Exposure to bacterial endotoxin generates a distinct strain ofalpha-synuclein fibril
| Autor: | Masato Hasegawa, Chul Suk Hong, Guohua Lv, Changyoun Kim, Seung-Jae Lee, He Jin Lee, Masami Masuda-Suzukake, David Eliezer, Eliezer Masliah, Seung R. Paik, Byung Chul Jung, Jun Sung Lee, Elvira Valera |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Lewy Body Disease Lipopolysaccharides Amyloid Lipopolysaccharide Biology Protein aggregation Fibril Article 03 medical and health sciences chemistry.chemical_compound Mice Protein Aggregates 0302 clinical medicine Atrophy mental disorders medicine Animals Humans Cells Cultured Synucleinopathies Neurons Multidisciplinary Strain (chemistry) Dementia with Lewy bodies Protein primary structure Parkinson Disease Multiple System Atrophy medicine.disease Protein Structure Tertiary Mice Inbred C57BL Protein Transport 030104 developmental biology Biochemistry chemistry alpha-Synuclein Female Microglia 030217 neurology & neurosurgery |
| Zdroj: | SCIENTIFIC REPORTS(6) Scientific Reports |
| Popis: | A single amyloidogenic protein is implicated in multiple neurological diseases and capable of generating a number of aggregate “strains” with distinct structures. Among the amyloidogenic proteins, α-synuclein generates multiple patterns of proteinopathies in a group of diseases, such as Parkinson disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA). However, the link between specific conformations and distinct pathologies, the key concept of the strain hypothesis, remains elusive. Here we show that in the presence of bacterial endotoxin, lipopolysaccharide (LPS), α-synuclein generated a self-renewable, structurally distinct fibril strain that consistently induced specific patterns of synucleinopathies in mice. These results suggest that amyloid fibrils with self-renewable structures cause distinct types of proteinopathies despite the identical primary structure and that exposure to exogenous pathogens may contribute to the diversity of synucleinopathies. |
| Databáze: | OpenAIRE |
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