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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sawashita, Jinko Mori, Masayuki Zhang, Beiru Naiki, Hironobu Kametani, Fuyuki Higuchi, Keiichi Hasegawa, Kazuhiro |
| Description | Author Affiliation: Sawashita J ( Department of Biological Sciences for Intractable Neurological Diseases, Institute for Biomedical Sciences, Interdisciplinary Cluster for Cutting Edge Research, Shinshu University, 3-1-1 Asahi, Matsumoto, Nagano 390-8621, Japan); Zhang B ( Department of Nephrology, Shengjing-Hospital of China Medical University, Shenyang, Liaoning, 110004, China); Hasegawa K ( Division of Molecular Pathology, Department of Pathological Sciences, Faculty of Medical Science, University of Fukui, Yoshida-gun, Fukui 910-1193, Japan); Mori M ( Department of Aging Biology, Institute of Pathogenesis and Disease Prevention, Shinshu University Graduate School of Medicine, 3-1-1 Asahi, Matsumoto, Nagano 390-8621, Japan); Naiki H ( Division of Molecular Pathology, Department of Pathological Sciences, Faculty of Medical Science, University of Fukui, Yoshida-gun, Fukui 910-1193, Japan); Kametani F ( Department of Dementia and Higher Brain Function, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan.); Higuchi K ( Department of Biological Sciences for Intractable Neurological Diseases, Institute for Biomedical Sciences, Interdisciplinary Cluster for Cutting Edge Research, Shinshu University, 3-1-1 Asahi, Matsumoto, Nagano 390-8621, Japan); |
| Abstract | In murine senile amyloidosis, misfolded serum apolipoprotein (apo) A-II deposits as amyloid fibrils (AApoAII) in a process associated with aging. Mouse strains carrying type C apoA-II (APOA2C) protein exhibit a high incidence of severe systemic amyloidosis. Previously, we showed that N- and C-terminal sequences of apoA-II protein are critical for polymerization into amyloid fibrils in vitro. Here, we demonstrate that congenic mouse strains carrying type F apoA-II (APOA2F) protein, which contains four amino acid substitutions in the amyloidogenic regions of APOA2C, were absolutely resistant to amyloidosis, even after induction of amyloidosis by injection of AApoAII. In vitro fibril formation tests showed that N- and C-terminal APOA2F peptides did not polymerize into amyloid fibrils. Moreover, a C-terminal APOA2F peptide was a strong inhibitor of nucleation and extension of amyloid fibrils during polymerization. Importantly, after the induction of amyloidosis, we succeeded in suppressing amyloid deposition in senile amyloidosis-susceptible mice by treatment with the C-terminal APOA2F peptide. We suggest that the C-terminal APOA2F peptide might inhibit further extension of amyloid fibrils by blocking the active ends of nuclei (seeds). We present a previously unidentified model system for investigating inhibitory mechanisms against amyloidosis in vivo and in vitro and believe that this system will be useful for the development of novel therapies. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 8 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-02-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Amyloid Metabolism Apolipoprotein A-II Chemistry Amino Acid Sequence Amino Acid Substitution Ultrastructure Amyloidosis Blood Pathology Animals Cholesterol Lipoproteins, HDL Mice, Inbred C57BL Models, Biological Molecular Sequence Data Mutant Proteins Peptides Polymerization Structure-Activity Relationship Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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