GLUTAMATE INCREASES TAU-PHOSPHORYLATION IN PRIMARY NEURONAL CULTURES FROM FETAL-RAT CEREBRAL-CORTEX

Tau proteins are microtubule-associated proteins which promote microtu bule polymerisation and stabilisation. AT8 is a new monoclonal antibod y raised against a phosphorylated Tau protein probably at Serine 202. Tau protein, recognized by AT8 antibody is present in fetal human and rat brains, and in Alzheimer's brains. Here we report that glutamate a n excitatory neurotransmitter and also a potent excitotoxin produces i n primary neuronal cultures a rapid increase in phosphorylated Tau pro tein immunoreactivity using AT8 antibody. Glutamate augments neuronal Tau immunoreactivity by 225% using laser confocal immunocytochemistry and by 355% on immunoblot analysis. This experimental model of Tau pro tein modifications could help to decipher the intracellular biochemica l pathways at the origin of phosphorylated Tau protein.