Internal medicine

Pathology

Neuroscience

Disease

Pathogenesis

Amyloid precursor protein

Biology

Epistemology

Phosphorylation

Philosophy

Biochemistry of Alzheimer's disease

Immunology

Amyloid (mycology)

Hyperphosphorylation

Tau protein

Extracellular

Neurotoxicity

Senile plaques

Mechanism (biology)

Cell biology

Toxicity

Alzheimer's disease

Medicine

International Journal of Biological Sciences

Extracellular neuritic plaques composed of amyloid‑β (Aβ) protein and intracellular neurofibrillary tangles containing phosphorylated tau protein are the two hallmark proteins of Alzheimer's disease (AD), and the separate neurotoxicity of these proteins in AD has been extensively studied. However, interventions that target Aβ or tau individually have not yielded substantial breakthroughs. The interest in the interactions between Aβ and tau in AD is increasing, but related drug investigations are in their infancy. This review discusses how Aβ accelerates tau phosphorylation and the possible mechanisms and pathways by which tau mediates Aβ toxicity. This review also describes the possible synergistic effects between Aβ and tau on microglial cells and astrocytes. Studies suggest that the coexistence of Aβ plaques and phosphorylated tau is related to the mechanism by which Aβ facilitates the propagation of tau aggregation in neuritic plaques. The interactions between Aβ and tau mediate cognitive dysfunction in patients with AD. In summary, this review summarizes recent data on the interplay between Aβ and tau to promote a better understanding of the roles of these proteins in the pathological process of AD and provide new insights into interventions against AD.

Interaction between Aβ and Tau in the Pathogenesis of Alzheimer's Disease