Aluminum interaction with human brain tau protein phosphorylation by various Kinases
Title:
Aluminum interaction with human brain tau protein phosphorylation by various Kinases
Author:
El-Sebae, A. H. Abdel-Ghanv, M. E. Shalloway, D. Zeid, M.M. Abou Blancato, J. Saleh, M. A.
Appeared in:
Journal of environmental science and health. Part B, Pesticides, food contaminants, and agricultural wastes
Paging:
Volume 28 (1993) nr. 6 pages 763-777
Year:
1993-12
Contents:
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.