Alzheimer's protein has good side too
The Amyloid Precursor Protein or APP plays a crucial role in Alzheimer’s disease, the most common dementia in the elderly. APP is located on the surface of neurons and is abnormally cleaved in Alzheimer’s disease. This aberrant processing of APP results in excessive formation of a toxic peptide, A-beta, that ends up killing neurons. A team of researchers, led by Professor Jochen Herms at the Center for Neuropathology and Prion Research at the Ludwig-Maximilians-Universität (LMU) Munich, has shown that A-beta causes not only dangerous and pathogenic effects.
Their results, published in the online edition of “The Journal of Neuroscience”, indicate that neurons without APP – and, therefore, without amyloid beta – display changes in their synapses. Synapses are small structures that mediate the communication between neurons. They form the structural basis of complex functions of the brain like learning and memory. “According to our results it is most likely that the A-beta peptide has a normal, physiological role in synaptic formation and function,” says Herms. “For years there has been research on therapies which aim to repress the production of the A-beta peptide altogether. In light of our results those approaches may be very problematic.”
"Synapse Formation and Function is Modulated by the Amyloid Precursor Protein", Priller, Christina; Bauer, Thomas; Mitteregger, Gerda; Krebs, Bjarne; Kretzschmar, Hans; Herms, Jochen, in "The Journal of Neuroscience"
Professor Dr. Jochen Herms
Center for Neuropathology und Prion Research at LMU Munich
Tel.: +49 (0)89 / 2180 - 78010
Fax: +49 (0)89 / 2180 - 78037