Mandujano A, Montes S, Guzmán A, Espinosa B, Rembao D, Martínez-Cairo S, Zenteno E, Guevara J

Language: Spanish
References: 60
Page: 399-406
PDF size: 188.72 Kb.

ABSTRACT

Prion diseases are a group of degenerative disorders characterized by being progressive, fast growing, and fatal, they affect humans and animals. Due to their physiopathogeny, these disorders can be sporadic, genetic, or infectious. Prions are cellular proteins that lack nucleic acids; they are not viruses or microorganisms. Prions induce neuronal death, brain spongiosis, which are a hallmark of these diseases, as well as amyloid prion protein plaque aggregates. Although the causes that favor pathogenic prion proteins remain uncertain, it is possible that conformational changes of the prion protein allow them to create copies of themselves to form aggregates and induce neuronal death. Other theories suggest that quantitative and qualitative changes in the glycosylation pattern induce the pathological prion form. The latter allows to explain some of their interactions and to understand better the conformational changes and the physico-chemical properties of the prion protein. We review some of the first biological functions (as a transporter of Cu²⁺ ions) that have been described to this molecule. The present review focuses on different aspects of prion diseases aimed at understanding better their physiopathogenic characteristics.

REFERENCES

1. Weissmann C. Molecular genetics of Transmisible Spongiform Encephalopathies. J Biol Chem 1999;274;1:3-6.

2. Weissmann C. The state of the prion. Nat Rev Microbiol 2004;11:861-871.

3. Belay ED. Transmissible spongiform encephalopathies in humans. Ann Rev Microbiol 1999;53:283-314.

4. Bendheim PE, Bockman MP, McKinley MP, Kingsbury DT, Prusiner S. Scrapie and Creutzfedtl-Jakob disease prion proteins share physical properties and antigenic determinants. Proc Natl Acad Sci USA 1985;82:997-1001.

5. Kovacs GG, Kalev O, Budka H. Contribution of neuropathology to the understanding of human prion disease. Folia Neuropathol 2004;42 Suppl A: 69-76.

6. Prusiner S. Novel Proteinaceous Infectious Particles cause Scrapie. Science 1982;216:136-144.

7. Mallucci G, Collinge J. Update on Creutzfeldt-Jakob disease. Curr Opin Neurol 2004;6:641-647.

8. Croes EA. Therapeutic approaches in treating Creutzfeldt-Jakob disease - what does the future hold? Expert Opin Pharmacother 2004;11:2391-2396.

9. Coria BF. Demencias por priones. En: Alberca R, López Pousa YS. Enfermedad de Alzheimer y otras demencias. Médica Panamericana. España. 2002.

10. Weihl CC, Ross RP. Enfermedad de Creutzdeldt-Jakob, nueva variedad de la enfermedad de Creutzfeldt-Jakob, y la encefalopatía espongiforme bovina. En: Clínicas Neurológicas de Norteamérica. Infecciones del Sistema Nervioso Central. Vol. 4. McGraw-Hill Interamericana. México 1998.

11. Liemann S,.Glockshuber R. Influence of amino acid substitutions related to inherited prion disease on the thermodynamic stability of the cellular prion protein. Biochem 1999;38:3258-3267.

12. Kitamoto T, Lizuka R, Tateishi YJ. An amber mutation of prion protein in Gerstmann-Straussler-Scheinker syndrome with mutant PrP plaques. Biochem Biophys Res Commu 1993;192:525-531.

13. Liberski PP, Gajdusek DC. Kuru: Forty years later, a historical note. Brain Pathol 1997;7:555-560.

14. Hainfellner JA, Liberski PP, Guiroy DC, Cervenakova L, Brown P, Gajdusek DC, et al. Pathology and Inmunocytochemistry of a Kuru Brain. Brain Pathol 1997;7:547-553.

15. Aguzzi A, Bitifler T, Klein M, Brandner S, Raeber A, Flechsing E, Weissmann C. Neurotoxicity and Neuroinvasiveness of prions. Brain Pathol 1997;7:1137-1138.

