Each one of our brain cells has more than millions of proteins in it and these proteins are responsible for carrying out the cell functions. So which of these proteins/protein pathways are dysregulated in Alzheimer's Disease (AD)?
Our new study published in March 2021 in International Society for Neurochemistry journal, employed a tandem mass tags (TMT) approach coupled to high-resolution mass spectrometry to quantify 8,066 proteins in frontal cortex from AD patients with corresponding age-matched brain samples. Out of these proteins 432 were observed to be significantly altered (>1.5 fold) in their expression in AD brains.
8,066 proteins were quantified in frontal cortices of AD patients and compared with age-matched controls.
Proteins whose abundance was previously known to be altered in AD were identified including secreted phosphoprotein 1 (SPP1), somatostatin (SST), SPARC related modular calcium binding 1 (SMOC1), dual specificity phosphatase 26 (DUSP26) and neuronal pentraxin 2 (NPTX2). In addition, we identified several novel candidates whose association with AD has not been previously described. Of the novel molecules, we validated chromogranin A (CHGA), inner membrane mitochondrial protein (IMMT) and RAS like proto-oncogene A (RALA) in an additional set of 20 independent brain samples using targeted parallel reaction monitoring (PRM) mass spectrometry assays. The differentially expressed proteins discovered in our study, once validated in larger cohorts, should help discern the pathogenesis of AD.
432 proteins were found to be changed in AD brain among which exist proteins that were previously known to be altered in AD.
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