Alzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity
Alzheimer's disease (AD) is the most common dementia affecting tens of million people worldwide. The primary neuropathological hallmark in AD is amyloid plaques composed of amyloid-β peptide (Aβ). Several familial mutations found in Aβ sequence result in early onset of AD. Previous studies show...
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Published in | PloS one Vol. 12; no. 3; p. e0174561 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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Public Library of Science
31.03.2017
Public Library of Science (PLoS) |
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Abstract | Alzheimer's disease (AD) is the most common dementia affecting tens of million people worldwide. The primary neuropathological hallmark in AD is amyloid plaques composed of amyloid-β peptide (Aβ). Several familial mutations found in Aβ sequence result in early onset of AD. Previous studies showed that the mutations located at N-terminus of Aβ, such as the English (H6R) and Tottori (D7N) mutations, promote fibril formation and increase cytotoxicity. However, A2T mutant located at the very N-terminus of Aβ shows low-prevalence incidence of AD, whereas, another mutant A2V causes early onset of AD. To understand the molecular mechanism of the distinct effect and develop new potential therapeutic strategy, here, we examined the effect of full-length and N-terminal A2V/T variants to wild type (WT) Aβ40 by fibrillization assays and NMR studies. We found that full-length and N-terminal A2V accelerated WT fibrillization and induced large chemical shifts on the N-terminus of WT Aβ, whereas, full-length and N-terminal A2T retarded the fibrillization. We further examined the inhibition effect of various N-terminal fragments (NTFs) of A2T to WT Aβ. The A2T NTFs ranging from residue 1 to residue 7 to 10, but not 1 to 6 or shorter, are capable to retard WT Aβ fibrillization and rescue cytotoxicity. The results suggest that in the presence of full-length or specific N-terminal A2T can retard Aβ aggregation and the A2T NTFs can mitigate its toxicity. Our results provide a novel targeting site for future therapeutic development of AD. |
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AbstractList | Alzheimer's disease (AD) is the most common dementia affecting tens of million people worldwide. The primary neuropathological hallmark in AD is amyloid plaques composed of amyloid-β peptide (Aβ). Several familial mutations found in Aβ sequence result in early onset of AD. Previous studies showed that the mutations located at N-terminus of Aβ, such as the English (H6R) and Tottori (D7N) mutations, promote fibril formation and increase cytotoxicity. However, A2T mutant located at the very N-terminus of Aβ shows low-prevalence incidence of AD, whereas, another mutant A2V causes early onset of AD. To understand the molecular mechanism of the distinct effect and develop new potential therapeutic strategy, here, we examined the effect of full-length and N-terminal A2V/T variants to wild type (WT) Aβ40 by fibrillization assays and NMR studies. We found that full-length and N-terminal A2V accelerated WT fibrillization and induced large chemical shifts on the N-terminus of WT Aβ, whereas, full-length and N-terminal A2T retarded the fibrillization. We further examined the inhibition effect of various N-terminal fragments (NTFs) of A2T to WT Aβ. The A2T NTFs ranging from residue 1 to residue 7 to 10, but not 1 to 6 or shorter, are capable to retard WT Aβ fibrillization and rescue cytotoxicity. The results suggest that in the presence of full-length or specific N-terminal A2T can retard Aβ aggregation and the A2T NTFs can mitigate its toxicity. Our results provide a novel targeting site for future therapeutic development of AD. |
Author | Yu, Hui-Ming Lin, Tien-Wei Liao, Yi-Hung Chang, Chi-Fon Chen, Yun-Ru Chang, Yu-Jen |
AuthorAffiliation | USF Health Morsani College of Medicine, UNITED STATES 2 Genomics Research Center, Academia Sinica, Taipei, Taiwan 1 Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan |
AuthorAffiliation_xml | – name: USF Health Morsani College of Medicine, UNITED STATES – name: 1 Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan – name: 2 Genomics Research Center, Academia Sinica, Taipei, Taiwan |
Author_xml | – sequence: 1 givenname: Tien-Wei surname: Lin fullname: Lin, Tien-Wei organization: Genomics Research Center, Academia Sinica, Taipei, Taiwan – sequence: 2 givenname: Chi-Fon surname: Chang fullname: Chang, Chi-Fon organization: Genomics Research Center, Academia Sinica, Taipei, Taiwan – sequence: 3 givenname: Yu-Jen surname: Chang fullname: Chang, Yu-Jen organization: Genomics Research Center, Academia Sinica, Taipei, Taiwan – sequence: 4 givenname: Yi-Hung surname: Liao fullname: Liao, Yi-Hung organization: Genomics Research Center, Academia Sinica, Taipei, Taiwan – sequence: 5 givenname: Hui-Ming surname: Yu fullname: Yu, Hui-Ming organization: Genomics Research Center, Academia Sinica, Taipei, Taiwan – sequence: 6 givenname: Yun-Ru surname: Chen fullname: Chen, Yun-Ru organization: Genomics Research Center, Academia Sinica, Taipei, Taiwan |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28362827$$D View this record in MEDLINE/PubMed |
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Copyright | 2017 Lin et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2017 Lin et al 2017 Lin et al |
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Notes | Competing Interests: The authors have declared that no competing interests exist. Conceptualization: YRC.Data curation: TWL CFC YJC YHL.Formal analysis: TWL CFC YJC YHL.Funding acquisition: YRC.Investigation: TWL CFC YHL YRC.Methodology: TWL CFC YJC YHL.Project administration: TWL CFC YJC YHL YRC.Resources: HMY CFC.Supervision: YRC.Validation: TWL YRC.Visualization: TWL YRC.Writing – original draft: TWL YHL.Writing – review & editing: CFC YRC. |
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Snippet | Alzheimer's disease (AD) is the most common dementia affecting tens of million people worldwide. The primary neuropathological hallmark in AD is amyloid... Alzheimer’s disease (AD) is the most common dementia affecting tens of million people worldwide. The primary neuropathological hallmark in AD is amyloid... |
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SubjectTerms | Acceleration Agglomeration Aggregates Alanine Aluminum Alzheimer Disease - metabolism Alzheimer's disease Amino acids Amyloid beta-Peptides - metabolism Amyloid precursor protein Assembly Attention Attitude control Biochemistry Biocompatibility Biology and Life Sciences Body fluids Brain C-Terminus Cadmium Cell Line, Tumor Cell Survival - physiology Cerebrospinal fluid Chelates Chelation Chemical compounds Circular Dichroism Cognition Cognitive ability Copper Cytotoxicity Dementia disorders Fibrillogenesis Fluorescence Fragmentation Humans Hydrophobic and Hydrophilic Interactions Immunology Inhibitors Iron Isoforms Magnetic Resonance Spectroscopy Medicine and Health Sciences Metal ions Metals Microbiology Microscopy, Electron, Transmission Mutants Mutation N-Terminus Neurobiology Neuroblastoma Neurodegeneration Neurodegenerative diseases Neuroimaging Nucleation Older people Peptides Pharmacology Physical Sciences Positron emission tomography Research and Analysis Methods Residues Secretase Senile plaques Solubility Spectroscopy, Fourier Transform Infrared Tomography Toxicity Viability Zinc β-Amyloid |
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Title | Alzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity |
URI | https://www.ncbi.nlm.nih.gov/pubmed/28362827 https://www.proquest.com/docview/1882796147 https://pubmed.ncbi.nlm.nih.gov/PMC5376091 https://doaj.org/article/782a4ce0167d4ff899f19adf98a2b697 http://dx.doi.org/10.1371/journal.pone.0174561 |
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