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Extracellular Amyloid Deposits in Alzheimer's and Creutzfeldt-Jakob Disease: Similar Behavior of Different Proteins

N. Jankovska, T. Olejar, R. Matej

. 2020 ; 22 (1) : . [pub] 20201222

Jazyk angličtina Země Švýcarsko

Typ dokumentu časopisecké články, přehledy

Perzistentní odkaz   https://www.medvik.cz/link/bmc21011709

Grantová podpora
VFN64165 Ministry of Health, Czech Republic (Conceptual development of research organization, General University Hospital in Prague)
TN64190 Ministry of Health, Czech Republic (Conceptual development of research organization, Thomayer Hospital in Prague)
NV19-04-00090 Grants Agency of the Ministry of Health
NV18-04-00179 Grants Agency of the Ministry of Health
Q27/LF1 Charles University - Project Progress
142120 Charles University (Project GAUK)

Neurodegenerative diseases are characterized by the deposition of specific protein aggregates, both intracellularly and/or extracellularly, depending on the type of disease. The extracellular occurrence of tridimensional structures formed by amyloidogenic proteins defines Alzheimer's disease, in which plaques are composed of amyloid β-protein, while in prionoses, the same term "amyloid" refers to the amyloid prion protein. In this review, we focused on providing a detailed didactic description and differentiation of diffuse, neuritic, and burnt-out plaques found in Alzheimer's disease and kuru-like, florid, multicentric, and neuritic plaques in human transmissible spongiform encephalopathies, followed by a systematic classification of the morphological similarities and differences between the extracellular amyloid deposits in these disorders. Both conditions are accompanied by the extracellular deposits that share certain signs, including neuritic degeneration, suggesting a particular role for amyloid protein toxicity.

Citace poskytuje Crossref.org

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