Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/891
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dc.contributor.authorSuri, Anil-
dc.contributor.authorJagadish, Nirmala-
dc.contributor.authorAgarwal, Sumit-
dc.contributor.authorGupta, Namita-
dc.contributor.authorFatima, Rukhsar-
dc.contributor.authorDevi, Sonika-
dc.contributor.authorKumar, Vikash-
dc.contributor.authorSuri, Vaishali-
dc.contributor.authorKumar, Rajive-
dc.contributor.authorSuri, Vitusha-
dc.contributor.authorSadasukhi, Trilok Chand-
dc.contributor.authorGupta, Anju-
dc.contributor.authorAnsari, Abdul S-
dc.contributor.authorLohiya, Nirmal Kumar-
dc.date.accessioned2017-03-24T07:43:25Z-
dc.date.available2017-03-24T07:43:25Z-
dc.date.issued2016-09-
dc.identifier.urihttp://hdl.handle.net/123456789/891-
dc.description.abstractBACKGROUND: Breast cancer is one of the leading cause of cancer-related deaths in women worldwide and increasing rapidly in developing countries. In the present study, we investigated the potential role and association of HSP70-2 with breast cancer. METHODS: HSP70-2 expression was examined in 154 tumor and 103 adjacent non-cancerous tissue (ANCT) specimens and breast cancer cell lines (MCF7, BT-474, SK-BR-3 and MDA-MB-231) by RT-PCR, quantitative-PCR, immunohistochemistry, Western blotting, flow cytometry and indirect immunofluorescence. Plasmid driven short hairpin RNA approach was employed to validate the role of HSP70-2 in cellular proliferation, senescence, migration, invasion and tumor growth. Further, we studied the effect of HSP70-2 protein ablation on signaling cascades involved in apoptosis, cell cycle and Epithelial-Mesenchymal-Transition both in culture as well as in-vivo human breast xenograft mouse model. RESULTS: HSP70-2 expression was detected in majority of breast cancer patients (83 %) irrespective of various histotypes, stages and grades. HSP70-2 expression was also observed in all breast cancer cells (BT-474, MCF7, MDA-MB-231 and SK-BR-3) used in this study. Depletion of HSP70-2 in MDA-MB-231 and MCF7 cells resulted in a significant reduction in cellular growth, motility, onset of apoptosis, senescence, cell cycle arrest as well as reduction of tumor growth in the xenograft model. At molecular level, down-regulation of HSP70-2 resulted in reduced expression of cyclins, cyclin dependent kinases, anti-apoptotic molecules and mesenchymal markers and enhanced expression of CDK inhibitors, caspases, pro-apoptotic molecules and epithelial markers. CONCLUSIONS: HSP70-2 is over expressed in breast cancer patients and was involved in malignant properties of breast cancer. This suggests HSP70-2 may be potential candidate molecule for development of better breast cancer treatment.en_US
dc.publisherBioMed Centralen_US
dc.titleHeat shock protein 70-2 (HSP70-2) overexpression in breast canceren_US
dc.keywordHSP70-2, Breast cancer, Gene silencing, Apoptosis, Tumor growthen_US
dc.journalJournal of Experimental & Clinical Cancer Researchen_US
dc.volumeno35en_US
dc.issueno1en_US
dc.pages150en_US
Appears in Collections:Genes and Proteins, Publications

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