medigraphic.com

2004, Número 1

<< Anterior Siguiente >>

Bioquimia 2004; 29 (1)


Fagocitosis: mecanismos y consecuencias Segunda parte

Rojas-Espinosa O, Arce-Paredes P

Idioma: Español
Referencias bibliográficas: 87
Paginas: 18-31
Archivo PDF: 1385.62 Kb.


RESUMEN

Ellie Metchnikoff, en 1880, descubrió que la función de las células fagocíticas era esencial para la supervivencia de todas las especies del reino animal. En los organismos unicelulares como los protozoarios, la función fagocítica es el único medio por el cual estos organismos adquieren su alimento. La función fagocítica de estas células se mejora a lo largo de la evolución y se mantiene en los animales más evolucionados, aunque aquí la función de los fagocitos deja de ser preponderantemente nutricional para constituirse en un eficiente mecanismo de protección no específico contra agentes infecciosos y de eliminación de células muertas o seniles. Cada etapa del proceso fagocítico (la migración, el reconocimiento de lo que puede y debe ingerirse, la endocitosis y la destrucción de partículas) se descubre cada vez más complicada; día a día se identifican más componentes moleculares y se establecen más interacciones y rutas metabólicas. Aunque el proceso de la fagocitosis no está esclarecido en su totalidad, ahora tenemos una mejor idea de cómo se reconocen las partículas que deben eliminarse y de los mecanismos subsecuentes que llevan a su destrucción. En este artículo, se hace una revisión concisa del proceso de la fagocitosis y se enfatiza su importancia como mecanismo de protección en los vertebrados, señalando, aunque de manera somera, aquellos aspectos que en la actualidad son objeto de mayor estudio, incluyendo estructura celular, la existencia y función de las proteínas de adhesión, los receptores para endocitosis, las proteínas G, las cascadas de señalización, la maduración de los fagosomas, y la generación de los metabolitos tóxicos del oxígeno y el nitrógeno.


REFERENCIAS (EN ESTE ARTÍCULO)

  1. Aderem A, Underhill DM. Mechanisms of phagocytosis in macrophages. Annu Rev Immunol 1999; 170: 593-623.

  2. Underhill DM, Ozinsky A. Phagocytosis of microbes: complexity in action. Annu Rev Immunol 2002; 20: 825-852.

  3. Greenberg S, Grinstein S. Phagocytosis and innate immunity. Curr Opin Immunol 2002; 14: 136-145.

  4. Bainton DF, Ullot JL, Farquhar MG. The development of neutrophilic polymorphonuclear leukocytes in human bone marrow. J Exp Med 1971; 134: 907-939.

  5. Dransfield I, Buckle AM, Savill JS, McDowall A, Haslett C, Hogg N. Neutrophil apoptosis is associated with a reduction in CD16 (Fc gamma RIII) expression. J Immunol 1994; 153: 1254-1263.

  6. Gallin JI. Leukocyte adherence-related glycoproteins LFA-1, Mo-1, and p150,95: A new group of monoclonal antibodies, a new disease, and a possible opportunity to understand the molecular basis of leukocyte adherence. J Infect Dis 1985; 152: 661-664.

  7. Etzioni A. Integrins: The glue of life. Lancet 1999; 353: 341-343.

  8. Carlos TM, Harlan JM. Leukocyte-endothelial adhesion molecules. Blood 1994; 84: 2068-2101.

  9. Frenette PS, Wagner DD. Adhesion molecules-Part II: blood vessels and blood cells. N Engl J Med 1996; 335: 43-48.

  10. Rosales C, Brown EJ. Neutrophil receptors and modulation of the immune response. In: The Neutrophil. Ed for JS Abramson and JG Wheeler, London: Oxford University Press; 1993. p. 23-62.

  11. Hayward AR, Harvey BA, Leonard J, Greenwood MC, Wood CB, Soothill JF. Delayed separation of the umbilical cord, widespread infections, and defective neutrophil mobility. Lancet 1979; 26: 1099-1001.

  12. Abramson JS, Mills EL, Sawyer MK, Regelmann WR, Nelson JD, Quie PG. Recurrent infections and delayed separation of the umbilical cord in an infant with abnormal phagocytic cell locomotion and oxidative response during particle phagocytosis. J Pediatrics 1982; 99: 887-894.

  13. Arnaout MA, Pitt J, Cohen HJ, Melamed J, Rosen FS, Colten HR. Deficiency of a granulocyte-membrane glycoprotein (gp150) in a boy with recurrent bacterial infections. N Engl J Med 1982; 306: 693-699.

