Home > Publications Database > Tau neurotoxicity and rescue in animal models of human Tauopathies. |
Journal Article (Review Article) | DZNE-2020-04704 |
;
2016
Current Biology
Philadelphia, Pa.
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Please use a persistent id in citations: doi:10.1016/j.conb.2015.09.004
Abstract: Pathological Tau is a hallmark of various neuronal disorders and spreads in the brain of Alzheimer patients in a well-defined manner. Beside Tau's main function in stabilizing microtubules for axonal transport, a variety of novel functions for neurons and glia have emerged recently. Tau regulates the susceptibility to hyperexcitation and plays a role in neuron-glia contact formation. Studies implicate soluble oligomeric species of Tau, rather than insoluble aggregates, as more detrimental to proper neuronal function. Tau is not exclusively intracellular; instead Tau can be released into the extracellular space. This has led to the hypothesis of a prion-disease like mechanism to explain the stereotypical progression of Tau. Targeting pathological Tau with antibodies or aggregation inhibitors may help to prevent pathology.
Keyword(s): Animals (MeSH) ; Antibodies: pharmacology (MeSH) ; Brain: metabolism (MeSH) ; Brain: physiopathology (MeSH) ; Disease Models, Animal (MeSH) ; Disease Susceptibility (MeSH) ; Humans (MeSH) ; Mice (MeSH) ; Presynaptic Terminals: metabolism (MeSH) ; Protein Aggregates: drug effects (MeSH) ; Protein Aggregation, Pathological: metabolism (MeSH) ; Protein Aggregation, Pathological: physiopathology (MeSH) ; Tauopathies: metabolism (MeSH) ; Tauopathies: physiopathology (MeSH) ; tau Proteins: metabolism (MeSH) ; Antibodies ; Protein Aggregates ; tau Proteins
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