Tau protein-prepared post-mortem from brains of Alzheimer's disease pa
tients was treated with protein phosphatase 1 catalytic subunit, 2A ca
talytic subunit, and 2B (calcineurin). Dephosphorylation was monitored
by immunoblotting with two monoclonal antibodies, TAU-1 and SMI31, wh
ich recognize in tau the dephospho- and phospho-states, respectively,
of proline-directed protein kinase phosphorylation sites. Out of the t
hree enzymes tested, protein phosphatase 2A was only effective in deph
osphorylating tau at these Alzheimer-type epitopes.