  14. Crowley CA, Curnutte JT, Rosin RE, Schwartz J, Gallin JI, Klempner M, et al. An inherited abnormality of neutrophil adhesion. Its genetic transmission and its association with a missing protein. N Engl J Med 1980; 302: 1163-1168.

  15. Kohl S, Springer TA, Schmalstieg FC, Loo LS, Anderson DC. Defective natural killer cytotoxicity and polymorphonuclear leukocyte antibody-dependent cellular cytotoxicity in patients with LFA-1/OKM-1 deficiency. J Immunol 1984; 133: 2972-2978.

  16. Arnaout MA, Todd RF, Dana N, Melamed J, Schlossman SF, Colten HR. Inhibition of phagocytosis of complement C3- or immunoglobulin-coated particles and of C3bi binding by monoclonal antibodies to a monocyte-granulocyte membrane glycoprotein (Mo1) J Clin Invest 1983; 72: 171-179.

  17. Anderson DC, Schmalsteig FC, Finegold MJ, Hughes BJ, Rothlein R, Miller LJ, et al. The severe and moderate phenotypes of heritable Mac-1, LFA-1 deficiency: their quantitative definition and relation to leukocyte dysfunction and clinical features. J Infect Dis 1985; 152: 668-689.

  18. Patarroyo M, Beatty PG, Serhan CN, Gahmberg CG. Identification of a cell-surface glycoprotein mediating adhesion in human granulocytes. Scand J Immunol 1985; 22: 19-631.

  19. Beller DI, Springer TA, Schreiber RD. Anti-Mac-1 selectively inhibits the mouse and human type three complement receptor. J Exp Med 1982; 156: 1000-1009.

  20. Wright SD, Rao PE, Van Voorhis WC, Craigmyle LS, Lida K, Talle MA, et al. Identification of the C3b1 receptor of human monocytes and macrophages by using monoclonal antibodies. Proc Natl Acad Sci (USA) 1983; 80: 5699-5703.

  21. Page RC, Sims TJ, Geissler F, Altman LC, Baab DA. Defective neutrophil and monocyte motility in patients with early onset periodontitis. Infect Immun 1985; 47: 169-175.

  22. Van Dyke TE, Horoszewics HU, Cianciola LJ, Genco RJ. Neutrophil chemotaxis dysfunction in human periodontitis. Infect Immun 1980; 27: 124-132.

  23. Frenette PS, Wagener DD. Adhesion molecules-Part I. N Engl J Med 1996; 335: 1526-1529.

  24. Phillips ML, Schwartz BR, Etzioni A, Bayer R, Ochs HD, Paulson JC, et al. Neutrophil adhesion in leukocyte adhesion deficiency syndrome type 2. J Clin Invest 1995; 96: 2898-2906.

  25. Marquardt T, Brune T, Luhn K, Zimmer KP, Fabritz L, van der Werft N, et al. Leukocyte adhesion deficiency II syndrome, a generalized defect in fucose metabolism. J Pediatr 1999; 134: 681-688.

  26. Marquardt T, Luhn K, Srikrishna G, Freeze HH, Harms E, Westweber D. Correction of leukocyte adhesion deficiency type II with oral fucose. Blood 1999; 94: 3976-3985.

  27. Linder ME, Gilman AG. G proteins. Sci Amer 1992; 267: 36-43.

  28. Lefkowitz RJ. Clinical implications of basic research. G proteins in medicine. N Engl J Med 1995; 332: 186-187.

  29. Birnbaumer L, Birnbaumer M. Signal transduction by G proteins. J Recept Signal Transduct Res 1997; 15: 213-252.

  30. Quinn MT, Parkos CA, Walker L, Orkin SH, Dinauer MC, Jesaitis AJ. Association of a ras-related protein with cytochrome b of human neutrophils. Nature 1989; 342: 198-200.

  31. Bokoch GM. Signal transduction by GTP binding proteins during leukocyte activation of phagocytic cells. Curr Top Membr Transp 1990; 35: 65-111.

  32. Bokoch GM. Regulation of cell function by Rho family GTPases. Immunol Res 2000; 21: 139-148.

  33. Aderem A. The Marcks brothers: A family of protein kinase C substrates. Cell 1992; 71: 713-716.

  34. Rosen A, Keenan KF, Thelen M, Nairn AC, Aderem A. Activation of PKC results in the displacement of its myristoilated, alanin-rich substrate from punctuate structures in macrophage filopodia. J Exp Med 1990; 172: 1211-1215.

  35. Kyat M, Anderson S, Allen LA, Aderem A. MARKS regulates membrane ruffling and cell spreading. Curr Biol 1997; 7: 611-614.

  36. Vicente-Manzanares M, Sancho D, Yañez-Mó, M, Sánchez-Madrid M. The leukocyte cytoskeleton in cell migration and immune interactions. Internat Rev Cytol 2002; 216: 233-289.

