Respuesta inmune innata y sus implicaciones fisiopatológicas

  1. Díaz Martín, D.
  2. Úbeda Cantera, M.
  3. López Suárez, A.
  4. Álvarez de Mon Soto, M.
Revista:
Medicine: Programa de Formación Médica Continuada Acreditado

ISSN: 0304-5412

Año de publicación: 2017

Serie: 12

Número: 24

Páginas: 1388-1397

Tipo: Artículo

DOI: 10.1016/J.MED.2016.12.009 DIALNET GOOGLE SCHOLAR

Otras publicaciones en: Medicine: Programa de Formación Médica Continuada Acreditado

Resumen

Abstract Overview Innate or natural immunity is the first line of defense against microorganisms. The term “innate” refers to the sensors involved in the pathogen recognition are encoded by genes in germline suffering non-somatic rearrangement to generate variants Components of the innate immunity The weapons of the innate immune system include molecular and cellular defense mechanisms that exist before an infection takes place, allowing them to respond to it quickly. Sensors of the innate immunity are specific structures common to groups of related pathogens, however they cannot distinguish subtle differences between them. Receptors of the innate immunity The first block analyzes receptors used by the innate immunity to identify characteristic molecules of groups of pathogens, as well as damaged and stressed cells, named pattern recognition receptors. Molecules of the innate immunity The second block examines in depth the soluble molecules that mediate innate immunity. These molecules act quickly against extracellular pathogens in three important ways: as opsonins, lytic agents and as pro-inflammatory agents.

Referencias bibliográficas

  • Medzhitov R, Janeway CA Jr. Decoding the patterns of self and nonself by the innate immune system. Science. 2002;296(5566):298-300.
  • Kumar H, Kawai T, Akira S. Pathogen recognition by the innate immune system. Int Rev Immunol. 2011;30(1):16-34.
  • Janeway C A, Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol. 1989;54:1-13.
  • Brubaker SW, Bonham KS, Zanoni I, Kagan JC. Innate immune pattern recognition: a cell biological perspective. Annu Rev Immu-nol. 2015;33:257-90.
  • Deretic V, Saitoh T, Akira S. Autophagy in infection, inflammation and immunity. Nat Rev Immunol. 2013;13(10):722-37.
  • Lamkanfi M, Dixit VM. Mechanisms and functions of inflammasomes. Cell. 2014;157(5):1013-22.
  • Broz P, Monack DM. Newly described pattern recognition receptors team up against intracellular pathogens. Nat Rev Immunol. 2013;13(8):551-65.
  • Bianchi ME. DAMPs, PAMPs and alarmins: all we need to know about danger. J Leukoc Biol. 2007;81(1):1-5.
  • Osorio F, Reis E, Sousa C. Myeloid C-type lectin receptors in pathogen recognition and host defence. Immunity. 2011;651-64.
  • Brown GD. Dectin-1: a signalling non-TLR pattern recognition receptor. Nat Rev Immunol. 2006;6:33-43.
  • Elinav E, Trowig T, Henao-Mejia J, Flavell RA. Regulation of the antimicrobial response by NLR proteins. Immunity. 2011;34:665-79.
  • Philpott DJ, Sorbara MT, Robertson SJ, Croitoru K, Girardin SE. NOD proteins: regulators of inflammation in health and disease. Nat Rev Immunol. 2014;14(1):9-23.
  • Tschopp J, Martinon F, Burns K. NALPs: a novel protein family involved in inflammation. Nat Rev Mol Cell Biol. 2003;4(2):95-104.
  • Yoneyama M, Kikuchi M, Matsumoto K, Imaizumi T, Miyagishi M, Taira K. Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity. J Immunol. 2005;175(5):2851-8.
  • Unterholzner L. The interferon response to intracellular DNA: why so many receptors? Immunobiology. 2013;218(11):1312-21.
  • Canton J, Neculai D, Grinstein S. Scavenger receptors in homeostasis and immunity. Nat Rev Immunol. 2013;13(9):621-34.
  • Hancock RE, Haney EF, Gill EE. The immunology of host defence peptides: beyond antimicrobial activity. Nat Rev Immunol. 2016;16(5):321-34.
  • Nijnik A, Hancock REW. The roles of cathelicidin LL-37 in immune defences and novel clinical applications. Curr Opin Hematol. 2009;16:41-7.
  • Hazlett L, Wu M. Defensins in innate immunity. Cell Tissue Res. 2011; 343:175-88.
  • Semple F, Dorin JR. E-Defensins: multifunctional modulators of infec-tion, inflammation and more? J Innate Immun. 2012;4:337-48.
  • Winter J, Pantelis A, Reich R, Martini M, Kraus D, Jepsen S. Human E-defensin-1, –2, and –3 exhibit opposite effects on oral squamous cell carcinoma cell proliferation. Cancer Invest. 2011;29:196-201.
  • Lecaille F, Lalmanach G, Andrault PM. Antimicrobial proteins and peptides in human lung diseases: a friend and foe partnership with host proteases. Biochimie. 2016;122:151-68.
  • Kahlenberg J M, Kaplan MJ. Little peptide, big effects: the role of LL-37 in inflammation and autoimmune disease. J Immunol. 2013;191:4895-901.
  • Holers VM. Complement and its receptors: new insights into human disease. Annu Rev Immunol. 2014;32:433-59.
  • Lachmann PJ, Hughes-Jones NC. Initiation of complement activation. Springer Semin Immunopathol. 1984;7:143-62.
  • Muller-Eberhard HJ. Molecular organization and function of the complement system. Annu Rev Biochem. 1988;57:321-47.
  • Reid KBM, Turner MW. Mammalian lectins in activation and clearance mechanisms involving the complement system. Springer Semin Immunopathol. 1994;15:307-25.
  • Wetsel RA. Structure, function and cellular expression of complement anaphylatoxin receptors. Curr Opin Immunol. 1995;7:48-53.
  • Christiaans SC, Wagener BM, Esmon CT, Pittet JF. Protein C and acute inflammation: a clinical and biological perspective. Am J Physiol Lung Cell Mol Physiol. 2013;305(7):L455-66.
  • Bottazzi B, Inforzato A, Messa M, Barbagallo M, Magrini E, Garlanda Cl. The pentraxins PTX3 and SAP in innate immunity, regulation of inflammation and tissue remodelling. J Hepatol. 2016; 64(6):1416-27.
  • Foo SS, Reading PC, Jaillon S, Mantovani A, Mahalingam S. Pentraxins and collectins: friend or foe during pathogen invasion? Trends Microbiol. 2015;23(12):799-811.
  • Endo Y, Matsushita M, Fujita T. Role of ficolin in innate immunity and its molecular basis. Immunobiology. 2007;212(4-5):371-9.
  • Laine VJ, Grass DS, Nevalainen TJ. Protection by group II phospholipase A2 against Staphylococcus aureus. J Immunol. 1999;162(12): 7402-8.
  • Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997;41(1):54-9.
  • McKenzie HA, White FH. Lysozyme and alphalactalbumin: structure, function, and interrelationships. Adv. Protein Chem. 1991;41:173-315.
Fuente de los datos: Dialnet