Identification of Novel Cdc37 Interacting Proteins and Pathways in Human Alzheimers Disease Brain Tissue Using Mass SpectrometryMalathi Narayan1, Lisa Kirouac2, Dale Chaput3, Stanley Stevens3, Jaya Padmanabhan2 and Umesh K Jinwal1*
- *Corresponding Author:
- Umesh K Jinwal
Department of Pharmaceutical Sciences, College of Pharmacy
Byrd Alzheimer’s Institute, University of South Florida-Health
4001 E. Fletcher Ave, MDC36, Tampa, FL, 33613 USA
E-mail: [email protected]
Received Date: February 18, 2016 Accepted Date: March 01, 2016 Published Date: March 07, 2016
Citation: Narayan M, Kirouac L, Chaput D, Stevens S, Padmanabhan J, et al. (2016) Identification of Novel Cdc37 Interacting Proteins and Pathways in Human Alzheimer’s Disease Brain Tissue Using Mass Spectrometry. J Data Mining Genomics & Proteomics 7:193. doi: 10.4172/2153-0602.1000193
Copyright: © 2016 Narayan M, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Alzheimer’s disease (AD) is the most common form of dementia and the 6th leading cause of death in the United States. The major pathological hallmarks observed in AD include the formation of intracellular neurofibrillary tangles comprised of phosphorylated forms of the microtubule associated protein tau, and the deposition of extracellular plaques composed of amyloid beta. Cdc37 is a co-chaperone of Hsp90, which recruits client kinases to the Hsp90 complex for folding and stabilization. It has been previously shown that Cdc37 can not only bind and preserve tau, but also stabilize kinases that can phosphorylate tau. The goal of the current study was to identify novel Cdc37- interacting proteins in human AD tissue compared to normal tissue using an immunoprecipitation-based approach combined with mass spectrometry. We identified 39 unique proteins that interacted with Cdc37 in AD samples only and 7 proteins that interacted with Cdc37 in normal samples only. 39 proteins were found to bind Cdc37 in both AD and normal tissue. Of these, 18 showed increased interaction in AD tissue, 10 showed increased interaction in normal tissue and 11 showed equal nteraction in both samples. Ingenuity Pathway Analysis of the data indicates that these Cdc37-interacting proteins could signal through the p70S6K, PI3K / Akt, TGFß, ErbB, NF- kB, calmodulin, p38 MAPK and JNK pathways. Identification of these novel proteins and pathways linked to Cdc37 may indicate its role both as a non-kinase co-chaperone and in other pathways in the AD brain.