16. Masters CL, Beyreuther K. Tracking turncoat prion proteins. News and Views. Nature 1997;388:228-229.

17. Sánchez A, Guzmán A, Ortiz A, Rembao D, Espinosa B, Zenteno E, Guevara J. Toluidine blue-O staining of prion protein deposits. Histochem Cell Biol 2001;116:519-524.

18. Prusiner S. El prion en la patología. Investigación y Ciencia. 1995; Marzo: 14-21.

19. Aranda A. Possible cell-free Prion replication. Med Hypotheses 1992;38:249-251.

20. Tatzelt J, Winklhofer KF. Folding and misfolding of the prion protein in the secretory pathway. Amyloid 2004;3:162-172.

21. Zhang H, Stockel J, Mehlhorn I, Groth D, Baldwin MA, Prusiner S, Lames TL, Cohen F. Physical studies of conformational plasticity in a recombinant Prion protein. Biochem 1997;36:3543-3553.

22. Kuwata K, Li H, Yamada H, Legname G, Prusiner S, Akasaka K, James T. Locally disordered conformer of the hamster prion protein: A crucial intermediate to PrPSc? Biochem 2002;41:12277-12283.

23. Brown DR. Prion and prejuice: normal protein and the synapse. Trends of Neuroscience 2001;24:85-90.

24. Horiuchi M, Yamazaki N, Ikeda T, Ishiguro N, Shinagawa M. A cellular form of prion protein (PrPC) exists in many non-neuronal tissues of sheep. J Gen Virol 1995;76:2583-2587.

25. Brockes J. Topics in prion cell biology. Current Opinion in Neurobiol 1999;9:571-577.

26. Hölscher C, Bach UC, Dobberstein B. Prion Protein Contains a SecondEndoplasmic Reticulum Targeting Signal Sequence Located at its C Terminus. J Biol Chem 2001;276:13388-13394.

27. Stahl N, Baldwin MA, Burlingame A, Prusiner S. Identification of Glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochem 1990;29:8879-8884.

28. Nandi PK, Leclerc E, Marc D. Unusual property of prion protein unfolding in neutral salt solution. Biochem 2002;41:11017-11024.

29. Zahn R, Liu A, Lührs T, Riek R, Von Schroetter C, López F, Billeter M, Calzolai L, Wider G, Wüthrich K. NMR solution structure of human prion protein. Proc Natl Acad Sci USA 1999;97:145-150.

30. Pan KM, Baldwin MA, Nguyen J, Gassey M, Serban A. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993;90:10962-10966.

31. Bell JE, Ironside JW. Neuropathology of spongiform encephalopathies in humans. Brain Med Bull 1993;49:738-777.

32. DebBurman S, Raymond G, Caughey B, Lindquist A. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc Natl Acad Sci USA 1997;94:13938-13943.

33. Cohen FE. Protein misfolding and prion diseases. J Mol Biol 1999;293:313-320.

34. Fernandez-Escamilla AM, Rousseau F, Schymkowitz J, Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat Biotechnol 2004;10:1302-1306.

35. Castilla J, Hetz C, Soto C. Molecular mechanisms of neurotoxicity of pathological prion protein. Curr Mol Med 2004;4:397-403.

36. Jarrett J, Lansbury PT. Seeding “One-Dimensional crystallization” of amyloid A pathogenic mechanism in Alzheimer´s disease and Scrapie? Cell 1993;73:1055-1058.

37. Georgieva D, Koker M, Redecke L, Perbandt M, Clos J, Bredehorst R, Genov N, Betzel C. Oligomerization of the proteolytic products is an intrinsic property of prion proteins. Biochem Biophys Res Commun 2004;323:1278-1286.

38. Gasset M. El prion, una herejía científica en la vida cotidiana. Fronteras de la Ciencia y Tecnología (Francia) 1996;13:4-6.

