HYPERPHOSPHORYLATION of the microtubule-associated tau proteins is one
of the main pathological events that leads to neurofibrillary neurode
generation in Alzheimer's disease. A similar tau phosphorylation patte
rn may be obtained in SY-5Y neuroblastoma cells after okadaic acid tre
atment. In this paper, we clearly demonstrate phosphorylation of Ser42
2 in tau proteins of treated cells as well as in Alzheimer brain homog
enates. By contrast, Ser422 was not phosphorylated on native tau prote
ins from non-treated cells or rapidly processed biopsies. These result
s confirm that this cell model is still relevant to study neurofibrill
ary neurodegeneration of the Alzheimer type.