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Hsp90 and Co-Chaperones: Impact on Tumor Progression and Prospects for Molecular-Targeted Cancer Therapy Publisher Pubmed



Jafari A1, 2 ; Rezaeitavirani M2 ; Farhadihosseinabadi B3 ; Taranejoo S4 ; Zali H5
Authors
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Authors Affiliations
  1. 1. Student Research Committee, Shahid Beheshti University of Medical Sciences, Tehran, Iran
  2. 2. Proteomics Research Center, School of Allied Medical Sciences, Shahid Beheshti University of Medical Sciences, Tehran, Iran
  3. 3. Neuroscience Research Center (NRC), Iran University of Medical Sciences, Tehran, Iran
  4. 4. Wellman Centre for Photomedicine, Harvard-MIT Division of Health Sciences and Technology (HST), Boston, MA, United States
  5. 5. Department of Tissue engineering and applied cell, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran

Source: Cancer Investigation Published:2020


Abstract

Heat shock protein 90 (HSP90), a highly and unique chaperone, presents as a double-edged sword. It plays an essential role in many physiological and pathological processes, including tumor development. The current review highlights a recent understanding of the roles of HSP90 in molecular mechanisms underlying cancer survival and progression. HSP90 and its client proteins through the regulation of oncoproteins including signaling proteins, receptors, and transcriptional factors involved in tumorigenesis. It also has potential clinical application as diagnostic and prognostic biomarkers for assessing cancer progression. In this way, using HSP90 to develop new anticancer therapeutic agents including HSP90 inhibitors, anti-HSP90 antibody, and HSP90-based vaccines has been promising. © 2020, © 2020 Taylor & Francis Group, LLC.