Abstract
Tau protein phosphorylation has been implicated as a main process that regulates microtubule dynamics. A large number of tau isoforms is generated by phosphorylation through the action of a diversity of kinases. We have analysed variations in tau phosphorylation by two-dimensional gel electrophoresis, where a great heterogeneity of isoforms can be detected. Using mouse brain slices from various developmental stages we have found preferential phosphorylation of low molecular weight tau isoforms in all the ages analysed. A greater isoform diversity was found in juvenile than in adult brain. Brain slices provide a tightly regulated environment that preserves cell compartmentalization and has shown to be very useful for studies on tau phosphorylation.
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