Journal of Proteomics & Bioinformatics
Open Access
ISSN: 0974-276X
ISSN: 0974-276X
Ahmed E Dhamad, Zhenqi Zhou, Jianhong Zhou and Yuchun Du
University of Arkansas, USA
Posters & Accepted Abstracts: J Proteomics Bioinform
Heat shock proteins (HSPs) are known to associate with Estrogen Receptors (ER) and regulate ER-mediated cell proliferation. Historically, the studies in this area have been focused on HSP90. However, some critical questions on the HSP-ER�± interactions remain unclear. In this study, through a quantitative proteomic method we found that 21 HSPs and three HSP co-chaperones were associated with ER�± in human cells. Four HSP70 family members, HSP70-1, HSC70, GRP75 and GRP78 were the predominate HSPs accounting for 78% of all identified ER�±-associated HSPs. Two HSP90 family members, HSP90�± and HSP90�² three HSP110 family members, HSP105, HSP4 and HSP4L were also identified to associate with ER�±, accounting for 8% and 6% of identified ER�±-associated HSPs respectively. The abundance of HSP90�± in the ER�±-complexes was two-fold of that of HSP90�². Among the reported HSP co-chaperones, we detected p23, FKBP51 and CHIP in the ER�±-containing protein complexes. Studies with the two most abundant ER�±-associated HSPs, HSP70-1 and HSC70 demonstrated that the two HSPs interacted with ER�± in the nucleus despite that the majority of them were localized in the cytoplasm. Further studies showed that a significant portion of HSP70-1 and HSC70 were associated with transcriptionally active and inactive chromatin in human breast cancer cells.
Ahmed E Dhamad has received his Bachelor’s degree in 2004 and completed his Master’s degree in Biological Science in 2006. He has worked as an Instructor for five years. He taught basically three subjects Biotechnology, Genetic Engineering, Immunology and Molecular Biology. Presently, He is a PhD candidate in Cell and Molecular Biology at the University of Arkansas, USA. He has published 4 papers and was involved in 3 conferences in USA.
Email: adhamad@email.uark.edu