Regulation Of Alzheimer-Like Phosphorylation Of Tau Protein By Protein Kinases
Keywords
Protein Kinase, Alzheimer’S Disease, Tau Protein, Abnormal Phosphorylation
Abstract
Abnormal phosphorylation of microtubule-associated protein ¦Ó is one of the important mechanisms of neurofibrillary degeneration in Alzheimer’s disease (AD). Research has found that: casein kinase-1 (ck-1), camp-dependent protein kinase (pka) ) and glycogen synthase kinase-3 (gsk-3) can catalyze the phosphorylation of recombinant tau protein to varying degrees, thereby inhibiting the biological function of tau protein in promoting microtubule assembly to varying degrees. If tau protein is prewarmed with pka first After 2 hours of incubation with gsk-3, it was found that the phosphorylation degree of tau protein was significantly higher than that treated with gsk-3 alone, and the biological activity was significantly reduced. The formation of microtubules was almost invisible under electron microscopy. The results suggested: pka and gsk- 3 has a positive synergistic effect in the ad-like phosphorylation of tau protein and its functional inhibition.
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Original research done by Wang Jianzhi, Wang Qun, Wu Qiongli, I.GRUNDKE-IQBAL, K.IQBAL
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