NDLI: The Alzheimer disease protective mutation A2T modulates kinetic and thermodynamic properties of amyloid-ß (Aß) aggregation.

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The Alzheimer disease protective mutation A2T modulates kinetic and thermodynamic properties of amyloid-ß (Aß) aggregation.

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The Alzheimer disease protective mutation A2T modulates kinetic and thermodynamic properties of amyloid-ß (Aß) aggregation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Benilova, Iryna Rousseau, Frederic De Strooper, Bart Ramakers, Meine Bartic, Carmen Gallardo, Rodrigo Ungureanu, Andreea-alexandra Castillo Cano, Virginia Snellinx, An Schymkowitz, Joost
Description	Author Affiliation: Benilova I ( From the VIB Center for the Biology of Disease, the Center for Human Genetics and Leuven Institute for Neurodegenerative Diseases, University of Leuven.); Gallardo R ( the VIB Switch Laboratory, the Switch Laboratory, Department of Cellular and Molecular Medicine.); Ungureanu AA ( Laboratory of Solid State Physics and Magnetism, University of Leuven, 3000 Leuven, and Imec, 3001 Leuven, Belgium.); Castillo Cano V ( the VIB Switch Laboratory, the Switch Laboratory, Department of Cellular and Molecular Medicine.); Snellinx A ( From the VIB Center for the Biology of Disease, the Center for Human Genetics and Leuven Institute for Neurodegenerative Diseases, University of Leuven.); Ramakers M ( the VIB Switch Laboratory, the Switch Laboratory, Department of Cellular and Molecular Medicine.); Bartic C ( Laboratory of Solid State Physics and Magnetism, University of Leuven, 3000 Leuven, and Imec, 3001 Leuven, Belgium.); Rousseau F ( the VIB Switch Laboratory, the Switch Laboratory, Department of Cellular and Molecular Medicine.); Schymkowitz J ( the VIB Switch Laboratory, the Switch Laboratory, Department of Cellular and Molecular Medicine.); De Strooper B ( From the VIB Center for the Biology of Disease, the Center for Human Genetics and Leuven Institute for Neurodegenerative Diseases, University of Leuven, bart.destrooper@cme.vib-kuleuven.be.)
Abstract	Missense mutations in alanine 673 of the amyloid precursor protein (APP), which corresponds to the second alanine of the amyloid ß (Aß) sequence, have dramatic impact on the risk for Alzheimer disease; A2V is causative, and A2T is protective. Assuming a crucial role of amyloid-Aß in neurodegeneration, we hypothesized that both A2V and A2T mutations cause distinct changes in Aß properties that may at least partially explain these completely different phenotypes. Using human APP-overexpressing primary neurons, we observed significantly decreased Aß production in the A2T mutant along with an enhanced Aß generation in the A2V mutant confirming earlier data from non-neuronal cell lines. More importantly, thioflavin T fluorescence assays revealed that the mutations, while having little effect on Aß42 peptide aggregation, dramatically change the properties of the Aß40 pool with A2V accelerating and A2T delaying aggregation of the Aß peptides. In line with the kinetic data, Aß A2T demonstrated an increase in the solubility at equilibrium, an effect that was also observed in all mixtures of the A2T mutant with the wild type Aß40. We propose that in addition to the reduced ß-secretase cleavage of APP, the impaired propensity to aggregate may be part of the protective effect conferred by A2T substitution. The interpretation of the protective effect of this mutation is thus much more complicated than proposed previously.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	45
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-11-07
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alzheimer Disease Genetics Amyloid Beta-Peptides Chemistry Amyloid Beta-Protein Precursor Peptide Fragments Metabolism Amyloid Precursor Protein Secretases Animals Brain Cell Culture Techniques Cell Line Cricetinae Disease Models, Animal Kinetics Mice Mice, Inbred C57BL Mutagenesis Mutation Neurons Cytology Solubility Thermodynamics Thiazoles Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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