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Free Radic Biol Med. 2015 Jun;83:186-91. doi: 10.1016/j.freeradbiomed.2015.02.028. Epub 2015 Mar 5.

Molecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer׳s disease.

Author information

1
Department of Physiology, Faculty of Medicine, University of Valencia and Fundacion Investigacion Hospital Clinico Universitario/INCLIVA, 46010 Valencia, Spain.
2
Department of Physiology, Faculty of Medicine, University of Valencia and Fundacion Investigacion Hospital Clinico Universitario/INCLIVA, 46010 Valencia, Spain. Electronic address: jose.vina@uv.es.

Abstract

Neurofibrillary tangles (aggregates of cytoskeletal Tau protein) and senile plaques (aggregates mainly formed by amyloid β peptide) are two landmark lesions in Alzheimer׳s disease. Some researchers have proposed tangles, whereas others have proposed plaques, as primary lesions. For a long time, these were thought of as independent mechanisms. However, experimental evidence suggests that both lesions are intimately related. We review here some molecular pathways linking amyloid β and Tau toxicities involving, among others, glycogen synthase kinase 3β, p38, Pin1, cyclin-dependent kinase 5, and regulator of calcineurin 1. Understanding amyloid β and Tau toxicities as part of a common pathophysiological mechanism may help to find molecular targets to prevent or even treat the disease.

KEYWORDS:

Alzheimer׳s disease; Amyloid β; Dementia; Free radicals; Neurodegeneration; p-Tau

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