[HTML][HTML] Insulin and insulin-like growth factor-1 regulate tau phosphorylation in cultured human neurons
M Hong, VMY Lee - Journal of Biological Chemistry, 1997 - ASBMB
Hyperphosphorylated tau is the major component of paired helical filaments in
neurofibrillary lesions associated with Alzheimer's disease. Hyperphosphorylation reduces
the affinity of tau for microtubules and is thought to be a critical event in the pathogenesis of
this disease. Recently, glycogen-synthase kinase-3 has been shown to phosphorylate tau in
vitro and in non-neuronal cells transfected with tau. The activity of glycogen-synthase kinase-
3 can be down-regulated in response to insulin or insulin-like growth factor-1 through the …
neurofibrillary lesions associated with Alzheimer's disease. Hyperphosphorylation reduces
the affinity of tau for microtubules and is thought to be a critical event in the pathogenesis of
this disease. Recently, glycogen-synthase kinase-3 has been shown to phosphorylate tau in
vitro and in non-neuronal cells transfected with tau. The activity of glycogen-synthase kinase-
3 can be down-regulated in response to insulin or insulin-like growth factor-1 through the …