2026-04-17T20:41:59Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/1545392025-11-20T15:02:56Zcom_2072_1057col_2072_478916col_2072_478917col_2072_478929

00925njm 22002777a 4500 dc Zafar, Saima author Shafiq, Mohsin author Younas, Neelam author Schmitz, Matthias author Ferrer, Isidro (Ferrer Abizanda) author Zerr, Inga author 2020-03-31T11:58:35Z 2020-03-31T11:58:35Z 2017 2020-03-31T11:58:36Z Rapidly progressive Alzheimer's disease (rpAD) is a variant of AD distinguished by a rapid decline in cognition and short disease duration from onset to death. While attempts to identify rpAD based on biomarker profile classifications have been initiated, the mechanisms which contribute to the rapid decline and prion mimicking heterogeneity in clinical signs are still largely unknown. In this study, we characterized prion protein (PrP) expression, localization, and interactome in rpAD, slow progressive AD, and in non-dementia controls. PrP along with its interacting proteins were affinity purified with magnetic Dynabeads Protein-G, and were identified using Q-TOF-ESI/MS analysis. Our data demonstrated a significant 1.2-fold decrease in di-glycosylated PrP isoforms specifically in rpAD patients. Fifteen proteins appeared to interact with PrP and only two proteins3/4histone H2B-type1-B and zinc alpha-2 protein3/4were specifically bound with PrP isoform isolated from rpAD cases. Our data suggest distinct PrP involvement in association with the altered PrP interacting protein in rpAD, though the pathophysiological significance of these interactions remains to be established. Keywords: Aldolase A, Alzheimer's disease, co-immunofluorescence, co-immunoprecipitation, histone, myelin P2, peroxiredoxin 1, prion, proteomics, synapsin, tubulin, zinc Malaltia d'Alzheimer Patologia Metabolisme Cervell Malaltia de Creutzfeldt-Jakob Alzheimer's disease Pathology Metabolism Brain Creutzfeldt-Jakob disease Prion protein interactome: identifying novel targets in slowly and rapidly progressive forms of alzheimer's disease