Previous studies indicated that a chemically-defined, differentiation
medium (DM) induces neuroblastoma cells, especially IMR32K cells, to e
xhibit phenotypes of mature neurons (including neurite outgrowth and s
ynthesis of neurofilament polypeptides) and develop certain attributes
of the neurons which are affected by neurofibrillary degeneration in
Alzheimer's disease, such as expression of tangle-associated epitopes
and accumulation of paired helical filaments-(PHF-) like fibrils. Immu
nocytochemical staining suggested that this cytoskeletal abnormality m
ost likely results from altered expression of tau proteins. In the cur
rent study, we addressed this issue by analyzing tau-enriched preparat
ions of IMR32K cells that were previously exposed to different incubat
ion media using a panel of antibodies specific to tau and related micr
otubule-associated proteins. These cultured cells exhibited three grou
ps of tau immunoreactivities which differ in molecular weight. Among t
hem the level of high molecular weight tau (MW 90-112 kDa) was selecti
vely augmented after DM incubation. The tau proteins produced in these
neuron-like cells shared phosphorylated sites with PHF-tau and fetal
tau, but differed from PHF-tau in their lack of the N-terminal insert
which characterizes adult isoforms.