Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/106286
Title: Brain site-specific proteome changes in aging-related dementia
Authors: Manavalan, Arulmani
Mishra, Manisha
Feng, Lin
Sze, Siu Kwan
Akatsu, Hiroyasu
Heese, Klaus
Keywords: DRNTU::Science::Biological sciences::Molecular biology
Issue Date: 2013
Source: Manavalan, A., Mishra, M., Feng, L., Sze, S. K., Akatsu, H., & Heese, K. (2013). Brain site-specific proteome changes in aging-related dementia. Experimental & molecular Medicine, 45(9), e39-.
Series/Report no.: Experimental & molecular medicine
Abstract: This study is aimed at gaining insights into the brain site-specific proteomic senescence signature while comparing physiologically aged brains with aging-related dementia brains (for example, Alzheimer’s disease (AD)). Our study of proteomic differences within the hippocampus (Hp), parietal cortex (pCx) and cerebellum (Cb) could provide conceptual insights into the molecular mechanisms involved in aging-related neurodegeneration. Using an isobaric tag for relative and absolute quantitation (iTRAQ)-based two-dimensional liquid chromatography coupled with tandem mass spectrometry (2D-LC-MS/MS) brain site-specific proteomic strategy, we identified 950 proteins in the Hp, pCx and Cb of AD brains. Of these proteins, 31 were significantly altered. Most of the differentially regulated proteins are involved in molecular transport, nervous system development, synaptic plasticity and apoptosis. Particularly, proteins such as Gelsolin (GSN), Tenascin-R (TNR) and AHNAK could potentially act as novel biomarkers of aging-related neurodegeneration. Importantly, our Ingenuity Pathway Analysis (IPA)-based network analysis further revealed ubiquitin C (UBC) as a pivotal protein to interact with diverse AD-associated pathophysiological molecular factors and suggests the reduced ubiquitin proteasome degradation system (UPS) as one of the causative factors of AD.
URI: https://hdl.handle.net/10356/106286
http://hdl.handle.net/10220/23994
ISSN: 2092-6413
DOI: 10.1038/emm.2013.76
Rights: © 2013 KSBMB. This work is licensed under a Creative Commons Attribution 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by/3.0/.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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