NR AVPD
AU Mandujano,A.; Montes,S.; Guzman,A.; Espinosa,B.; Rembao,D.; Martinez-Cairo,S.; Zenteno,E.; Guevara,J.
TI [Physiopathology of prion diseases]
OT Fisiopatologia de las enfermedades por priones
QU Gaceta Medica de Mexico 2006 Sep-Oct; 142(5): 399-406
PT english abstract; journal article; review
AB 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.
ZR 60
MH Humans; Molecular Biology; Prion Diseases/*physiopathology
AD Facultad de Ciencias, Universidad Autonoma del Estado de Mexico, Mexico.
SP spanisch
PO Mexiko