Heat Shock Proteins and Cancer.

Heat shock proteins (HSPs) constitute a large family of proteins involved in protein folding and maturation whose expression is induced by heat shock or other stressors. The major groups are classified based on their molecular weights and include HSP27, HSP40, HSP60, HSP70, HSP90, and large HSPs. HSPs play a significant role in cellular proliferation, differentiation, and carcinogenesis. In this article we comprehensively review the roles of major HSPs in cancer biology and pharmacology. HSPs are thought to play significant roles in the molecular mechanisms leading to cancer development and metastasis. HSPs may also have potential clinical uses as biomarkers for cancer diagnosis, for assessing disease progression, or as therapeutic targets for cancer therapy.

Wu J ，Liu T ，Rios Z ，Mei Q ，Lin X ，Cao S ... -  《-》

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

Yun CW ，Kim HJ ，Lim JH ，Lee SH ... -  《Cells》

Targeting heat shock protein 90 for anti-cancer drug development.

Heat shock proteins (HSPs) constitute a large family of proteins involved in protein folding and maturation. HSP expression is induced by heat shock or other stressors including cellular damage and hypoxia. The major groups, which are classified based on their molecular weight, include HSP27, HSP40, HSP60, HSP70, HSP90, and large HSP (HSP110 and glucose-regulated protein 170). HSPs play a significant role in cellular proliferation, differentiation, survival, apoptosis, and carcinogenesis. The human HSP90 family consists of five members and has a strong association with cancer. The primary objective is to review the important functions of heat shock protein 90 in cancer, especially as an anti-cancer drug target. The HSP90 proteins not only play important roles in cancer development, progression, and metastasis, but also have potential clinical use as biomarkers for cancer diagnosis or assessing disease progression, and as therapeutic targets for cancer therapy. In this chapter, we discuss the roles of HSP90 in cancer biology and pharmacology, focusing on HSP90 as an anti-cancer drug target. An understanding of the functions and molecular mechanisms of HSP90 is critical for enhancing the accuracy of cancer diagnosis as well as for developing more effective and less toxic chemotherapeutic agents. We have provided an overview of the complex relationship between cancer and HSP90. HSP90 proteins play an important role in tumorigenesis and may be used as potential clinical biomarkers for the diagnosis and predicting prognostic outcome of patients with cancer. HSP90 proteins may be used as therapeutic targets for cancer therapy, prompting discovery and development of novel chemotherapeutic agents.

Aswad A ，Liu T 《-》

Clinical, Prognostic and Therapeutic Significance of Heat Shock Proteins in Cancer.

Heat Shock Proteins (HSPs) constitute a group of proteins that play a crucial role in the process of protein folding. HSPs are also known to modulate a number of key apoptotic factors. High expression of these proteins is reported in an array of cancers, such as breast, prostate, colorectal, lung, ovarian, gastric, oral and esophageal cancer. Ample amount of investigations were carried out on a variety of cancers suggesting HSPs as a promising hallmark in cancers. Their expression profile in several tumors elucidates that they help in proliferation, invasion, metastasis and death of cancerous cells. Detection of the levels of heat shock proteins and their specific antibodies in the sera of diseased individuals can play an important role in cancer diagnosis. This review will present and summarize latest research being carried out on heat shock proteins. It will also highlight the clinical and prognostic features of HSP27, HSP60, HSP70, HSP90 and HSP110, and will discuss future implications of HSPs in the diagnosis and prognosis of cancer. Furthermore, the role of heat shock proteins as a therapeutic target in cancer will be discussed. In addition, the review article will report various studies, where HSPs have been targeted for their therapeutic potential. In summary, multiple experimental investigations have been successful in suggesting the role of heat shock protein as a clinical biomarker and therapeutic target in cancer. HSPs are associated with a number of cancer hallmarks such as cell proliferation, invasion and metastasis. Inhibition of HSPs has resulted in successful therapeutic outcome in cancer. It has served as a novel anti-cancer therapy for the treatment of several cancer forms. However, more experimental studies are required to elucidate the reliability and efficacy of heat shock proteins in combination with other conventional markers for cancer diagnosis and prognosis. Novel and effective interventions through HSP inhibition are expected to decrease the burden of cancer in the near future.

Saini J ，Sharma PK 《-》

Recent advances in heat shock proteins in cancer diagnosis, prognosis, metabolism and treatment.

Heat shock proteins (HSPs) are a group of proteins, also known as molecular chaperones, which participate in protein folding and maturation in response to stresses or high temperature. According to their molecular weights, mammalian HSPs are classified into HSP27, HSP40, HSP60, HSP70, HSP90, and large HSPs. Previous studies have revealed that HSPs play important roles in oncogenesis and malignant progression because they can modulate all six hallmark traits of cancer. Because of this, HSPs have been propelled into the spotlight as biomarkers for cancer diagnosis and prognosis, as well as an exciting anticancer drug target. However, the relationship between the expression level of HSPs and their activity and cancer diagnosis, prognosis, metabolism and treatment is not clear and has not been completely established. Herein, this review summarizes and discusses recent advances and perspectives in major HSPs as biomarkers for cancer diagnosis, as regulators for cancer metabolism or as therapeutic targets for cancer therapy, which may provide new directions to improve the accuracy of cancer diagnosis and develop more effective and safer anticancer therapeutics.

Yang S ，Xiao H ，Cao L 《-》