Pore-like Aggregates of Tau Protein Induced by Formaldehyde

Though the hypothesis of aspecific amyloid ion channels has been proposed by Lin, et at (University of California, Santa Barbara) to explain the mechanism of metabolic dysfunction and cell death during protein conformational diseases, the pore-like aggregates of misfolded neural Tau have not been observed Revulsants involved in the formation of pore-like aggregates have not been found yet According to the hypothesis chronic impairment resulted from abnormally-increased endogenous formaldehyde is one of the important risk factors related to sporadic senile dementia, formaldehyde has been utilized to incubate with Tau protein resulting in amyloid-like deposits with marked cytotoxicity Under the experimental conditions, 0 5% formaldehyde-treated Tau could form pore-like aggregates These results may deliver a novel approach to study the mechanism of cellular metabolic disturbance, even cell death, which is induced by formaldehyde-treated neural Tau