Share
Blog
Cite
Print
Email
BookmarkScienceDaily (Oct. 9, 2005) — 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 Aß. The mechanisms underlying the production ofAß are complex, but it is known that this peptide is derived from a larger precursor known as the amyloid precursor protein (AßPP). Interestingly, and of potential therapeutic significance, AßPPcan be processed within the cell via different pathways, some of which preclude the formation of the toxic peptideAß.
See also:
Cellular stress has been associated with the disease and may impact upon AßPP processing and, consequently, toxic amyloid peptide termedAß production. University of Aveiro researchers, in their recent article 'Cellular stress affects phosphorylation dependent AßPP 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 (AßPP) 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.
