4.2 Review

HSP90 and Co-chaperones: Impact on Tumor Progression and Prospects for Molecular-Targeted Cancer Therapy

Journal

CANCER INVESTIGATION
Volume 38, Issue 5, Pages 310-328

Publisher

TAYLOR & FRANCIS INC
DOI: 10.1080/07357907.2020.1752227

Keywords

HSP90 inhibitor; cancer; targeted therapy; tumor biomarker; client protein

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Funding

  1. Student Research Committee, Shahid Beheshti University of Medical Sciences, Tehran, Iran [1397/68917]
  2. Student Research Committee and Research AMP
  3. Technology Chancellor in Shahid Beheshti University of Medical Sciences

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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.

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