39. Satheeshkumar KS, Murali J, Jayakumar R. Assemblages of prion fragments: novel model systems for understanding amyloid toxicity. J Struct Biol 2004;148:176-193.

40. Kocisko A, Come H, Priola A. Cell free formation of protease resistant prion protein. Nature 1994;370:471-474.

41. Guevara J, Espinosa B, Zenteno E, Vázquez L, Luna J, Perry G, Mena R. Altered glycosylation pattern of proteins in Alzheimer Disease. J. Neuropathol Exp Neurol 1998;57:905-914.

42. Espinosa B, Guevara J, Hernández P, Slomianny MC, Guzmán A, Martínez- Cairo S, Zenteno E. Characterization of an O-glycosylated plaque-associated protein from Alzheimer’s disease brain. J Neuropathol Exp Neurol 2003;62:34-41.

43. Clausen H, Benneth EP. One family de UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferases control the initiation of mucin-type O-linked glycosylation. Glycobiology 1996;6:635-646.

44. Rudd PM, Endo T, Colominas C, Groth D, Wheeler SF, Harvey DJ, et al. Glycosylation differences between the normal and pathogenic prion protein isoforms. Proc Natl Acad Sci USA 1999;96:13044-13049.

45. Rudd PM, Wormald MR, Wing DR, Prusiner SB and Dwek RA. Prion glycoprotein: Structure, dynamics and roles for sugars. Biochemistry 2001;40:3759-3766.

46. Chen PY, Lin CC, Chang YT, Lin SC, Chan SI. One O-linked sugar can affect the coil-to-beta structural transition of the prion peptide. Proc Natl Acad Sci USA 2002;99:12633-12638.

47. Quaglio E, Chiesa R, Harris A. Copper converts the Cellular prion protein into a protease-resistant species than is distinct from the scrapie isoform. J Biol Chem 2001;276:11432-11438.

48. Kuczius T, Buschmann A, Zhang W, Karch H, Becker K, Peters G, Groschup MH. Cellular prion protein acquires resistance to proteolytic degradation following copper ion binding. Biol Chem 2004;385:739-747.

49. Martins VR, Brentani RR. The biology of the cellular prion protein. Neurochem International 2002;41:353-355.

50. Dormont D. Prion diseases: pathogenesis and public health concerns. FEBS Letters 2002;529:17-21.

51. Cashman NR, Caughey B. Prion diseases, close to effective therapy?. Nat Rev Drug Discov 2004;10:874-884.

52. Brown P. Drug therapy in human and experimental transmissible spongiform encephalopathy. Neurology 2002;58:1720-1725.

53. Mallucci G, Collinge J. Rational targeting for prion therapeutics. Nat Revs 2005;6:23-34.

54. Rossi G, Salmona M, Forloni G, Bugiani O, Tagliavini F. Therapeutic approaches to prion diseases. Clin Lab Med 2003;23:187-208.

55. Ramasamy I, Law M, Collins S, Brooke F. Organ distribution of prion proteins in variant Creutzfeldt-Jakob disease. Lancet Infect Dis 2003;3:214-222.

56. Hopkin M. Fears grow as blood stocks pass on prion undetected. Nature 2004; 430:712.

57. Peden AH, Head MW, Ritchie DI, Bell JE, Ironside JW. Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 2004;264:527-529.

58. Van Everbroeck B, Dewulf E, Pals P, Lubke U, Martin JJ, Cras P. The role of cytokines, astrocytes, microglia and apoptosis in Creutzfeldt-Jakob disease. Neurobiol Aging. 2002;23:59-64.

59. Perry VH, Cunningham C, Boche D. Atypical inflammation in the central nervous system in prion disease. Curr Opin Neurol. 2002;15:349-354.

60. Perry VH. The influence of systemic inflammation on inflammation in the brain: implications for chronic neurodegenerative disease. Brain Behav Immun. 2004; 18:407-413.