A molecular basis for selective therapeutic intervention in Alzheimer's disease
Alzheimer's disease, a complex neurological disorder, has as one of its hallmarks the presence of senile plaques in the brains of affected individuals. These senile plaques are rich in a toxic amyloid peptide termed Aâ. The mechanisms underlying the production of Aâ are complex, but it is known that this peptide is derived from a larger precursor known as the amyloid precursor protein (AâPP). Interestingly, and of potential therapeutic significance, AâPP can be processed within the cell via different pathways, some of which preclude the formation of the toxic peptide Aâ.
Cellular stress has been associated with the disease and may impact upon AâPP processing and, consequently, toxic amyloid peptide termed Aâ production. University of Aveiro researchers, in their recent article 'Cellular stress affects phosphorylation dependent AâPP processing' by A. G. Henriques et al, published in the Journal of Alzheimer's Disease, Vol. 7, pp 201-212, addressed how the non-toxic amyloid precursor protein (AâPP) processing was affected by cellular stress.
The research was carried out in the recently established Neuroscience Laboratory of the University of Aveiro, headed by Prof. Odete A. B. da Cruz e Silva. The University of Aveiro was created in 1973 and is generally recognized as one of the most dynamic universities in Portugal, being a member of the European Consortium of Innovative Universities. The university prides itself in the quality of its research groups and, in addition to its traditional strength in areas such as Material Science, Signal Transduction, Environment and Marine Studies, Electronics and Telematics, Telecommunications and Telemedicine, it has recently promoted the development of internationally competitive research in Biomolecular and Health Sciences.
Source: Eurekalert & othersLast reviewed: By John M. Grohol, Psy.D. on 21 Feb 2009
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