Abstract
Protein aggregation likely plays a key role in the initiation and spreading of Alzheimer’s disease pathology through the brain. Soluble aggregates of amyloid beta are believed to play a key role in this process. However, the aggregates present in humans are still poorly characterized due to a lack of suitable methods required for characterizing the low concentration of heterogeneous aggregates present. We have used a variety of biophysical methods to characterize the aggregates present in human Alzheimer’s disease brains at Braak stage III. We find soluble amyloid beta-containing aggregates in all regions of the brain up to 200 nm in length, capable of causing an inflammatory response. Rather than aggregates spreading through the brain as disease progresses, it appears that aggregation occurs all over the brain and that different brain regions are at earlier or later stages of the same process, with the later stages causing increased inflammation.
Highlights
Alzheimer’s disease is a progressive neurodegenerative disease characterized by memory loss and cognitive decline
This can lead to microglial activation and inflammation,[7] a key player in Alzheimer’s disease pathology.[6,8,9]
Microglial activation increases as the disease progresses, and they become dystrophic at late stages.[10]
Summary
Alzheimer’s disease is a progressive neurodegenerative disease characterized by memory loss and cognitive decline. It is the leading cause of dementia, which is currently the leading cause of death in the UK.[1] The aggregation of the amyloid beta 42 peptide (Ab42) is believed to play a key role in the initiation and development of the disease.[2]. Ab42 aggregates have been shown to cause neuronal cell death, synaptic dysfunction, as well as cognitive impairment in Alzheimer’s disease patients and animal models of the disease.[12,13,14,15,16,17,18,19,20,21,22]
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