Scientists have identified a new, longer species of amyloid â-peptide that has the potential to be a new target for the treatment of Alzheimers disease. The research appears as the "Paper of the Week" in the December 3 issue of the Journal of Biological Chemistry, an American Society for Biochemistry and Molecular Biology journal.
One of the characteristic features of Alzheimers disease is the deposition of amyloid â-peptides in the brain. These amyloid â-peptides are derived from a large amyloid precursor protein through a series of cleavage events. Under normal conditions, cleavage first by á-secretase and then by ã-secretase results in a soluble ectodomain, a short peptide called p3, and an intracellular C-terminal domain, none of which are amyloidogenic. Alternatively, amyloid precursor protein can be processed by the enzymes â-secretase and ã-secretase to produce a soluble ectodomain along with the full-length amyloidogenic amyloid â-peptide and the intracellular C-terminal domain.
Although amyloid precursor protein is found in many cells, its normal biological function is not well understood. "It has been suggested that amyloid precursor protein may function as a receptor or growth factor precursor," notes Dr. Xuemin Xu of The University of Tennessee. "Recent studies also suggest that the intracellular C-terminal domain of the amyloid precursor protein may function as a transcription factor."
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