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In addition, tau accumulated in neurodegenerative diseases is characterized by being highly modified via phosphorylation.
Moreover, in patients exhibiting mild cognitive impairment (MCI), a correlation is observed between the level of phosphorylated tau in the spinal fluid and the degree of pituitary atrophy, suggesting phosphorylated tau as a highly reliable biomarker for neurodegeneration in patients with tauopathy (Wendy Noble et al.
Based on these findings, attempts have been made to develop a treatment using inhibitors against kinases, which are enzymes involved in phosphorylation, and particularly against GSK-3 beta, for inhibiting excessive phosphorylation of tau (Id).
In fact, some of the sites where tau is phosphorylated by GSK-3 beta coincide with sites of tau phosphorylation seen in fetal and normal human brains (Burnes, et. al.
[0007] Although it was believed that extracellular tau originates from leakage from degenerated nerve cells as a consequence of cell death, recent studies have suggested that following excessive intracellular phosphorylation, tau is processed and then actively secreted out of the cell.
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