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http://dx.doi.org/10.3810/pgm.2002.02.1117 | DOI Listing |
Cureus
November 2024
Acute Medicine, Peterborough City Hospital, Peterborough, GBR.
Creutzfeldt-Jakob disease (CJD) is a fatal neurodegenerative disorder that leads to rapid cognitive decline, dementia, and neurological deterioration. CJD has several forms, including sporadic CJD (sCJD), which accounts for most cases, and variant CJD (vCJD), linked to exposure to bovine spongiform encephalopathy (BSE or mad cow disease). The disease is caused by abnormal prion proteins, which damage the brain and lead to death.
View Article and Find Full Text PDFPLoS One
October 2024
Department of Microbiology, Immunology and Pathology, Prion Research Center, College of Veterinary Medicine and Biomedical Sciences, Colorado State University, Fort Collins, Colorado, United States of America.
Zoonotic transmission of bovine spongiform encephalopathy or mad cow disease, by presumed consumption of infected beef, has increased awareness of the public health risk associated with prion diseases. Chronic wasting disease (CWD) affects moose, elk, and deer, all of which are frequently consumed by humans. Clear evidence of CWD transmission to humans has not been demonstrated, yet, establishing whether CWD prions are present in muscle tissue preferentially consumed by humans is of increasing interest.
View Article and Find Full Text PDFPhys Chem Chem Phys
October 2024
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, USA.
Transmissible spongiform encephalopathies (or prion diseases) such as Creutzfeldt-Jacob disease, mad cow disease, and scrapie are characterized by accumulation in the brain of misfolded prion protein aggregates (PrP) that have properties of amyloid fibrils. Given that transition metal ions, such as copper and zinc, appear to be important for physiological functions of cellular PrP (PrP) as well as for prion disease pathogenesis, exploring their role in the protein aggregation process is of considerable interest. Copper(II) in particular is well-known to bind to the four tandem octapeptide repeats (PHGGGWGQ) located in the N-terminal region of PrP (human PrP amino acids 60-91), as well as to additional histidine binding sites outside the octarepeat region with distinct binding modes depending on Cu concentration.
View Article and Find Full Text PDFBrain Sci
April 2024
Institute of Medical Biochemistry Leopoldo de Meis and National Institute of Science and Technology for Structural Biology and Bioimaging, Federal University of Rio de Janeiro, Rio de Janeiro 21941-902, RJ, Brazil.
Transmissible Spongiform Encephalopathies (TSEs), including prion diseases such as Bovine Spongiform Encephalopathy (Mad Cow Disease) and variant Creutzfeldt-Jakob Disease, pose unique challenges to the scientific and medical communities due to their infectious nature, neurodegenerative effects, and the absence of a cure. Central to the progression of TSEs is the conversion of the normal cellular prion protein (PrPC) into its infectious scrapie form (PrPSc), leading to neurodegeneration through a complex interplay involving the immune system. This review elucidates the current understanding of the immune response in prion diseases, emphasizing the dual role of the immune system in both propagating and mitigating the disease through mechanisms such as glial activation, cytokine release, and blood-brain barrier dynamics.
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