High Mobility Group B Proteins, Their Partners, and Other Redox Sensors in Ovarian and Prostate Cancer
Cancer cells try to avoid the overproduction of reactive oxygen species by metabolic rearrangements. These cells also develop specific strategies to increase ROS resistance and to express the enzymatic activities necessary for ROS detoxification. Oxidative stress produces DNA damage and also induces...
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description | Cancer cells try to avoid the overproduction of reactive oxygen species by metabolic rearrangements. These cells also develop specific strategies to increase ROS resistance and to express the enzymatic activities necessary for ROS detoxification. Oxidative stress produces DNA damage and also induces responses, which could help the cell to restore the initial equilibrium. But if this is not possible, oxidative stress finally activates signals that will lead to cell death. High mobility group B (HMGB) proteins have been previously related to the onset and progressions of cancers of different origins. The protein HMGB1 behaves as a redox sensor and its structural changes, which are conditioned by the oxidative environment, are associated with different functions of the protein. This review describes recent advances in the role of human HMGB proteins and other proteins interacting with them, in cancerous processes related to oxidative stress, with special reference to ovarian and prostate cancer. Their participation in the molecular mechanisms of resistance to cisplatin, a drug commonly used in chemotherapy, is also revised. |
doi_str_mv | 10.1155/2016/5845061 |
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The protein HMGB1 behaves as a redox sensor and its structural changes, which are conditioned by the oxidative environment, are associated with different functions of the protein. This review describes recent advances in the role of human HMGB proteins and other proteins interacting with them, in cancerous processes related to oxidative stress, with special reference to ovarian and prostate cancer. Their participation in the molecular mechanisms of resistance to cisplatin, a drug commonly used in chemotherapy, is also revised.</description><identifier>ISSN: 1942-0900</identifier><identifier>EISSN: 1942-0994</identifier><identifier>DOI: 10.1155/2016/5845061</identifier><identifier>PMID: 26682011</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><subject>Amino acids ; Angiogenesis ; Animals ; Apoptosis ; Autophagy ; Biomedical research ; Cancer ; Chemotherapy ; Chromosomal proteins ; Deoxyribonucleic acid ; Development and progression ; DNA ; DNA damage ; DNA repair ; Enzymes ; Female ; Genes ; Genomes ; HMGB Proteins - metabolism ; Humans ; Immune system ; Kinases ; Localization ; Male ; Medical research ; Neoplasm Proteins - metabolism ; Ovarian Neoplasms - metabolism ; Ovarian Neoplasms - pathology ; Oxidation-Reduction ; Oxidative stress ; Prostate cancer ; Prostatic Neoplasms - metabolism ; Prostatic Neoplasms - pathology ; Proteins ; Reactive Oxygen Species - metabolism ; Review ; Sensors</subject><ispartof>Oxidative medicine and cellular longevity, 2016-01, Vol.2016 (2016), p.1-17</ispartof><rights>Copyright © 2016 Aida Barreiro-Alonso et al.</rights><rights>COPYRIGHT 2015 John Wiley & Sons, Inc.</rights><rights>Copyright © 2016 Aida Barreiro-Alonso et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2016 Aida Barreiro-Alonso et al. 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-f4ecfea574bea59e32e93400b997ca83ec0960bf9e92e383f83826218e2f05db3</citedby><cites>FETCH-LOGICAL-c499t-f4ecfea574bea59e32e93400b997ca83ec0960bf9e92e383f83826218e2f05db3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4670870/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4670870/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,886,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26682011$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Prasad, Sahdeo</contributor><creatorcontrib>Barreiro-Alonso, Aida</creatorcontrib><creatorcontrib>Lamas-Maceiras, Monica</creatorcontrib><creatorcontrib>Rodriguez-Belmonte, Esther</creatorcontrib><creatorcontrib>Vizoso-Vazquez, Angel</creatorcontrib><creatorcontrib>Quindos, Maria</creatorcontrib><creatorcontrib>Cerdan, M. Esperanza</creatorcontrib><title>High