPs, the major structural macromolecular constituents of the outer membrane, carry out a fundamental role in the pathogenesis of Gram-negative infections. This brief review describes the multiple facets of the biological activities of porins both in vitro and in vivo, particularly focusing on their ability to induce the expression of cytokines and other factors that modulate cellular activities with either pathological or adaptive consequences. This brief discussion will focus on the signal transmission mechanisms induced by bacterial porins. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Microbiological Societies.
11 Records (11 escludendo Abstract e Conferenze). Impact factor totale: 32.885 (32.885 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 33.758 (33.758 escludendo Abstract e Conferenze).
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