Bacterial Lipopolysaccharide (Lps) And Alzheimer'S Disease

Data found in literature have reported that bacterial endotoxins may be involved in the inflammatory and pathological processes associated with amyloidosis and Alzheimer's disease (AD). In fact, it has been observed that the chronic infusion of the bacterial lipopolysaccharide (LPS), the outer cell wall component of Gram negative bacteria, into the fourth ventricle of rats reproduces many of the inflammatory and pathological features seen in the brain of AD patients. In this context, a key player in the pathogenesis of AD is the amyloid-beta peptide (A beta) that is capable of aggregating in fibrils that represent the main component of amyloid plaques. These deposits that accumulate among brain cells are indeed one of the hallmarks of AD. This aggregation in fibrils seems to correlate with A beta toxic effects. However, recent data have shown that amyloid fibril formation not only results in toxic aggregates but also provides biologically functional molecules; such amyloids have been identified on the surface of fungi and bacteria. The aim of this work was to get a better insight on the influence of bacterial endotoxins on A beta fibrillogenesis; factors that influence fibril formation may be important for A beta toxic potential. Following 3 days of incubation at 37 degrees C, A beta was organized in compact fibrils and the in vitro A beta fibrillogenesis was potentiated by the Escherichia coli endotoxin. This suggests the importance of infectious events in the pathogenesis of Alzheimer's disease and proposes a new aspect related to the putative pathological factors that can be implicated in the mechanisms involved in A beta 25-35 fibrillogenesis.