KANNO is a new human blood group that was recently discovered. The KANNO antigen shares the gene with the prion protein and the prion protein E219K polymorphism determines the presence or absence of the KANNO antigen and the development of anti-KANNO alloantibodies. These alloantibodies specifically react with prion proteins, which serve as substrates for conversion into pathological isoforms in some prion diseases and may serve as effective targets for resisting prion infection. These findings establish a potential link between the KANNO blood group and human prion disease via the prion protein E219K polymorphism. We reviewed the interesting correlation between the human gene's E219K polymorphism and the prion proteins it expresses, as well as human red blood cell antigens. Based on the immune serological principles of human blood cells, the prion protein E219K polymorphism may serve as a foundation for earlier molecular diagnosis and future drug development for prion diseases.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11266091 | PMC |
http://dx.doi.org/10.3389/fneur.2024.1392984 | DOI Listing |
Alzheimers Dement
December 2024
Colorado State University, Fort Collins, CO, USA.
Background: In tauopathies, the protein tau misfolds into a b-sheet conformation that self-templates and spreads throughout the brain causing progressive degeneration. Biological and structural data have shown that the shape, or strain, that tau adopts when it misfolds determines which disease a patient will develop. We previously used HEK293T cells expressing TauRD-YFP to show that tau strain formation is isoform-specific.
View Article and Find Full Text PDFAlzheimers Dement
December 2024
Peking University, Beijing, Beijing, China.
Background: Prion diseases are a group of neurodegenerative diseases associated with prion protein. The disease can be caused by mutations in the PRNP gene, the gene that encodes prion protein. An octapeptide repeat on the N-terminus of prion protein plays an important role in normal intercellular function of prion protein.
View Article and Find Full Text PDFAlzheimers Dement
December 2024
Ecole polytechnique - CNRS UMR7654, Palaiseau, Ile-de-France, France; Université Paris Cité - Inserm UMR-S1124, Paris, Ile-de-France, France.
Alzheimer's disease (AD) is the most common dementia in humans that today concerns 50 million individuals worldwide and will affect more than 100 million people in 2050. Except for familial AD cases (<5% of AD patients) for which AD pathology connects to mutations in critical genes involved in the processing of the amyloid precursor protein into neurotoxic Aß peptides, it remains unknown what provokes the overproduction and deposition of Aß peptides in the brain of sporadic AD cases (>95% of AD patients). Some nanosized materials, e.
View Article and Find Full Text PDFAlzheimers Dement
December 2024
University of Texas Medical Branch, Galveston, TX, USA.
Background: Tauopathies, including Alzheimer's Disease and Frontotemporal Dementia, are characterized as intracellular lesions composed of aggregated tau proteins. Soluble tau oligomers are shown to be one of the most toxic species and are responsible for the spread of tau pathology. Recent studies have found that several proteins such as amyloid b, a-synuclein, and TDP-43 can aggregate tau.
View Article and Find Full Text PDFAlzheimers Dement
December 2024
University of Malaga/CIBERNED/IBIMA, Málaga, Spain.
Background: Alzheimer's Disease (AD) is a neurodegenerative proteinopathy in which Aβ can misfold and aggregate into seeds that structurally corrupt native proteins, mimicking a prion-like process. These amyloid aggregation and propagation processes are influenced by three factors: the origin of the Aβ seed, time of incubation and host. However, the mechanism underlying the differential effect of each factor is poorly known.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!