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phalopathiesare neurodegenerative diseasescaused by abnormal accumulation of pathogenicisoform the prion protein, which induces theformation of conglomerates protein resistantto degradation. They are also responsible forsynaptic dysfunction, neuronal damage and theclassic symptoms of disease. This membraneprotein is encoded by exon 2 of the gene PRNP,located on the short arm of chromosome 20 andappears to be involved in synaptic transmission,signal transduction, the antioxidant activity ofthe superoxid dismutasa, neuroplasticity andcell survival. One polymorphism at codon 129is associated with differential susceptibility todisease sporadic Creutzfeldt-Jakob disease.Aim: Clinical, pathological and molecularreport on an 58 year-old woman with pathologicaldiagnosis of Creutzfeldt-Jakob sporadicdisease.Methods and results. The clinic courseappears with a behavior depressive disorder withprogressive dementia and symptoms. At theend of the disease, the scenario progressed to aneurological deficit focused on the visual area.The MRI showed nonspecific hyperintensity incortiço-subcortical nucleus in the striatum, theEEG showed patterns of recurrent generalizeddischarges and complex three-phase, the brainbiopsy post-morten showed severe loss of theneuronal population in all the layers, vacuolesin the neuropil, in the neuronal soma and theglial. The analysis of sequence of the gene PRNPidentified homozygotes for methionine atcodon 129. The patient died at 3 months of theonset of symptoms.Conclusions: Epidemiology, clinical courseand paraclinical examinations confirmed thediagnosis of Creutzfeldt-Jakob sporadic.The genotyping for polymorphisms of riskbecomes useful tool to complement throughmolecular diagnosis and to deepen the understandingof the pathophysiology of Creutzfeldt-Jakob disease, both for sporadic forms and forthe new variant. |
