2015
DOI: 10.1007/978-3-319-17211-8_3
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Heat Shock Proteins and Cancer: Plant Based Therapy

Abstract: Cancer is one of the major causes of mortality in the world. Each year approximately 13 million people suffer from cancer disease, and approximately 60 % of them die because of cancer. Besides most of the patients response harmful side effects of chemo-and radiotherapies. Therefore the establishment of new therapeutic strategies for the treatment of cancers will be required. A number of studies have shown that some HSP are induced in specific tumor cells. For example, increased levels of HSP105, HSP90, HSP70, … Show more

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Cited by 7 publications
(4 citation statements)
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“…Graphs represents the mean ± SD (n = 6). *P < 0.05, **P < 0.01, ***P < 0.001 determined by oneway ANOVA using Dunnet's multiple comparison test resistance and poor prognosis (Samali and Cotter 1996;Bądziul et al 2014;Lianos et al 2015;Önay-Uçar 2015). Therefore, they act as negative prognostic markers in tumor cells.…”
Section: Discussionmentioning
confidence: 99%
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“…Graphs represents the mean ± SD (n = 6). *P < 0.05, **P < 0.01, ***P < 0.001 determined by oneway ANOVA using Dunnet's multiple comparison test resistance and poor prognosis (Samali and Cotter 1996;Bądziul et al 2014;Lianos et al 2015;Önay-Uçar 2015). Therefore, they act as negative prognostic markers in tumor cells.…”
Section: Discussionmentioning
confidence: 99%
“…Therefore, scientists and clinicians are still searching for better therapies for malignant gliomas. Since the therapeutic potential of reducing the abnormal levels of stress proteins (also known as heat shock proteins, Hsps) in diverse tumor cells have been revealed, Hsp-based therapies have become a significant target for new approaches against cancer (Jakubowicz-Gil et al 2010;Lianos et al 2015;Önay-Uçar 2015).…”
Section: Introductionmentioning
confidence: 99%
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“…The rationale for targeting HSP90 to treat cancer is based on multiple studies demonstrating that the biology of HSP90 in cancer cells is remarkably different from its basic functions in normal cells. Indeed, HSP90 is highly overexpressed in various cancers [28], complexing with other chaperones, oncogenic proteins, and cochaperones, and exhibiting ~200-fold higher affinity for ATP than homodimeric HSP90 in normal cells [29]. Importantly, the lower affinity shown by the uncomplexed form of HSP90 found in normal cells toward ATP and its competitive inhibitors provides a promising therapeutic window for developing new anticancer agents [19,30].…”
Section: Introductionmentioning
confidence: 99%