Small Heat Shock Proteins in Cancers: Functions and Therapeutic Potential for Cancer Therapy

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Abstract

Small heat shock proteins (sHSPs) are ubiquitous ATP-independent chaperones that play essential roles in response to cellular stresses and protein homeostasis. Investigations of sHSPs reveal that sHSPs are ubiquitously expressed in numerous types of tumors, and their expression is closely associated with cancer progression. sHSPs have been suggested to control a diverse range of cancer functions, including tumorigenesis, cell growth, apoptosis, metastasis, and chemoresistance, as well as regulation of cancer stem cell properties. Recent advances in the field indicate that some sHSPs have been validated as a powerful target in cancer therapy. In this review, we present and highlight current understanding, recent progress, and future challenges of sHSPs in cancer development and therapy.

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Guidelines for the nomenclature of the human heat shock proteins.

Elspeth Bruford, Jurre Hageman, J T W M Vos … (2008)

The expanding number of members in the various human heat shock protein (HSP) families and the inconsistencies in their nomenclature have often led to confusion. Here, we propose new guidelines for the nomenclature of the human HSP families, HSPH (HSP110), HSPC (HSP90), HSPA (HSP70), DNAJ (HSP40), and HSPB (small HSP) as well as for the human chaperonin families HSPD/E (HSP60/HSP10) and CCT (TRiC). The nomenclature is based largely on the more consistent nomenclature assigned by the HUGO Gene Nomenclature Committee and used in the National Center of Biotechnology Information Entrez Gene database for the heat shock genes. In addition to this nomenclature, we provide a list of the human Entrez Gene IDs and the corresponding Entrez Gene IDs for the mouse orthologs.

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Small heat shock proteins: Simplicity meets complexity

Martin Haslbeck, Sevil Weinkauf, Johannes Buchner (2019)

Small heat shock proteins (sHsps) are a ubiquitous and ancient family of ATP-independent molecular chaperones. A key characteristic of sHsps is that they exist in ensembles of iso-energetic oligomeric species differing in size. This property arises from a unique mode of assembly involving several parts of the subunits in a flexible manner. Current evidence suggests that smaller oligomers are more active chaperones. Thus, a shift in the equilibrium of the sHsp ensemble allows regulating the chaperone activity. Different mechanisms have been identified that reversibly change the oligomer equilibrium. The promiscuous interaction with non-native proteins generates complexes that can form aggregate-like structures from which native proteins are restored by ATP-dependent chaperones such as Hsp70 family members. In recent years, this basic paradigm has been expanded, and new roles and new cofactors, as well as variations in structure and regulation of sHsps, have emerged.

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Quercetin and cancer: new insights into its therapeutic effects on ovarian cancer cells

Asma Vafadar, Zahra Shabaninejad, Ahmad Movahedpour … (2020)

Ovarian cancer is known as a serious malignancy that affects women’s reproductive tract and can considerably threat their health. A wide range of molecular mechanisms and genetic modifications have been involved in ovarian cancer pathogenesis making it difficult to develop effective therapeutic platforms. Hence, discovery and developing new therapeutic approaches are required. Medicinal plants, as a new source of drugs, could potentially be used alone or in combination with other medicines in the treatment of various cancers such as ovarian cancer. Among various natural compounds, quercetin has shown great anti-cancer and anti-inflammatory properties. In vitro and in vivo experiments have revealed that quercetin possesses a cytotoxic impact on ovarian cancer cells. Despite obtaining good results both in vitro and in vivo, few clinical studies have assessed the anti-cancer effects of quercetin particularly in the ovarian cancer. Therefore, it seems that further clinical studies may introduce quercetin as therapeutic agent alone or in combination with other chemotherapy drugs to the clinical setting. Here, we not only summarize the anti-cancer effects of quercetin but also highlight the therapeutic effects of quercetin in the ovarian cancer.

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Journal

Journal ID (nlm-ta): Int J Mol Sci

Journal ID (iso-abbrev): Int J Mol Sci

Journal ID (publisher-id): ijms

Title: International Journal of Molecular Sciences

Publisher: MDPI

ISSN (Electronic): 1422-0067

Publication date (Electronic): 10 September 2020

Publication date Collection: September 2020

Volume: 21

Issue: 18

Electronic Location Identifier: 6611

Affiliations

Department of Pharmacology and Shenzhen University International Cancer Center, Shenzhen University School of Medicine, Shenzhen 518039, China; liyuting@ 123456szu.edu.cn (Y.L.); tanxiangyu@ 123456szu.edu.cn (X.T.)

Author notes

[* ]Correspondence: xiongjixian@ 123456szu.edu.cn (J.X.); gracelfu@ 123456szu.edu.cn (L.F.); Tel.: +86-755-8667-0623 (J.X.); +86-755-8667-1992 (L.F.)

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Jixian Xiong https://orcid.org/0000-0003-3154-250X

Li Fu https://orcid.org/0000-0003-2643-6278

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Publisher ID: ijms-21-06611

DOI: 10.3390/ijms21186611

PMC ID: 7555140

PubMed ID: 32927696

SO-VID: 5626092c-09d2-448a-8751-a512adc4c152

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Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

Small Heat Shock Proteins in Cancers: Functions and Therapeutic Potential for Cancer Therapy

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Higher order chromatin architecture

Most cited references 162

Guidelines for the nomenclature of the human heat shock proteins.

Small heat shock proteins: Simplicity meets complexity

Quercetin and cancer: new insights into its therapeutic effects on ovarian cancer cells

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