The role of HSP90 molecular chaperones in hepatocellular carcinoma
Misfolded proteins have enhanced formation of toxic oligomers and nonfunctional protein copies lead to recruiting wild‐type protein types. Heat shock protein 90 (HSP90) is a molecular chaperone generated by cells that are involved in many cellular functions through regulation of folding and/or local...
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| Veröffentlicht in: | Journal of cellular physiology 2020-12, Vol.235 (12), p.9110-9120 |
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| container_title | Journal of cellular physiology |
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| creator | Nouri‐Vaskeh, Masoud Alizadeh, Leila Hajiasgharzadeh, Khalil Mokhtarzadeh, Ahad Halimi, Monireh Baradaran, Behzad |
| description | Misfolded proteins have enhanced formation of toxic oligomers and nonfunctional protein copies lead to recruiting wild‐type protein types. Heat shock protein 90 (HSP90) is a molecular chaperone generated by cells that are involved in many cellular functions through regulation of folding and/or localization of large multi‐protein complexes as well as client proteins. HSP90 can regulate a number of different cellular processes including cell proliferation, motility, angiogenesis, signal transduction, and adaptation to stress. HSP90 makes the mutated oncoproteins able to avoid misfolding and degradation and permits the malignant transformation. As a result, HSP90 is an important factor in several signaling pathways associated with tumorigenicity, therapy resistance, and inhibiting apoptosis. Clinically, the upregulation of HSP90 expression in hepatocellular carcinoma (HCC) is linked with advanced stages and inappropriate survival in cases suffering from this kind of cancer. The present review comprehensively assesses HSP90 functions and its possible usefulness as a potential diagnostic biomarker and therapeutic option for HCC.
The main focus of this study is the structural, mechanistic, and therapeutic studies that have been conducted to explain how heat shock protein 90 molecular chaperone and its inhibitors act on different processes involved in hepatocellular carcinoma development and progression. |
| doi_str_mv | 10.1002/jcp.29776 |
| format | Article |
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The main focus of this study is the structural, mechanistic, and therapeutic studies that have been conducted to explain how heat shock protein 90 molecular chaperone and its inhibitors act on different processes involved in hepatocellular carcinoma development and progression.</description><identifier>ISSN: 0021-9541</identifier><identifier>EISSN: 1097-4652</identifier><identifier>DOI: 10.1002/jcp.29776</identifier><identifier>PMID: 32452023</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>Angiogenesis ; Apoptosis ; Biomarkers ; Cancer ; Carcinoma, Hepatocellular - metabolism ; Cell proliferation ; Cell Proliferation - physiology ; Cell Transformation, Neoplastic - metabolism ; chaperone proteins ; Chaperones ; Diagnostic systems ; heat shock protein 90 ; Heat shock proteins ; Hepatocellular carcinoma ; HSP90 Heat-Shock Proteins - metabolism ; Hsp90 protein ; Humans ; Liver cancer ; Liver Neoplasms - metabolism ; Localization ; Oligomers ; Protein folding ; Proteins ; Signal processing ; Signal Transduction ; Tumorigenicity</subject><ispartof>Journal of cellular physiology, 2020-12, Vol.235 (12), p.9110-9120</ispartof><rights>2020 Wiley Periodicals, Inc.</rights><rights>2020 Wiley Periodicals LLC</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3536-b0ad937ed203e10cda043c71c3ed23fe2528e7fafdae8e3aa026c0b5686b161c3</citedby><cites>FETCH-LOGICAL-c3536-b0ad937ed203e10cda043c71c3ed23fe2528e7fafdae8e3aa026c0b5686b161c3</cites><orcidid>0000-0002-6656-0292 ; 0000-0002-8642-6795 ; 0000-0003-4593-4803</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjcp.29776$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjcp.29776$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,778,782,1414,27911,27912,45561,45562</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32452023$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nouri‐Vaskeh, Masoud</creatorcontrib><creatorcontrib>Alizadeh, Leila</creatorcontrib><creatorcontrib>Hajiasgharzadeh, Khalil</creatorcontrib><creatorcontrib>Mokhtarzadeh, Ahad</creatorcontrib><creatorcontrib>Halimi, Monireh</creatorcontrib><creatorcontrib>Baradaran, Behzad</creatorcontrib><title>The role of HSP90 molecular chaperones in hepatocellular carcinoma</title><title>Journal of cellular physiology</title><addtitle>J Cell Physiol</addtitle><description>Misfolded proteins have enhanced formation of toxic oligomers and nonfunctional protein copies lead to recruiting wild‐type protein types. Heat shock protein 90 (HSP90) is a molecular chaperone generated by cells that are involved in many cellular functions through regulation of folding and/or localization of large multi‐protein complexes as well as client proteins. HSP90 can regulate a number of different cellular processes including cell proliferation, motility, angiogenesis, signal transduction, and adaptation to stress. HSP90 makes the mutated oncoproteins able to avoid misfolding and degradation and permits the malignant transformation. As a result, HSP90 is an important factor in several signaling pathways associated with tumorigenicity, therapy resistance, and inhibiting apoptosis. Clinically, the upregulation of HSP90 expression in hepatocellular carcinoma (HCC) is linked with advanced stages and inappropriate survival in cases suffering from this kind of cancer. The present review comprehensively assesses HSP90 functions and its possible usefulness as a potential diagnostic biomarker and therapeutic option for HCC.
