Quantitative proteomics analysis of phosphorylated proteins in the hippocampus of Alzheimer's disease subjects.

摘要: Phosphorylation on tyrosine, threonine and serine residues represents one of the most important post-translational modifications is a key regulator cellular signaling multiple biological processes that require strict control by protein kinases phosphatases. Abnormal phosphorylation has been associated with several human diseases including Alzheimer's disease (AD). One characteristic hallmarks AD presence neurofibrillary tangles, composed microtubule-associated, abnormally hyperphosphorylated tau protein. However, others proteins showed altered levels in suggesting deregulated may contribute to pathogenesis. Phosphoproteomics recently gained attention as valuable approach analyze phosphorylation, both quantitative qualitative way. We used fluorescent phosphospecific Pro-Q Diamond dye identify alterations their overall hippocampus vs. (CTR) subjects. Significant changes were found for 17 involved crucial neuronal process such energy metabolism or signal transduction. These phosphoproteome data provide new clues better understand molecular pathways are pathogenesis progression AD.