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A new species of amyloid peptide

to cell death, including activation of cell death programs, oxidation of lipids and disruption of cell membranes, an inflammatory response, and possibly neurofibrillary tangle formation, which is a close correlate of neuron loss. Therefore, the problem of production, accumulation, and clearance of amyloid β-peptide in the brain emerges as one of the possible rational approaches for the treatment of Alzheimer's disease.

Generally, amyloid β-peptides are around 39-43 amino acid long. Studies have shown that the longer amyloid β-peptides are more amyloidogenic and more pathogenic than the shorter ones. Now, Dr. Xu and his colleagues have discovered a new species of amyloid β-peptide that is 46 amino acids long, called Aβ46. This Aβ46 peptide is produced by γ-secretase at a novel cleavage site, the ζ-site. This site also happens to be the site of a mutation found in early-onset familial Alzheimer's disease called the APP717 or London mutation.

"Another well characterized Alzheimer's disease-linked amyloid precursor protein mutation, the Swedish mutation, also occurs at a major cleavage site, the β-cleavage site at the N-terminus of amyloid β-peptide," adds Dr. Xu. "Studies have shown that Swedish mutation at the β-cleavage site makes the amyloid precursor protein more susceptible to β-secretase activity. The finding that ζ-cleavage site is the APP717 mutation site suggests that the APP717 mutation may cause enhanced production of the longer amyloid β-peptide, Aβ42, by influencing the ζ-cleavage. Therefore, this finding may open a new avenue for studying the mechanism by which APP717 mutations cause enhanced production of the longer amyloid β-peptide."

Dr. Xu and his colleagues also discovered that γ-secretase cleavage at the new ζ-site is specifically inhibited by compounds known as transition state analogs, but is less
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Contact: Nicole Kresge
nkresge@asbmb.org
301-634-7415
American Society for Biochemistry and Molecular Biology
26-Nov-2004


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