  37. Olmsted JB, Borisy GG. Microtubules. Annu Rev Biochem 1973; 42: 507-540.

  38. Lazarides E. Weber K. Actin antibody: The specific visualization of actin filaments in non-muscle cells. Proc Nat Acad Sci 1974; 71: 2268-2272.

  39. Weber K, Groeschel-Stewart U. Antibody to myosin: the specific visualization of myosin-containing filaments in nonmuscle cells. Proc Natl Acad Sci 1974; 71: 4561-4564.

  40. Lazarides E. Tropomyosin antibody: the specific localization of tropomyosin in non-muscle cells. J Cell Biol 1975; 65: 549-561.

  41. Janmey PA. Mechanical properties of cytoskeletal polymers. Curr Opin Cell Biol 1991; 3: 4-11.

  42. Sarndahl E, Lindroth M, Bengtsson T, Farllman M, Gustavsso J, Stendahl O, et al. Association of ligand-receptor complexes with actin filaments in human neutrophils: A possible regulatory role for a G-protein. J Cell Biol 1990; 109: 2791-2799.

  43. Southwick FS, Young CL. The actin released from profilin-actin complexes is insufficient to account for the increase in F-actin in chemoattractant-stimulated polymorphonuclear leukocytes. J Cell Biol 1990; 110: 1965-1973.

  44. Snyderman R. Regulatory mechanisms of a chemoattractant receptor on human polymorphonuclear leukocytes. Rev Infect Dis 1985; 7: 390-394.

  45. Saba TM. Aespecific opsonins. In: The human system and infectious diseases. Karger, Basel; 1975. p. 489-504.

  46. Kaplan G. Differences in the mode of phagocytosis with Fc and C3 receptors in macrophages. Scand J Immunol 1977; 6: 797-807.

  47. Johnson E, Eskeland T. Complement C3b receptor mediated phagocytosis of agarose beads by mouse macrophages. I. Intracellular degradation of agarose-bound C3bi and C3b by lysosomal enzymes. Scand J Immunol 1983; 18: 193-200.

  48. Johnson E, Gauperaa T, Eskeland T. Fibronectin binds to complement-coated agarose beads and increases their association to mouse macrophages. Scand J Immunol 1985; 22: 315-320.

  49. Bevilacqua MP, Amrani D, Mosesson MW, Bianco C. Receptors for cold insoluble globulin (plasma fibronectin) on human monocytes. J Exp Med 1981; 153: 42-60.

  50. Proctor RA. Fibronectin: an enhancer of phagocytic function. Rev Infect Dis 1987; 9: 412-419.

  51. Wright SD, Silverstein S. Tumor promoting phorbol esters stimulate C3b and C3bi receptor-mediated phagocytosis in cultured human monocytes. J Exp Med 1982; 156: 1149-1164.

  52. Bianco C, Griffin FM, Silverstein SC. Studies of the macrophage complement receptor. Alterations of receptor function upon macrophage activation. J Exp Med 1975; 141: 1278-1282.

  53. Wright SD, Craigmyle LS, Silverstein SC. Fibronectin and serum amyloid P component stimulate C3b and C3bi-mediated phagocytosis in cultured human monocytes. J Exp Med 1983; 158: 1338-1343.

  54. Griffin JA, Griffin FM. Augmentation of macrophage complement receptor function in vitro. I. Characterization of the cellular interactions required for the generation of a T-lymphocyte product that enhances macrophage complement receptor function. J Exp Med 1979; 150: 653-675.

  55. Tulkens P, Schneider YJ, Trouet A. The fate of the plasma membrane during endocytosis. Biochem Rev 1977; 5: 1809-1815.

  56. Medzhitov R, Janeway CH. Innate immunity. N Engl J Med 2000; 343: 338-344.

  57. Ravetch JV. Fc receptors: rubor redux. Cell 1994; 78: 553-560.

  58. Ravetch JV. Fc receptors. Curr Opin Immunol 1997; 9: 121-125.

  59. Unkeless JC, Jin J. Inhibitory receptors, ITIM sequences and phosphatases. Curr Opin Immunol 1997; 9: 338-343.

  60. Reth M. Antigen receptor tail clue. Nature 1989; 338: 383-384.

  61. Strzelecka A, Kwiatkowska K, Sobota A. Tyrosine phosphorylation and Fc gamma receptor-mediated phagocytosis. FEBS Lett 1997; 400: 11-14.

  62. Greenberg S. Signal transduction of phagocytosis. Trends Cell Biol 1995; 5: 93-99.

  63. Agarwal A, Salem P, Robbins KC. Involvement of p72syk, a protein-tyrosine kinase in Fc gamma receptor signalling. J Biol Chem 1993; 268: 15900-15905.

