In a research report recently published in the Journal of Alzheimer's Disease, published by IOS Press, a research group from the International School for Advanced Studies (ISAS\SISSA) in Trieste (Luisa Fasulo, Gabriele Ugolini e Antonino Cattaneo) showed that a processed form of tau protein induces neuronal death by apoptosis (programmed cell death) when expressed in cultured rat hippocampal neurons.
Pathological changes in the microtubule associated protein tau are a major hallmark of the human dementias collectively defined as tauopathies, including Alzheimer’s disease (AD). In Fronto-Temporal Dementia with Parkinsonism linked to Chromosome 17 (FTDP-17), several mutations in the tau gene were identified showing that primary malfunction of tau can lead to neurodegeneration. Such findings shed new light on the role of post-translational modifications of tau protein occurring in other tauopathies (such as AD), including aberrant proteolysis. In AD, tau protein aggregates in intraneuronal deposits known as “neurofibrillary tangles” (NFT), one of the two hallmarks of the disease. Tau molecules normally associate to microtubules (major cytoskeletal structures); in AD, tau proteins dissociate from microtubules and aggregate into NFTs.