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Article type: Research Article
Authors: Chakrabarti, Arunabha; 1 | Roy, Kasturi; 1 | Mukhopadhyay, Debashis; *
Affiliations: Structural Genomics Division, Saha Institute of Nuclear Physics, Kolkata, WB, India
Correspondence: [*] Correspondence to: Debashis Mukhopadhyay, Associate Professor, Structural Genomics Division, Saha Institute of Nuclear Physics. Postal address: 1/AF, Bidhannagar, Kolkata-700064, WB, India. Tel.: +91 33 2337 5345; Fax: +91 33 2337 4637; E-mail: [email protected].
Note: [1] These authors contributed equally to this manuscript.
Abstract: Amyloid-β protein precursor intracellular domain (AICD), which exerts intracellular effects by interacting with proteins involved in a plethora of biological processes, is a key player behind the pathophysiology of Alzheimer's disease (AD). Keeping in mind that overwhelming presence of AICD would mimic AD-like conditions in neuroblastoma cell lines, we hypothesized alteration in the proteomic expression pattern in these cells in the presence of AICD compared to their normal proteome. The rationale behind the study was to distinguish between symptomatic pathophysiological effects as opposed to any artifactual consequence due to protein overload in the cell lines. Using 2D-DIGE analysis and MALDI-MS identifications in neuro2A (mouse) and SHSY5Y (human) cell lines, we have identified several proteins belonging to different functional classes and involved in several biological pathways including protein folding, cytoskeletal dynamics, metabolism, and stress. Many of these were being upregulated or downregulated due to AICD effects and could be correlated directly with AD phenotypes.
Keywords: Alzheimer's disease, AβPP intracellular domain, 2D-DIGE, MALDI-MS, transfection
DOI: 10.3233/JAD-130695
Journal: Journal of Alzheimer's Disease, vol. 38, no. 4, pp. 845-855, 2014
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