Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?

Choi, Seongjin; Kam, Heejin; Kim, Kye-Young; Park, Suk In; Lee, Yun‐Sil

doi:10.3390/cancers11081195

Cited by 87 publications

(83 citation statements)

References 95 publications

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“…Induced by heat shock, environmental, and pathophysiological stressors, HSP27 forms multimeric complexes and stabilize denatured or aggregated proteins and return them to their original form [14]. Other functions of HSP27 include direct interference with apoptotic pathway and regulation of cytoskeleton dynamics [15,16]. Whereas its primary function is to promote cellular homeostasis under stressor conditions, overexpression of HSP27 is closely related to tumorigenesis, metastasis, and invasiveness in various cancers such as head and neck squamous cell carcinoma, pediatric acute myeloid leukemia, breast cancer, and colorectal cancer [17][18][19][20].…”

Section: Role Of Hsp27 As An Upstream Regulator Of Oncogenic Pathwaysmentioning

confidence: 99%

Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy

Yun

Kim

Lim

et al. 2019

Cells

210

158

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Heat shock proteins (HSPs) constitute a large family of molecular chaperones classified by their molecular weights, and they include HSP27, HSP40, HSP60, HSP70, and HSP90. HSPs function in diverse physiological and protective processes to assist in maintaining cellular homeostasis. In particular, HSPs participate in protein folding and maturation processes under diverse stressors such as heat shock, hypoxia, and degradation. Notably, HSPs also play essential roles across cancers as they are implicated in a variety of cancer-related activities such as cell proliferation, metastasis, and anti-cancer drug resistance. In this review, we comprehensively discuss the functions of HSPs in association with cancer initiation, progression, and metastasis and anti-cancer therapy resistance. Moreover, the potential utilization of HSPs to enhance the effects of chemo-, radio-, and immunotherapy is explored. Taken together, HSPs have multiple clinical usages as biomarkers for cancer diagnosis and prognosis as well as the potential therapeutic targets for anti-cancer treatment.

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Section: Role Of Hsp27 As An Upstream Regulator Of Oncogenic Pathwaysmentioning

confidence: 99%

Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy

Yun

Kim

Lim

et al. 2019

Cells

210

158

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“…It is generally accepted that HSP27 is implicated in oncogenesis and contributes to drug resistance and radioresistance of tumor cells [52,135,137]. First indications about a link between HSP27 and cancer stemness appeared in 2010: The small chaperone was shown to be involved in TGF-β1-induced EMT in lung cancer cells (A549 cell line) and this involvement was independent of Smad [138].…”

Section: Hsp27mentioning

confidence: 99%

Molecular Chaperones in Cancer Stem Cells: Determinants of Stemness and Potential Targets for Antitumor Therapy

Kabakov

Yakimova

Matchuk

2020

Cells

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Cancer stem cells (CSCs) are a great challenge in the fight against cancer because these self-renewing tumorigenic cell fractions are thought to be responsible for metastasis dissemination and cases of tumor recurrence. In comparison with non-stem cancer cells, CSCs are known to be more resistant to chemotherapy, radiotherapy, and immunotherapy. Elucidation of mechanisms and factors that promote the emergence and existence of CSCs and their high resistance to cytotoxic treatments would help to develop effective CSC-targeting therapeutics. The present review is dedicated to the implication of molecular chaperones (protein regulators of polypeptide chain folding) in both the formation/maintenance of the CSC phenotype and cytoprotective machinery allowing CSCs to survive after drug or radiation exposure and evade immune attack. The major cellular chaperones, namely heat shock proteins (HSP90, HSP70, HSP40, HSP27), glucose-regulated proteins (GRP94, GRP78, GRP75), tumor necrosis factor receptor-associated protein 1 (TRAP1), peptidyl-prolyl isomerases, protein disulfide isomerases, calreticulin, and also a transcription heat shock factor 1 (HSF1) initiating HSP gene expression are here considered as determinants of the cancer cell stemness and potential targets for a therapeutic attack on CSCs. Various approaches and agents are discussed that may be used for inhibiting the chaperone-dependent development/manifestations of cancer cell stemness.

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“…Many members of the HSP family play key roles in cell survival and the promotion of drug resistance [39,45,[91][92][93][94] (Table 1). Extracellular HSPs and EVs enriched with HSPs are thus a major aspect of the RASP.…”

Section: Exosomal Drug Resistancementioning

confidence: 99%

Exosome Release of Drugs: Coupling with Epithelial-Mesenchymal Transition

Eguchi¹,

Ono²,

Calderwood³

et al. 2019

Preprint

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Extracellular vesicles (EVs), such as exosomes or oncosomes are released with molecules unfavorable for survival from cells. In addition, accumulating evidence has shown that tumor cells often eject anti-cancer drugs such as chemotherapeutics and targeted drugs within EVs, a novel mechanism of drug resistance. The EV-releasing, drug resistance phenotype is often coupled with cellular dedifferentiation and transformation, cells undergoing epithelial-mesenchymal transition (EMT) and taking on a cancer stem cell phenotype. Recent studies have shown that the release of EVs is also involved in immunosuppression. The concept of the resistance-associated secretory phenotype (RASP) is reviewed herein.

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Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?

Cited by 87 publications

References 95 publications

Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy

Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy

Molecular Chaperones in Cancer Stem Cells: Determinants of Stemness and Potential Targets for Antitumor Therapy

Exosome Release of Drugs: Coupling with Epithelial-Mesenchymal Transition

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