Phosphoproteome profiling of substantia nigra and cortex regions of Alzheimer's disease patients

2012 | journal article. A publication with affiliation to the University of Göttingen.

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​Phosphoproteome profiling of substantia nigra and cortex regions of Alzheimer's disease patients​
Zahid, S.; Oellerich, M.; Asif, A. R. & Ahmed, N.​ (2012) 
Journal of Neurochemistry121(6) pp. 954​-963​.​ DOI: https://doi.org/10.1111/j.1471-4159.2012.07737.x 

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Authors
Zahid, Saadia; Oellerich, Michael; Asif, Abdul R.; Ahmed, Nikhat
Abstract
J. Neurochem. (2012) 121, 954963. Abstract Alzheimers disease (AD) is the most common form of dementia and cognitive impairment usually characterized by widespread neurodegeneration throughout the association cortex, limbic system and hippocampus. Aberrant protein phosphorylation is a defining pathological hallmark of AD and implicated in the dysregulation of major cellular processes through highly dynamic and complex signaling pathways. Here in, we demonstrate 81 proteins, of 600 spots selected, unambiguously identified as phosphorylated, providing a partial phosphoproteome profile of AD substantia nigra and cortex and respective control brain regions. More importantly, abnormal phosphorylation signal intensity of nine physiologically important proteins observed can profoundly affect cell metabolism, signal transduction, cytoskeleton integration, and synaptic function and accounts for biological and morphological alterations. Our studies employed two-dimensional gel electrophoresis for protein separation, Pro-Q (R) Diamond phosphoprotein staining and electrospray ionization quadrupole time of flight tandem MS for protein identification. NetPhosk 1.0 is used for the confirmation of protein modification status as well known/putative phosphoproteins. A further insight into the links among the identified phosphoproteins and functional roles STRING 8.3, KEGG and REACTOME pathway databases were applied. The present quantitative phosphoproteomic analysis can be supportive in establishing a broad database of potential protein targets of abnormal phosphorylation in AD brain.
Issue Date
2012
Status
published
Publisher
Wiley-blackwell
Journal
Journal of Neurochemistry 
ISSN
0022-3042
Sponsor
Higher Education Commission, Pakistan [20-560/ RD/07]

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