Transglutaminase Induces Protofibril-like Amyloid β-Protein Assemblies That Are Protease-resistant and Inhibit Long-term Potentiation

• Published in: The Journal of biological chemistry Vol. 283; no. 24; pp. 16790 - 16800
• Main Authors: Hartley, Dean M., Zhao, Chaohui, Speier, Austin C., Woodard, Gavitt A., Li, Shaomin, Li, Zongli, Walz, Thomas
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 13.06.2008; American Society for Biochemistry and Molecular Biology
• Subjects: Alzheimer Disease - metabolism; Amyloid beta-Peptides - metabolism; Animals; Cross-Linking Reagents - chemistry; Cross-Linking Reagents - pharmacology; Disease Progression; GTP-Binding Proteins - metabolism; Guinea Pigs; Hippocampus - metabolism; Humans; Insulysin - chemistry; Long-Term Potentiation; Mice; Neprilysin - chemistry; Peptide Hydrolases - metabolism; Peptides - chemistry; Transglutaminases - metabolism

An increasing body of evidence suggests that soluble assemblies of amyloid β-protein (Aβ) play an important role in the initiation of Alzheimer disease (AD). In vitro studies have found that synthetic Aβ can form soluble aggregates through self-assembly, but this process requires Aβ concentrations 1...