Entrar/Registro  
INICIO ENGLISH
 
Revista Mexicana de Neurociencia
   
MENÚ

Contenido por año, Vol. y Num.

Índice de este artículo

Información General

Instrucciones para Autores

Mensajes al Editor

Directorio






>Revistas >Revista Mexicana de Neurociencia >Año 2007, No. 6


Reyes-Pablo A, Mena LR, Luna-Muñoz J, García SF
Encefalopatías producidas por priones
Rev Mex Neuroci 2007; 8 (6)

Idioma: Español
Referencias bibliográficas: 55
Paginas: 597-602
Archivo PDF: 99.74 Kb.


Texto completo




RESUMEN

Introducción: Actualmente se sabe que las enfermedades causadas por priones o encefalopatías espongiformes transmisibles (TSE), representan un grupo de patologías neurodegenerativas del sistema nervioso central, que afectan tanto a humanos como a animales. La menos rara de estas enfermedades es la de Creutzfeldt-Jakob (CJD). En 1998 se reportó el primer caso de Gerstman-Sträussler-Scheinker (GSS) de tipo familiar (un caso por millón de familias). La encefalopatía espongiforme bovina (BSE) –mejor conocida como el “mal de las vacas locas”– es atribuida al consumo de productos contaminados con la carne de vacas afectadas. La enfermedad por priones puede presentarse como un desorden genético, infeccioso o esporádico, los cuales involucran modificaciones de la proteína prion (PrP), un constituyente normal de las células de mamífero. Recientemente se ha sugerido que la proteína prion celular (PrPc) actúa como una metaloproteína, y tiene una tendencia intrínseca a adoptar algunas características estructurales de la proteína prion de Scrapie (PrPsc).


Palabras clave: priones, encefalopatías espongiformes neurodegenerativas.


REFERENCIAS

  1. Cuille J, Chelle PL. Pathologie animale. La maladie dite tremblant du mouton est-elle inoculable ? Compt Rend Acad Sci (Paris) 1936; 203: 1552-4.

  2. Dearmond SJ, Kretzschmar HA, Prusiner SB. Prion diseases. In: Graham DI, Lantos PL. Eds. Greenfield’s Neuropathology. New York. Arnold 2002: 273-323.

  3. Budka H. Neuropathology of prion diseases. British Medical Bulletin 2003; 66: 121-30.

  4. Cuille J, Chelle PL. Experimental transmission of trembling to the goat. C.R. Séances Acad Sci 1939; 208: 1058-60.

  5. Gordon WS. Vet Rec 1946; 58: 516-20.

  6. Gajdusek DC, Zigas V. Degenerative disease of the central nervous system in New Guinea. N Engl J Med 1957; 257: 974-8.

  7. Will RG, Ironside JW, Hornlimann B, Zeidler M. Creutzfeldt-Jakob disease. Lanced 1996; 347: 65-6.

  8. Goldfarb LG. Kiru: the old epidemic in a new mirror. Microbes Infect 2002; 4: 875-82.

  9. Ingrosso L, Pisani F, Pocchiari M. Transmission of the 263K scrapie strain by the dental route. J Gen Viro 1999; 180 (Pt 11): 3043-7.

  10. Maignien T, Lasmezas CI, Beringue V, Dormont D, Deslys JP. Pathogenesis of the oral route of infection of mice with scrapie and bovine spongiform encephalopathy agents. J Gen Virol 1999; 80 (Pt 11): 3035-42.

  11. Sansonetti PJ, Phalipon AM. Cells as ports of entry for enteroinvasive pathogens: mechanisms of interaction, consequences for the disease process. Semin Immunol 1999; 11: 193-203.

  12. Heppner FL, et al. Transepithelial prion transport by M cells. Nat Med 2001; 7: 976-7.

  13. Prinz M, et al. Lymph nodal prion replication and neuroinvasion in mice devoid of follicular dendritic cells. Proc Natl Acad Sci USA 2002; 99: 919-24.

  14. Beekes M, McBride PA, Baldauf E. Cerebral targeting indicates vagal spread of infection in hámsters fed with scrapie. J Gen Virol 1998; 79 (Pt 3): 601-7.

  15. Bencsik A, Lezmi S, Hunsmann G, Baron T. Close vicinity of PrP expressing cells (FDC) with noradrenergic fibers in healthy sheep spleen. Dev Immunol 2001; 8: 235-41.

  16. Pattison IH. Experiments with scrapie with special reference to the nature of the agent and the patholog of the disease. In Slow, Latent and Temperate Virus infections, NINDB Monogr. Ed Gajdusek CJ, Gibbs A. Washington DC: US Gov. Print. Off. 1965; 2: 249-57.

  17. Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 2001; 24: 519-50.

  18. Collinge J, Sidle KC, Meads J, Ironside J, Hill AF. Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature 1996; 383: 685-90.

