IJCM  Vol.11 No.2 , February 2020
Research Progress of Heat Shock Protein 90 and Hepatocellular Carcinoma
Abstract: Heat shock protein (HSP) is a kind of protein that mainly acts as a molecular chaperone to participate in the synthesis and folding of proteins, maintain the spatial conformation of proteins and protect cells from damage and other important biological functions. HSP90 plays an important role in maintaining molecular chaperone structure, regulating cell cycle and apoptosis, coordinating hormone signal transduction and promoting wound healing. And HSP90 also plays an important role in the occurrence and progression of tumors. In recent years, HSP90 inhibitors have made some achievements in molecular targeted therapy for malignant tumors, but further research is needed in clinical application. In this paper, the research status of the relationship between hepatocellular carcinoma targeted by heat shock protein 90 was reviewed.
Cite this paper: Jiang, Q. and Shen, X. (2020) Research Progress of Heat Shock Protein 90 and Hepatocellular Carcinoma. International Journal of Clinical Medicine, 11, 43-52. doi: 10.4236/ijcm.2020.112005.

[1]   Liu, H., Dicksved, J., et al. (2014) Heat Shock Proteins: Intestinal Gatekeepers That Are Influenced by Dietary Components and the Gut Microbiota. Pathogens, 1, 187-210.

[2]   Ritossa, F. (1962) A New Puffing Pattern Induced by Temperature Shock and DNP Indrosophila. Experientia, 12, 571-573.

[3]   Young, J.C., et al. (2001) Hsp90: A Specialized but Essential Protein-Folding Tool. Journal of Cell Biology, 2, 267-273.

[4]   Wu, S.H., Cheng, J. and Zheng, Y.J. (2005) Relationship between Heat Shock Protein Family and Liver Cancer. World Journal of Chinese Digestion, No. 14, 87-92.

[5]   Ali, M.M.U., et al. (2006) Crystal Structure of an Hsp90-Nucleotide-p23/Sbal Closed Chaperone Complex. Nature, 7087, 1013-1017.

[6]   Hellenkamp, B., Philipp, W. and Florian, K. (2017) Multidomain Structure and Correlated Dynamics Determined by Self-Consistent FRET Networks. Nature Methods, 14, 174-180.

[7]   Prodromou, C., et al. (1997) Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone. Cell, 1, 65-75.

[8]   Cheng, G. and Hu, W.X. (2009) Biological Characteristics of Heat Shock Protein 90. Chemistry of Life, 5, 687-690.

[9]   Andrija, F. and Pierre, G. (2013) Proteomic Data from Human Cell Cultures Refine Mechanisms of Chaperone-Mediated Protein Homeostasis. Cell Stress Chaperones, 5, 591-605.

[10]   Verba, K.A., et al. (2016) Atomic Structure of Hsp90-Cdc37-Cdk4 Reveals That Hsp90 Traps and Stabilizes an Unfolded Kinase. Science, 6293, 1542-1547.

[11]   Chen, Y., Wang, X. and Cao, C. (2017) Inhibition of HSP90 Sensitizes a Novel Raf/ERK Dual Inhibitor CY-9d in Triple-Negative Breast Cancer Cells. Oncotarget, 61, 104193-104205.

[12]   Stivarou, T., et al. (2016) Targeting Highly Expressed Extracellular HSP90 in Breast Cancer Stem Cells Inhibits Tumor Growth in Vitro and in Vivo. Cancer Biology & Therapy, 8, 799-812.

[13]   Lee, C.H., et al. (2012) Inhibition of Heat Shock Protein (Hsp) 27 Potentiates the Suppressive Effect of Hsp90 Inhibitors in Targeting Breast Cancer Stem-Like Cells. Biochimie, 6, 1382-1389.

[14]   Rong, B.X. and Yang, S.Y. (2018) Molecular Mechanism and Targeted Therapy of Hsp90 Involved in Lung Cancer: New Discoveries and Developments (Review). International Journal of Oncology, 2, 321-336.

[15]   Cedres, S., Felip, E. and Cruz, C. (2018) Activity of HSP90 Inhibiton in a Metastatic Lung Cancer Patient with a Germline BRCA1 Mutation. Journal of the National Cancer Institute, 8, 914-917.

[16]   Sun, Y., Huang, Y.H. and Huang, F.Y. (2018) 3’-epi-12beta-hydroxyfro-side, a New Cardenolide, Induces Cytoprotective Autophagy via Blocking the Hsp90/Akt/mTOR Axis in Lung Cancer Cells. Theranostics, 7, 2044-2060.

[17]   Dong, P.F. and Deng (2017) Clinical Significance of Serum Heat Shock Protein 90 α in Patients with Non-Small Cell Lung Cancer. Chinese General Medicine, 19, 2354-2357.

[18]   Sun, P.P. and Chen (2017) Research Progress of EGFR Targeted Therapy for Non-Small Cell Lung Cancer. International Respiratory Journal, 2, 148-151.