  64. Kiener PA, Rankin BM, Burkhardt AL, Schieven GL, Gilliland LK, Rowley RB, et al. Cross-linking of FcgRI and FcgRII on monocytic cells activates a signal transduction pathway common to both Fc receptors that involves the stimulation of p72 Syk protein tyrosine kinase. J Biol Chem 1993; 268: 24442-24448.

  65. Ghazizadeh S, Bolen JB, Fleith HB. Tyrosine phosphorylation and association of Syk with FcgRII in monocytic THP-1 cells. Biochem J 1995; 74: 669-674.

  66. Cox D, Chang P, Kurosaki T, Greenberg S. Sky tyrosine kinase is required for immunoreceptor tyrosine activation motif-dependent actin assembly. J Biol Chem 1996; 271: 16597-16602.

  67. Greenberg S. Modular components of phagocytosis. J Leuk Biol 1999; 66: 712-717.

  68. Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 1992; 70: 401-410.

  69. Modlin RL, Brightbill HD, Godowski PJ. The Toll of innate immunity on microbial pathogens. N Engl J Med 1999; 340: 1834-1835.

  70. Anderson KV. Toll signalling pathways in the innate immune response. Curr Opin Immunol 2000; 12: 13-19.

  71. Jeoung-Sook S, Zhimin G, Soman NA. Involvement of cellular caveolae in bacterial entry into mast cells. Science 2000; 289: 785-788.

  72. Schlegel A, Lisanti MP. Caveolae and their coat proteins, the caveolins: from electron microscopy novelty to biological launching pad. J Cell Physiol 2001; 186: 329-337.

  73. Rosenberg CM, Brumell JH, Finlay BB. Microbial pathogenesis: lipid rafts as pathogen portals. Current Biol 2000; 10: R823-R825.

  74. Swanson JA, Baer SC. Phagocytosis by zippers and triggers. Trends Cell Biol 1995; 5: 89-93.

  75. Pitt A, Mayorga LS, Stahl PD, Schwartz AL. Alterations in the protein composition of maturing phagosomes. J Clin Invest 1992; 90: 1978-1983.

  76. Racoosin EL, Swanson JA. Macropinosome maturation and fusion with tubular lysosomes in macrophages. J Cell Biol 1993; 121: 1011-1020.

  77. Desjardins M, Huber LA, Parton RG, Griffiths G. Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus. J Cell Biol 1994; 124: 677-688.

  78. de Chastellier C, Thilo L. Phagosome maturation and fusion with lysosomes in relation to surface property and size of the phagocytic particle. Eur J Cell Biol 1997; 74: 49-62.

  79. Berthiaume EP, Medina C, Swanson JA. Molecular size-fractionation during endocytosis in macrophages. J Cell Biol 1995; 129: 989-998.

  80. Desjardins M, Nizala NN, Corsini R, Rondeau C. Maturation of phagosomes is accompanied by changes in their fusion properties and size-selective acquisition of solute materials from endosomes. J Cell Sci 1997; 110: 2303-2314.

  81. Diakonova M, Gerke V, Ernst J, Liautard JP, van der VG, Griffiths G, et al. Localization of five annexins in J774 macrophages and on isolated phagosomes. J Cell Sci 1997; 110: 1199-1213.

  82. Pizon V, Desjardins M, Bucci C, Parton RG, Zerial M. Association of rap-1a and rap-1b proteins with late endocytic phagocytic compartments and rap-2a with the Golgi complex. J Cell Sci 1994; 107: 1661-1670.

  83. Gorvell JP, Chavrier P, Zerial M, Gruenberg J. Rab5 controls early endosome fusion in vitro. Cell 1991; 64: 915-925.

  84. Feng Y, Press B, Wandinger-Ness A. Rab7: an important regulator of late endocytic membrane traffic. J Cell Biol 1995; 131: 1435-1452.

  85. Claus V, Jahraus A, Tjelle T, Berg T, Kisrchke H, Faulstich H, et al. Lysosomal enzyme trafficking between phagosomes, endosomes and lysosomes in J774 macrophages. Enrichment of cathepsin H in early endosomes. J Biol Chem 1998; 273: 9842-9851.

  86. Blocker A, Severin FF, Burkhardt JK, Bingham JB, Yu H, Olivo JC, et al. Molecular requirements for bidirectional movement of phagosomes along microtubules. J Cell Biol 1997; 137: 113-129.

  87. Clague MJ. Molecular aspects of the endocytic pathway. Biochem J 1998; 336: 271-282.




2020     |     www.medigraphic.com