The main focus of this study is the structural, mechanistic, and therapeutic studies that have been conducted to explain how heat shock protein 90 molecular chaperone and its inhibitors act on different processes involved in hepatocellular carcinoma development and progression.</description><subject>Angiogenesis</subject><subject>Apoptosis</subject><subject>Biomarkers</subject><subject>Cancer</subject><subject>Carcinoma, Hepatocellular - metabolism</subject><subject>Cell proliferation</subject><subject>Cell Proliferation - physiology</subject><subject>Cell Transformation, Neoplastic - metabolism</subject><subject>chaperone proteins</subject><subject>Chaperones</subject><subject>Diagnostic systems</subject><subject>heat shock protein 90</subject><subject>Heat shock proteins</subject><subject>Hepatocellular carcinoma</subject><subject>HSP90 Heat-Shock Proteins - metabolism</subject><subject>Hsp90 protein</subject><subject>Humans</subject><subject>Liver cancer</subject><subject>Liver Neoplasms - metabolism</subject><subject>Localization</subject><subject>Oligomers</subject><subject>Protein folding</subject><subject>Proteins</subject><subject>Signal processing</subject><subject>Signal Transduction</subject><subject>Tumorigenicity</subject><issn>0021-9541</issn><issn>1097-4652</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMFKw0AQhhdRbK0efAEJePKQdnY32SRHLWqVggXredlsJjQlycbdhtK3dzXVm6dh5v_4Bz5CrilMKQCbbXU3ZVmSiBMyppAlYSRidkrGPqNhFkd0RC6c2wJAlnF-TkacRTEDxsfkYb3BwJoaA1MGi_dVBkHjN93XygZ6ozq0pkUXVG2wwU7tjMa6HkJlddWaRl2Ss1LVDq-Oc0I-nh7X80W4fHt-md8vQ81jLsIcVJHxBAsGHCnoQkHEdUI19ydeIotZikmpykJhilwpYEJDHotU5FR4bEJuh97Oms8e3U5uTW9b_1KyKBIpcJqmnrobKG2NcxZL2dmqUfYgKchvW9Lbkj-2PHtzbOzzBos_8lePB2YDsK9qPPzfJF_nq6HyC9ckcuM</recordid><startdate>202012</startdate><enddate>202012</enddate><creator>Nouri‐Vaskeh, Masoud</creator><creator>Alizadeh, Leila</creator><creator>Hajiasgharzadeh, Khalil</creator><creator>Mokhtarzadeh, Ahad</creator><creator>Halimi, Monireh</creator><creator>Baradaran, Behzad</creator><general>Wiley Subscription Services, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><orcidid>https://orcid.org/0000-0002-6656-0292</orcidid><orcidid>https://orcid.org/0000-0002-8642-6795</orcidid><orcidid>https://orcid.org/0000-0003-4593-4803</orcidid></search><sort><creationdate>202012</creationdate><title>The role of HSP90 molecular chaperones in hepatocellular carcinoma</title><author>Nouri‐Vaskeh, Masoud ; Alizadeh, Leila ; Hajiasgharzadeh, Khalil ; Mokhtarzadeh, Ahad ; Halimi, Monireh ; Baradaran, Behzad</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3536-b0ad937ed203e10cda043c71c3ed23fe2528e7fafdae8e3aa026c0b5686b161c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Angiogenesis</topic><topic>Apoptosis</topic><topic>Biomarkers</topic><topic>Cancer</topic><topic>Carcinoma, Hepatocellular - metabolism</topic><topic>Cell proliferation</topic><topic>Cell Proliferation - physiology</topic><topic>Cell Transformation, Neoplastic - metabolism</topic><topic>chaperone proteins</topic><topic>Chaperones</topic><topic>Diagnostic systems</topic><topic>heat shock protein 90</topic><topic>Heat shock proteins</topic><topic>Hepatocellular carcinoma</topic><topic>HSP90 Heat-Shock Proteins - metabolism</topic><topic>Hsp90 protein</topic><topic>Humans</topic><topic>Liver cancer</topic><topic>Liver Neoplasms - metabolism</topic><topic>Localization</topic><topic>Oligomers</topic><topic>Protein folding</topic><topic>Proteins</topic><topic>Signal