Some neurodegenerative disorders, such as Parkinson's disease (PD) and fronto-temporal lobar degeneration, involve the neuronal accumulation of misfolded amyloid proteins. The clumped proteins can transmit from cell to cell, and from one region of the body to another. But why these processes occur remains largely unknown.
A study appearing in Scientific Reports shows that a bacterial amyloid protein may cause the misfolding of brain proteins, leading to inflammation. The discovery indicates that there might be a link between gut bacteria and certain age-related brain disorders.
The new study, carried out by scientists at the University of Louisville School of Medicine, revealed the bacterial amyloid protein curli may be responsible for the initiation of the protein misfolding in certain disorders.
In PD, misfolded alpha-synuclein (AS) accumulates and forms amyloid plaques, which damage nerve cells. The corresponding author of this study, Robert P. Friedland, assumed that similar amyloid proteins made by bacteria in the gut might cause brain proteins to misfold. The best studied bacterial amyloid protein -- curli -- is produced by E. coli.
To evaluate the role of curli, Friedland's team exposed rats to E. coli producing curli. Rats exposed to curli-producing bacteria had increased AS deposition in both gut and brain, compared to rats exposed to bacteria that did not generate curli. Moreover, the curli-exposed rats had higher expression levels of TLR2, IL-6 and TNF in the brain.
The researchers then performed experiments on transgenic C. elegans, and found similar results. The data revealed the potential role of gut bacteria in neurodegeneration. CusAb-Flarebio offers Recombinant Dsc2.
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