What causes Alzheimer's disease: The pathophysiology of Amyloid.

Amyloid. 
 Learning objectives
Describe the function of amyloid precursor protein (APP) in normal brain function.
Explain how the processing of APP can lead to pathogenic Aβ generation.
Discuss the differences between amyloidogenic and non-amyloidogenic processing of APP and how they relate to Alzheimer's disease.
Understand the roles of Alpha, Beta, and Gamma secretase in APP processing and how they influence Aβ generation.
Explain why the cleavage location of APP is critical for pathogenic Aβ generation.
Describe how mutations in APP and Gamma secretase can lead to familial Alzheimer's disease.
Discuss the clinical significance of the Aβ42:Aβ40 ratio and how it relates to Alzheimer's disease.
Explain why Aβ42:Aβ40 is lower in Alzheimer's disease and how this relates to amyloid pathology.
By the end of this video, viewers should be able to explain the pathophysiology of Alzheimer's disease, including the role of APP in normal brain function, the different processing pathways for APP, and how mutations in APP and Gamma secretase can lead to familial Alzheimer's disease. Additionally, viewers should understand the clinical significance of the Aβ42:Aβ40 ratio and how it relates to Alzheimer's disease.

[@douglaswatt1582]

Somewhat disappointing that Jack does not mention that the alpha secretase pathway is actually promoting neuroplasticity while the beta amyloid pathway which is traditionally thought of as pathogenic is also physiologically recruited for synaptic pruning, and for immune defense.

[@brucestewart3170]

The accelerating and clumping seem to be indicative of prion disease. Some scientist are beginning to equate Alzheimer disease with prions. From what you are saying in this video I can not see the connection. What do you think?

[@douglaswatt1582]

Not quite. The seeding and templating process by which small aggregates termed oligomers recruit non pathologically folded forms of the protein to become more problematic is termed "prion like" but it's not fully prion because ingestion of these proteins does not cause templating like a true Prion would enable.