Phosphorylated Hsp27 promotes adriamycin resistance in breast cancer cells through regulating dual phosphorylation of c-Myc

Bi, Xiaowen; Zhang, Miao; Zhou, Jinyi; Yan, Xintong; Cheng, Lixia; Luo, Lan; Huang, Chunhong; Yin, Zhimin

doi:10.1016/j.cellsig.2023.110913

Cited by 3 publications

(3 citation statements)

References 56 publications

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“…The overexpression of Hsp27 in AS-B145 or BT-474 breast cancer cells diminished the inhibitory effect of ovatodiolide on mammosphere formation [26], while the phosphorylation of Hsp27 at Ser15 promoted its Ser78 phosphorylation and enhanced the nuclear localization of HER2 to induce Trastuzumab (TZMB) resistance in HER2 + breast cancer cells [27]. Hsp27-overexpressing KT breast cancer cells showed increased resistance to ultraviolet ray C (UVC) and interferon lethality [28], and our recent study also found that phosphorylated Hsp27 promoted ADR resistance in MCF-7 and MDA-MB-231 breast cancer cells by regulating DNA damage repair protein c-Myc dual phosphorylation [29]. A proposed model of Hsp27 in breast cancer development is illustrated in Figure 2.…”

Section: Hsp27mentioning

confidence: 90%

Heat Shock Proteins and Breast Cancer

Zhang,

2024

IJMS

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Heat shock proteins (Hsps) are a group of stress-induced proteins involved in protein folding and maturation. Based on their molecular weight, Hsps can be divided into six families: small Hsps, Hsp40, Hsp60, Hsp70, Hsp90, and large Hsps. In the process of breast cancer tumorigenesis, Hsps play a central role in regulating cell reactions and functions including proliferation, metastasis, and apoptosis. Moreover, some of the critical Hsps also regulate the fine balance between the protective and destructive immunological responses within the tumor microenvironment. In this review, we systematically summarize the roles of major Hsps in breast cancer biology and point out the potential uses of these proteins in breast cancer diagnosis and therapy. Understanding the roles of different families of Hsps in breast cancer pathogenesis will help in the development of more effective prevention and treatment measures for breast cancer.

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Section: Hsp27mentioning

confidence: 90%

Heat Shock Proteins and Breast Cancer

Zhang,

2024

IJMS

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Section: Hsp27 Mediates Resistance To a Wide Range Of Chemotherapeuticsmentioning

confidence: 99%

“…A recent study on MCF7 breast cancer cells gave consistent results and provided new insight. Bi et al [81] have shown that the phosphorylation of Hsp27 preceded by exposure to DOX led to the upregulation of c-Myc in the nucleus, causing ataxiatelangiectasia mutated (ATM) kinase activation and which further negatively affected p53 (Figure 2). Another agent in the resistance to which Hsp27 has been found implicated is trastuzumab, also known as herceptin, a monoclonal antibody targeting human epidermal growth factor receptor 2 (HER2), which is overexpressed in up to 30% of invasive breast cancer cases and also in some gastric cancer subtypes.…”

Section: Hsp27 Mediates Resistance To a Wide Range Of Chemotherapeuticsmentioning

confidence: 99%

Heat Shock Proteins, a Double-Edged Sword: Significance in Cancer Progression, Chemotherapy Resistance and Novel Therapeutic Perspectives

Kunachowicz,

Król-Kulikowska,

Raczycka

et al. 2024

Cancers

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Heat shock proteins (Hsps) are involved in one of the adaptive mechanisms protecting cells against environmental and metabolic stress. Moreover, the large role of these proteins in the carcinogenesis process, as well as in chemoresistance, was noticed. This review aims to draw attention to the possibilities of using Hsps in developing new cancer therapy methods, as well as to indicate directions for future research on this topic. In order to discuss this matter, a thorough review of the latest scientific literature was carried out, taking into account the importance of selected proteins from the Hsp family, including Hsp27, Hsp40, Hsp60, Hsp70, Hsp90 and Hsp110. One of the more characteristic features of all Hsps is that they play a multifaceted role in cancer progression, which makes them an obvious target for modern anticancer therapy. Some researchers emphasize the importance of directly inhibiting the action of these proteins. In turn, others point to their possible use in the design of cancer vaccines, which would work by inducing an immune response in various types of cancer. Due to these possibilities, it is believed that the use of Hsps may contribute to the progress of oncoimmunology, and thus help in the development of modern anticancer therapies, which would be characterized by higher effectiveness and lower toxicity to the patients.

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Heat shock protein 27 downregulation attenuates isoprenaline-induced myocardial fibrosis and diastolic dysfunction by modulating the endothelial-mesenchymal transition

Zou,

Shi,

et al. 2024

Biochemical Pharmacology

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Phosphorylated Hsp27 promotes adriamycin resistance in breast cancer cells through regulating dual phosphorylation of c-Myc

Cited by 3 publications

References 56 publications

Heat Shock Proteins and Breast Cancer

Heat Shock Proteins and Breast Cancer

Heat Shock Proteins, a Double-Edged Sword: Significance in Cancer Progression, Chemotherapy Resistance and Novel Therapeutic Perspectives

Heat shock protein 27 downregulation attenuates isoprenaline-induced myocardial fibrosis and diastolic dysfunction by modulating the endothelial-mesenchymal transition

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