processing</topic><topic>Signal Transduction</topic><topic>Tumorigenicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nouri‐Vaskeh, Masoud</creatorcontrib><creatorcontrib>Alizadeh, Leila</creatorcontrib><creatorcontrib>Hajiasgharzadeh, Khalil</creatorcontrib><creatorcontrib>Mokhtarzadeh, Ahad</creatorcontrib><creatorcontrib>Halimi, Monireh</creatorcontrib><creatorcontrib>Baradaran, Behzad</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Journal of cellular physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nouri‐Vaskeh, Masoud</au><au>Alizadeh, Leila</au><au>Hajiasgharzadeh, Khalil</au><au>Mokhtarzadeh, Ahad</au><au>Halimi, Monireh</au><au>Baradaran, Behzad</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The role of HSP90 molecular chaperones in hepatocellular carcinoma</atitle><jtitle>Journal of cellular physiology</jtitle><addtitle>J Cell Physiol</addtitle><date>2020-12</date><risdate>2020</risdate><volume>235</volume><issue>12</issue><spage>9110</spage><epage>9120</epage><pages>9110-9120</pages><issn>0021-9541</issn><eissn>1097-4652</eissn><abstract>Misfolded proteins have enhanced formation of toxic oligomers and nonfunctional protein copies lead to recruiting wild‐type protein types. Heat shock protein 90 (HSP90) is a molecular chaperone generated by cells that are involved in many cellular functions through regulation of folding and/or localization of large multi‐protein complexes as well as client proteins. HSP90 can regulate a number of different cellular processes including cell proliferation, motility, angiogenesis, signal transduction, and adaptation to stress. HSP90 makes the mutated oncoproteins able to avoid misfolding and degradation and permits the malignant transformation. As a result, HSP90 is an important factor in several signaling pathways associated with tumorigenicity, therapy resistance, and inhibiting apoptosis. Clinically, the upregulation of HSP90 expression in hepatocellular carcinoma (HCC) is linked with advanced stages and inappropriate survival in cases suffering from this kind of cancer. The present review comprehensively assesses HSP90 functions and its possible usefulness as a potential diagnostic biomarker and therapeutic option for HCC.
The main focus of this study is the structural, mechanistic, and therapeutic studies that have been conducted to explain how heat shock protein 90 molecular chaperone and its inhibitors act on different processes involved in hepatocellular carcinoma development and progression.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>32452023</pmid><doi>10.1002/jcp.29776</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-6656-0292</orcidid><orcidid>https://orcid.org/0000-0002-8642-6795</orcidid><orcidid>https://orcid.org/0000-0003-4593-4803</orcidid></addata></record> |
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| subjects | Angiogenesis Apoptosis Biomarkers Cancer Carcinoma, Hepatocellular - metabolism Cell proliferation Cell Proliferation - physiology Cell Transformation, Neoplastic - metabolism chaperone proteins Chaperones Diagnostic systems heat shock protein 90 Heat shock proteins Hepatocellular carcinoma HSP90 Heat-Shock Proteins - metabolism Hsp90 protein Humans Liver cancer Liver Neoplasms - metabolism Localization Oligomers Protein folding Proteins Signal processing Signal Transduction Tumorigenicity |
| title | The role of HSP90 molecular chaperones in hepatocellular carcinoma |
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