University of Cambridge > Talks.cam > Biophysical Seminars > Redox-dependent modulation of haemostasis and vascular function by amyloid peptide beta: a new interpretation of the vascular component of dementia.

Redox-dependent modulation of haemostasis and vascular function by amyloid peptide beta: a new interpretation of the vascular component of dementia.

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Alzheimer’s disease (AD) is the most common neurodegenerative cause of dementia in the elderly. AD is accompanied by the accumulation of amyloid peptides in the brain parenchyma and in the cerebral vessels. The sporadic form of AD accounts for about 95% of all cases. It is characterized by a late onset, typically after the age of 65, with a complex and still poorly understood aetiology. Several observations point towards a central role of cerebrovascular dysfunction in the onset of sporadic AD (SAD). According to the “vascular hypothesis”, AD may be initiated by vascular dysfunctions that precede and promote the neurodegenerative process. In accordance to this, AD patients show increased stroke risk. It is now clear that multiple bidirectional connections exist between AD and cerebrovascular disease, and in this new scenario, the effect of amyloid peptides on vascular cells and blood platelets appears to be central to AD. Reactive oxygen species (ROS) generation is critical in the regulation of platelets, which has important implications in the modulation of haemostasis and thrombosis. Interestingly, amyloid β (Aβ) 1-42 peptide stimulated superoxide anion formation in a concentration-dependent manner. Aβ peptide stimulated superoxide anion formation in a NOX -dependent manner, as proved by the use of VAS2870 . Aβ 1-42 peptide displayed only moderate activity as an aggregation stimulus, but was able to significantly potentiate platelet aggregation in response to submaximal agonist concentrations, such as 0.03 unit/ml thrombin and 10 μM arachidonic acid. The inhibition of NOXs by 10 μM VAS2870 abolished Aβ-dependent potentiation of platelet aggregation in response to 10 μM arachidonic acid, suggesting that the pro-thrombotic activity of Aβ peptides depends on NOX activity. These finding shed some new light on the pro-thrombotic activity of Aβ peptides.

This talk is part of the Biophysical Seminars series.

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