  19. Brown P, et al. Iatrogenic Cretuzfeldt-Jakob disease at the millennium. Neurology 2000; 55: 1075-81.

  20. Bernoulli C, et al. Danger of accidental person-to-person transmission of Creutzfeldt-Jakob disease by surgery. Lancet 1977; 1: 478-9.

  21. Zobeley E, Flechsig E, Cozzio A, Enari M, Weissmann C. Infectivity of crapie prions bound to a stainless steel surface. Mol Med 1999; 5: 240-3.

  22. Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 216: 136-44.

  23. Collinge J. Prion diseases of humans and animals : their causes and molecular basis. Annu Rev Neurosci 2001; 24: 519-50.

  24. Prusiner SB. Prions. Proc Natl Acad Sci USA 1998; 95: 13363-83.

  25. Prusiner SB. Molecular biology of prion diseases. Science 1991; 252: 1515-22.

  26. Harries-Jones R, et al. Creutzfeldt-Jakob disease in England and Wales, 1980-1984: a case-control study of potential risk factors. J Neurol Neurosurg Psychiaty 1988; 51: 1113-9.

  27. Pan KM, et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993; 90: 10962-6.

  28. Telling GC, Parchi P, DeArmond SJ, Cortelli P, Montagna P, Gabizon R, et al. Prion Diseases and the BSE Crisis. Science 1997; 278: 245-51.

  29. Stahl N, et al. Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 1993; 32: 1991-2002.

  30. Cohen FE, et al. Structural clues to prion replication. Science 1994; 264: 530-1.

  31. Harris DA. Cellular biology of prion diseases. Clin Microbiol Rev 1999; 12: 429-44.

  32. Wadsworth JD, et al. Strain-specific prion-protein conformation determined by metal ions. Nat Cell Biol 1999; 1: 55-9.

  33. Pattison IH, Jebbett JN. Histopathological similarities between scrapie and cuprizone toxicity in mice. Nature 1971; 230: 115-7.

  34. Hornshaw MP, McDermott JR, Candy JM, Lakey JH. Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides. Biochem Biophys Res Commun 1995; 214: 993-9.

  35. Hornshaw MP, McDermott JR, Candy JM. Copper binding to the Nterminal tandem repeat regions of mammalian and avian prion protein. Biochem Biophys Res Commun 1995; 207: 621-9.

  36. Pauly PC, Harris DA. Copper stimulates endocytosis of the prion protein. J Biol Chem 1998; 273: 33107-10.

  37. DeArmond SJ, et al. Selective neuronal targeting in prion disease. Neuron 1997; 19: 1337-48.

  38. Parchi P, et al. Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease. Ann Neurol 1996; 39: 767-78.

  39. Prusiner SB. Shattuck lecture-neurodegenerative diseases and prions. N Engl J Med 2001; 344: 1516-26.

  40. Wissniewski T, Sigurdsson EM, Aucouturier P, Frangione B. Conformation as a therapeutic target in the prionoses and other neurodegenerative conditions. In Baker HF ed. Mollecular and Cellular pathology in prion disease. Totowa, New Jersey: Human Press 2001: 223-36.

  41. Prusiner SB, Scott MR, DeArmond SJ, Cohen FE. Prion protein biology. Cell 1998; 93: 337-48.

  42. Caughey BW, et al. Secondary structure analysis of the scrapieassociated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 1991; 30: 7672-80.

  43. Safar J, Roller PP, Gajdusek DC, Gibbs CJ Jr. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J Biol Chem 1993; 268: 20276-84.

  44. Donne DG, et al. Structure of the recombinant full-length hámster prion protein PrP(29-231): the N terminus is highly flexible. Proc Natl Acad Sci USA 1997; 94: 13452-7.

  45. Riek R, et al. NMR structure of the mouse prion protein domain PrP(121-321). Nature 1996; 382: 180-2.

  46. Riek R. Hornemann S, Wider G, Glockshuber R, Wuthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett 1997; 413: 282-8.

  47. Peretz D, et al. A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform. J Mol Biol 1997; 273: 614-22.

  48. Bueler H, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993; 73: 1339-47.

  49. Sailer A, Bueler H, Fischer M, Aguzzi A, Weissmann C. No propagation of prions in mice devoid of PrP. Cell 1994; 77: 967-8.

  50. Prusiner SB, et al. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 1990; 63: 673-86.

  51. Scott M, et al. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 1989; 59: 847-57.

  52. Scott M, et al. Transtenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 1989; 59: 847-57.

  53. Chiti F, et al. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci USA 1999; 96: 3590-4.

  54. Zou W, Gambetti P. Modeling of human prions and prion diseases in vitro and in vivo. Drug Discovery Today: Disease Models 2004; 2: 157-64.

  55. Cann AJ. Principles of molecular virology. Elsevier Academic Press USA 1997.



>Revistas >Revista Mexicana de Neurociencia >Año2007, No. 6
 

· Indice de Publicaciones 
· ligas de Interes 






       
Derechos Resevados 2019