Induction of protein conformational change in mouse senile amyloidosis
| Autor: | Tatsumi Korenaga, Takatoshi Matsushita, Akihiro Nakamura, Masayuki Mori, Zhanjun Guo, Kumiko Kogishi, Junjie Yao, Masanori Hosokawa, Xiaoying Fu, Fuyuki Kametani, Yanming Xing, Keiichi Higuchi |
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| Rok vydání: | 2002 |
| Předmět: |
Amyloid
Protein Folding Time Factors Apolipoprotein B Protein Conformation Amyloid Neuropathies Biochemistry Amyloid disease Mice mental disorders medicine Animals Tissue Distribution Senile plaques Molecular Biology biology Chemistry Amyloidosis P3 peptide Cell Biology medicine.disease Molecular biology Biochemistry of Alzheimer's disease Microscopy Electron Phenotype biology.protein Protein folding Apolipoprotein A-II |
| Zdroj: | The Journal of biological chemistry. 277(36) |
| ISSN: | 0021-9258 |
| Popis: | Aggregated amyloid fibrils can induce further polymerization of precursor proteins in vitro, thus providing a possible basis for propagation or transmission in the pathogenesis of amyloidoses. Previously, we postulated that the transmission of amyloid fibrils induces conformational changes of endogenous amyloid protein in mouse senile amyloidosis (Xing, Y., Nakamura, A., Chiba, T., Kogishi, K., Matsushita, T., Fu, L., Guo Z., Hosokawa, M., Mori, M., and Higuchi, K. (2001) Lab. Invest. 81, 493-499). To further characterize this transmissibility, we injected amyloid fibrils (AApoAII(C)) of amyloidogenic C type apolipoprotein A-II (APOAIIC) intravenously into 2-month-old SAMR1 mice, which have B type apolipoprotein A-II (APOAIIB), and develop few if any amyloid deposits spontaneously. 10 months after amyloid injection, deposits were detected in the tongue, stomach, intestine, lungs, heart, liver, and kidneys. The intensity of deposition increased thereafter, whereas no amyloid was detected in distilled water-injected SAMR1 mice, even after 20 months. The deposited amyloid was composed of endogenous APOAIIB with a different amyloid fibril conformation. The injection of these amyloid fibrils of APOAIIB (AApoAII(B)) induced earlier and more severe amyloidosis in SAMR1 mice than the injection of AApoAII(C) amyloid fibrils. Thus, AApoAII(C) from amyloidogenic mice could induce a conformational change of less amyloidogenic APOAIIB to a different amyloid fibril structure, which could also induce amyloidosis in the less amyloidogenic strain. These results provide important insights into the pathogenesis of amyloid diseases. |
| Databáze: | OpenAIRE |
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