Anthony Aswad1, Tuoen Liu2. 1. Department of Biomedical Sciences, West Virginia School of Osteopathic Medicine, Lewisburg, WV, United States. 2. Department of Biomedical Sciences, West Virginia School of Osteopathic Medicine, Lewisburg, WV, United States. Electronic address: tliu@osteo.wvsom.edu.
Abstract
INTRODUCTION: 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. OBJECTIVES: The primary objective is to review the important functions of heat shock protein 90 in cancer, especially as an anti-cancer drug target. RESULTS: 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. CONCLUSION: 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.
INTRODUCTION: 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. OBJECTIVES: The primary objective is to review the important functions of heat shock protein 90 in cancer, especially as an anti-cancer drug target. RESULTS: 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. CONCLUSION: 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.
Authors: Francisco Tustumi; Gabriel Andrade Agareno; Ricardo Purchio Galletti; Rafael Benjamim Rosa da Silva; Julia Grams Quintas; Lucas de Abreu Sesconetto; Daniel José Szor; Nelson Wolosker Journal: Cells Date: 2022-08-27 Impact factor: 7.666