Aluminum interaction with human brain tau protein phosphorylation by various Kinases

Abstract

Phosphorylation is an indispensable process for energy and signal transduction in biological systems. AlCl₃ at 10 nM to 10 uM range activated in‐vitro [γ‐³²P)ATP phosphorylation of the brain (tau) T protein in both normal human or E.coli expressed T forms; in the presence of the kinases P34, PKP, and PKC. However, higher concentrations of ALCl₃ inhibited the T phosphorylation with P34, PKP, and PKC to a maximum at 1 mM level. AlCl₃ at 100 uM to 500 uM range induced non‐enzymatic phosphorylation of T with γ‐ATP, γ‐GTP, and α‐GTP. AlCl₃ activated histone phosphorylation by P34 in a similar pattern. The hyperphosphorylation of T by Al³⁺ was accompanied by molecular shift and mobility retardation in SDS‐PAGE. This may demonstrate the mechanism of the longterm neurological effect of Al³⁺ in human brain leading to the formation of the neurofibrillary tangles related to Alzeheimer's disease.     

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