Mobility Group B Proteins, Their Partners, and Other Redox Sensors in Ovarian and Prostate Cancer</title><title>Oxidative medicine and cellular longevity</title><addtitle>Oxid Med Cell Longev</addtitle><description>Cancer cells try to avoid the overproduction of reactive oxygen species by metabolic rearrangements. These cells also develop specific strategies to increase ROS resistance and to express the enzymatic activities necessary for ROS detoxification. Oxidative stress produces DNA damage and also induces responses, which could help the cell to restore the initial equilibrium. But if this is not possible, oxidative stress finally activates signals that will lead to cell death. High mobility group B (HMGB) proteins have been previously related to the onset and progressions of cancers of different origins. The protein HMGB1 behaves as a redox sensor and its structural changes, which are conditioned by the oxidative environment, are associated with different functions of the protein. This review describes recent advances in the role of human HMGB proteins and other proteins interacting with them, in cancerous processes related to oxidative stress, with special reference to ovarian and prostate cancer. Their participation in the molecular mechanisms of resistance to cisplatin, a drug commonly used in chemotherapy, is also revised.</description><subject>Amino acids</subject><subject>Angiogenesis</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Autophagy</subject><subject>Biomedical research</subject><subject>Cancer</subject><subject>Chemotherapy</subject><subject>Chromosomal proteins</subject><subject>Deoxyribonucleic acid</subject><subject>Development and progression</subject><subject>DNA</subject><subject>DNA damage</subject><subject>DNA repair</subject><subject>Enzymes</subject><subject>Female</subject><subject>Genes</subject><subject>Genomes</subject><subject>HMGB Proteins - metabolism</subject><subject>Humans</subject><subject>Immune system</subject><subject>Kinases</subject><subject>Localization</subject><subject>Male</subject><subject>Medical research</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Ovarian Neoplasms - metabolism</subject><subject>Ovarian Neoplasms - pathology</subject><subject>Oxidation-Reduction</subject><subject>Oxidative stress</subject><subject>Prostate cancer</subject><subject>Prostatic Neoplasms - metabolism</subject><subject>Prostatic Neoplasms - pathology</subject><subject>Proteins</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>Review</subject><subject>Sensors</subject><issn>1942-0900</issn><issn>1942-0994</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkUtv1DAURiNERUthxxpZYoNEh16_EnuDVEbQViqaCsracpKbiauMPdhJof8eDzNMgRUbP-Tjc339FcULCm8plfKUAS1PpRISSvqoOKJasBloLR7v1wCHxdOUbgFKzgR9UhyyslT5Hj0qugu37MmnULvBjffkPIZpTd6T6xhGdD6dkJseXSTXNo4eY95b35LF2GMkn7ENP8gX9CnERJwnizsbnfW_kCxIox2RzK1vMD4rDjo7JHy-m4-Lrx8_3MwvZleL88v52dWsEVqPs05g06GVlajzqJEz1FwA1FpXjVUcG9Al1J1GzZAr3imuWMmoQtaBbGt-XLzbetdTvcK2QT9GO5h1dCsb702wzvx94l1vluHOiLICVUEWvN4JYvg2YRrNyqUGh8F6DFMytJIguAROM_rqH_Q2TNHn9jIlREmpVuKBWtoBjfNdyHWbjdScCSlYrgk8Uydbqsn_liJ2-ydTMJuYzSZms4s54y__bHMP_841A2-2QO98a7-7_9RhZrCzDzSlAqTiPwGUY7ez</recordid><startdate>20160101</startdate><enddate>20160101</enddate><creator>Barreiro-Alonso, Aida</creator><creator>Lamas-Maceiras, Monica</creator><creator>Rodriguez-Belmonte, Esther</creator><creator>Vizoso-Vazquez, Angel</creator><creator>Quindos, Maria</creator><creator>Cerdan, M. 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subjects | Amino acids Angiogenesis Animals Apoptosis Autophagy Biomedical research Cancer Chemotherapy Chromosomal proteins Deoxyribonucleic acid Development and progression DNA DNA damage DNA repair Enzymes Female Genes Genomes HMGB Proteins - metabolism Humans Immune system Kinases Localization Male Medical research Neoplasm Proteins - metabolism Ovarian Neoplasms - metabolism Ovarian Neoplasms - pathology Oxidation-Reduction Oxidative stress Prostate cancer Prostatic Neoplasms - metabolism Prostatic Neoplasms - pathology Proteins Reactive Oxygen Species - metabolism Review Sensors |
title | High Mobility Group B Proteins, Their Partners, and Other Redox Sensors in Ovarian and Prostate Cancer |
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