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by AlzheimersSupport Staff
June 7, 2000
Summary
Scientists have ruled out certain protein developments as the primary catalyst for brain deterioration.
An investigation studied the aging of Abeta, a protein tied to Alzheimer’s disease, during tests of its chemical makeup. The study found that unusual structural alterations occurred when Abeta came into contact with abnormal deposits of starchy substances called amyloids , which are present in patients with Alzheimer’s disease.
Although scientists agree that changes in Abeta trigger neurodegenerative processes such as Alzheimer’s and make them more susceptible to the effects of toxic amyloid substances, they could not definitively say that the resulting chemical changes were related to any one of the specific tests performed on Abeta.
FASEB J 2000 Jun;14(9):1255-1263
Protein aging hypothesis of Alzheimer disease.
Orpiszewski J, Schormann N, Kluve-Beckerman B, Liepnieks JJ, Benson MD
Aprot Corporation, Carmel, Indiana 46082-3813, USA. Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA. Richard L. Roudebush Veterans Affairs Medical Center, Indianapolis, Indiana 46202, USA.
Alzheimer’s disease (AD), the most common form of aging-related neurodegenerative disorders, is associated with formation of fibrillar deposits of amyloid beta-protein (Abeta). While the direct involvement of Abeta in AD has been well documented, the relations between Abeta production, amyloid formation, and neurodegeneration remain unknown. We propose that AD is initiated by a protein aging-related structural transformation in soluble Abeta. We hypothesize that spontaneous chemical modification of aspartyl residues in Abeta to transient succinimide induces a non-native conformation in a fraction of soluble Abeta, rendering it amyloidogenic and neurotoxic. Conformationally altered Abeta is characterized by increased stability in solution and the presence of a non-native beta-turn that determines folding of Abeta in solution and the structure of Abeta subunits incorporated into amyloid fibrils. While the soluble 'non-native' Abeta is both the factor triggering the neurodegenerative cascade and the precursor of amyloid plaques, these two events result from interaction of Abeta with different sets of cellular components and need not coincide in space and time. Extensive literature data and experimental evidence are provided in support of this hypothesis.-Orpiszewski, J., Schormann, N., Kluve-Beckerman, B., Liepnieks, J. J., Benson, M. D. Protein aging hypothesis of Alzheimer disease.
PMID: 10834947
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