The microtubule-associated protein tau, a major component of paired he
lical filaments in Alzheimer's disease, had been thought to be a neuro
n-specific protein. We investigated various rat tissues using both rev
erse transcriptase-coupled polymerase chain reaction and immunoblottin
g. tau was found to be widely expressed in many tissues besides the ne
rvous system: at relatively high levels in the heart, skeletal muscle,
lung, kidney, and testis and at low levels in the adrenal gland, stom
ach, and liver. In terms of the tau isoform expression, tissues fall i
nto three classes: those expressing predominantly small tau, those exp
ressing predominantly big tau, and those expressing both at comparable
levels. The phosphorylation state of tau varied among the tissues, as
shown by differences in the extents of changes in the reactivities wi
th Tau 1 and electrophoretic mobilities after dephosphorylation. It is
notable that tau in many nonneural tissues was highly phosphorylated
at Ser(396) (according to the numbering of the 441-residue human tau i
soform). Thus, tau is widely expressed in rat tissues.