Alzheimer’s disease is known to be the most common human dementia and therefore puts forth a massive burden on patients, caregivers and society at large. The molecular pathways which apparently cause Alzheimer’s are not examined well, however significant data highlight that the amyloid β-protein plays a vital role.
The firm state level of Aβ is seemingly managed by its production, degradation and clearance. Experts share that in disease a defect paving a path towards over-production or low clearance may cause a buildup of Aβ. This may stimulate formation of a pathogenic cascade culminating in the cognitive deficits that are similar to attributes of Alzheimer’s.
Aβ supposedly has the ability to self-associate and develop a wide range of diverse assembly forms ranging from individual monomers to large insoluble aggregates which are generally known as amyloid plaques.
Plaques are known to be pathologic hallmarks of Alzheimer’s and it has been assumed that they may also cause the disease. The quantity and temporal progression of amyloid plaques do not associate with disease status, thereby highlighting the question, if Aβ causes AD, then why doesn’t the quantity of Aβ in the form of amyloid plaques relate to the severity of dementia?
Scientists evaluated the correlation between several biochemical forms of Aβ and the occurrence of Alzheimer-type dementia. In order to understand this better, experts examined 43 brains which were obtained from the MRC Cognitive Function and Ageing Study. They identified that the level of SDS-stable Aβ dimers are apparently linked with the existence of Alzheimer-type dementia.
This new investigation is based on prior analysis conducted by the Walsh group who revealed that SDS-stable Aβ dimers may weaken neuronal functions which are essential for memory formation. They also shared that targeting Aβ dimers may lessen the memory loss typical of Alzheimer’s.
A follow-up study examining the relationship between biochemically different forms of Aβ and AD-type dementia among 220 brains C may allow for further validation of Aβ dimers as mediators of disease. In addition, other corresponding studies intend to develop antibodies and small molecules which attach to Aβ dimers and neutralize their activity are ongoing.
These findings were recently published in the Brain.