[19]   da Silva, V.C. and Ramos, C.H. (2012) The Network Interaction of the Human Cytosolic 90 kDa Heat Shock Protein Hsp90: A Target for Cancer Therapeutics. Journal of Proteomics, 10, 2790-2802.

[20]   White, P.T., et al. (2016) Novel HSP90 Inhibitors Effectively Target Functions of Thyroid Cancer Stem Cell Preventing Migration and Invasion. Surgery, 1, 142-151.

[21]   Lin, S.F., et al. (2017) Efficacy of an HSP90 Inhibitor, Ganetespib, in Preclinical Thyroid Cancer Models. Oncotarget, 25, 41294-41304.

[22]   Su, Y.H., et al. (2015) Targeting of Multiple Oncogenic Signaling Pathways by Hsp90 Inhibitor Alone or in Combination with Berberine for Treatment of Colorectal Cancer. Biochim Biophys Acta, 1853, 2261-2272.

[23]   Ma, W., et al. (2018) The Progress of Heat Shock Protein 90 in the Study of Gastric Cancer. Medical Science Journals of Central South China, 1, 98-112.

[24]   Cheng, Z.J., et al. (2015) Risk Factors and Management for Early and Late Intrahepatic Recurrence of Solitary Hepatocellular Carcinoma after Curative Resection. HPB, 5, 422-427.

[25]   Sohn, W., et al. (2014) HBV DNA and HBsAg Levels as Risk Predictors of Early and Late Recurrence after Curative Resection of HBV-Related Hepatocellular Carcinoma. Annals of Surgical Oncology, 7, 2429-2435.

[26]   Sun, S.P., et al. (2003) Sun Level, the Expression and Significance of HSP90 α in Hepatocellular Carcinoma. Chinese Journal of Basic and Clinical General Surgery, No. 3, 243-245.

[27]   Li, H., et al. (2014) The Significance of Heat Shock Protein 90 α Expression in HBV-Related Hepatocellular Carcinoma. Journal of Guangzhou Medical University, 42, 21-24.

[28]   Fu, Y., et al. (2017) Plasma Heat Shock Protein 90alpha as a Biomarker for the Diagnosis of Liver Cancer: An Official, Large-Scale, and Multicenter Clinical Trial. EBioMedicine, 24, 56-63.

[29]   Ochiana, S.O., Taldone, T. and Chiosis, G. (2014) Designing Drugs against Hsp90 for Cancer Therapy. In: Houry, W.A., Ed., the Molecular Chaperones Interaction Networks in Protein Folding and Degradation, Interactomics and Systems Biology, Vol. 1, Springer, Berlin, 151-183.

[30]   Patel, H.J., et al. (2011) Advances in the Discovery and Development of Heat-Shock Protein 90 Inhibitors for Cancer Treatment. Expert Opinion on Drug Discovery, 6, 559-587.

[31]   Supko, J.G., et al. (1995) Preclinical Pharmacologic Evaluation of Geldanamycin as an Antitumor Agent. Cancer Chemotherapy and Pharmacology, 36, 305-315.

[32]   Soga, S., et al. (2003) Development of Radicicol Analogues. Current Cancer Drug Targets, 3, 359-369.

[33]   Banerji, U., et al. (2005) Phase I Pharmacokinetic and Pharmacodynamic Study of 17-Allylamino 17-Demethoxygeldanamycin in Patients with Advanced Malignancies. Journal of Clinical Oncology, 23, 4152-4161.

[34]   Lancet, J.E., et al. (2010) Phase I Study of the Heat Shock Protein 90 Inhibitor Alvespimycin (KOS-1022, 17-DMAG) Administered Intravenously Twice Weekly to Patients with Acute Myeloid Leukemia. Leukemia, 24, 699-705.

[35]   Kummar, S., et al. (2010) Phase I Trial of 17-Dimethylaminoethylamino-17-Demethoxygeldanamycin (17-D.M.A.G.), a Heat Shock Protein Inhibitor, Administered Twice Weekly in Patients with Advanced Malignancies. European Journal of Cancer, 46, 340-347.

[36]   Brough, P.A., et al. (2008) 4,5-Diarylisoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents for the Treatment of Cancer. Journal of Medicinal Chemistry, 51, 196-218.

[37]   Shiotsu, Y., et al. (2000) Novel Oxime Derivatives of Radicicol Induce Erythroid Differentiation Associated with Preferential G(1) Phase Accumulation against Chronic Myelogenous Leukemia Cells through Destabilization of Bcr-Abl with Hsp90 Complex. Blood, 96, 2284-2291.

[38]   Chatterjee, S. and Burns, T.F. (2017) Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach. International Journal of Molecular Sciences, 18, 1978.

[39]   Augello, G., et al. (2019) Targeting HSP90 with the Small Molecule Inhibitor AUY922 (Luminespib) as a Treatment Strategy against Hepatocellular Carcinoma. International Journal of Cancer, 144, 2613-2624.