A Dual Role of Heme Oxygenase-1 in Cancer Cells
Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions. HO-1 is commonly regarded as a survival molecule, exerting an important role in c...
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| Published in | International journal of molecular sciences Vol. 20; no. 1; p. 39 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
MDPI AG
21.12.2018
MDPI |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions. HO-1 is commonly regarded as a survival molecule, exerting an important role in cancer progression and its inhibition is considered beneficial in a number of cancers. However, increasing studies have shown a dark side of HO-1, in which HO-1 acts as a critical mediator in ferroptosis induction and plays a causative factor for the progression of several diseases. Ferroptosis is a newly identified iron- and lipid peroxidation-dependent cell death. The critical role of HO-1 in heme metabolism makes it an important candidate to mediate protective or detrimental effects via ferroptosis induction. This review summarizes the current understanding on the regulatory mechanisms of HO-1 in ferroptosis. The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator. Despite the dark side that is related to cell death, there is a prospective application of HO-1 to mediate ferroptosis for cancer therapy as a chemotherapeutic strategy against tumors. |
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| AbstractList | Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions. HO-1 is commonly regarded as a survival molecule, exerting an important role in cancer progression and its inhibition is considered beneficial in a number of cancers. However, increasing studies have shown a dark side of HO-1, in which HO-1 acts as a critical mediator in ferroptosis induction and plays a causative factor for the progression of several diseases. Ferroptosis is a newly identified iron- and lipid peroxidation-dependent cell death. The critical role of HO-1 in heme metabolism makes it an important candidate to mediate protective or detrimental effects via ferroptosis induction. This review summarizes the current understanding on the regulatory mechanisms of HO-1 in ferroptosis. The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator. Despite the dark side that is related to cell death, there is a prospective application of HO-1 to mediate ferroptosis for cancer therapy as a chemotherapeutic strategy against tumors. Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions. HO-1 is commonly regarded as a survival molecule, exerting an important role in cancer progression and its inhibition is considered beneficial in a number of cancers. However, increasing studies have shown a dark side of HO-1, in which HO-1 acts as a critical mediator in ferroptosis induction and plays a causative factor for the progression of several diseases. Ferroptosis is a newly identified iron- and lipid peroxidation-dependent cell death. The critical role of HO-1 in heme metabolism makes it an important candidate to mediate protective or detrimental effects via ferroptosis induction. This review summarizes the current understanding on the regulatory mechanisms of HO-1 in ferroptosis. The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator. Despite the dark side that is related to cell death, there is a prospective application of HO-1 to mediate ferroptosis for cancer therapy as a chemotherapeutic strategy against tumors.Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions. HO-1 is commonly regarded as a survival molecule, exerting an important role in cancer progression and its inhibition is considered beneficial in a number of cancers. However, increasing studies have shown a dark side of HO-1, in which HO-1 acts as a critical mediator in ferroptosis induction and plays a causative factor for the progression of several diseases. Ferroptosis is a newly identified iron- and lipid peroxidation-dependent cell death. The critical role of HO-1 in heme metabolism makes it an important candidate to mediate protective or detrimental effects via ferroptosis induction. This review summarizes the current understanding on the regulatory mechanisms of HO-1 in ferroptosis. The amount of cellular iron and reactive oxygen species (ROS) is the determinative momentum for the role of HO-1, in which excessive cellular iron and ROS tend to enforce HO-1 from a protective role to a perpetrator. Despite the dark side that is related to cell death, there is a prospective application of HO-1 to mediate ferroptosis for cancer therapy as a chemotherapeutic strategy against tumors. Excessive ROS can induce oxidative damage of DNA, and, to a higher degree, gene mutation and carcinogenesis [2,3,4]. [...]lipid peroxidation by excessive ROS may damage cellular structures and eventually induce cell death [1]. [...]the augmentation of ROS is a useful approach for clinical cancer treatment. Various chemotherapeutic agents, such as cisplatin, doxorubicin, and 5-fluorouracil, have been shown to exert their antitumor activity via ROS-dependent activation of apoptosis [4,5]. [...]oxidation therapy becomes a possible strategy by provoking ROS production and diminishing antioxidant enzymes in cancer cells. Certain cancer cells, such as pancreatic cancer cell lines (MIA PaCa-2, PANC-1, and BxPC-3) and a subset of triple-negative cancer cells also greatly depend on system Xc− to mediate cysteine uptake for growth, as well as survival under oxidative stress conditions [24,25], suggesting that system Xc− might serve as a good chemotherapeutic target. |
| Author | Chiang, Shih-Kai Chang, Ling-Chu Chen, Shuen-Ei |
| AuthorAffiliation | 1 Department of Animal Science, National Chung Hsing University, Taichung 40227, Taiwan; shihkaichiang@gmail.com (S.K.C.); chenshuenei@hotmail.com (S.E.C.) 2 Innovation and Development Center of Sustainable Agriculture (IDCSA), National Chung Hsing University, Taichung 40277, Taiwan 3 The iEGG and Animal Biotechnology Center, National Chung Hsing University, Taichung 40277, Taiwan 5 Chinese Medicinal Research and Development Center, China Medical University Hospital, Taichung 40447, Taiwan 4 Research Center for Sustainable Energy and Nanotechnology, National Chung Hsing University, Taichung 40277, Taiwan |
| AuthorAffiliation_xml | – name: 4 Research Center for Sustainable Energy and Nanotechnology, National Chung Hsing University, Taichung 40277, Taiwan – name: 2 Innovation and Development Center of Sustainable Agriculture (IDCSA), National Chung Hsing University, Taichung 40277, Taiwan – name: 3 The iEGG and Animal Biotechnology Center, National Chung Hsing University, Taichung 40277, Taiwan – name: 5 Chinese Medicinal Research and Development Center, China Medical University Hospital, Taichung 40447, Taiwan – name: 1 Department of Animal Science, National Chung Hsing University, Taichung 40227, Taiwan; shihkaichiang@gmail.com (S.K.C.); chenshuenei@hotmail.com (S.E.C.) |
| Author_xml | – sequence: 1 givenname: Shih-Kai surname: Chiang fullname: Chiang, Shih-Kai – sequence: 2 givenname: Shuen-Ei orcidid: 0000-0003-1737-2591 surname: Chen fullname: Chen, Shuen-Ei – sequence: 3 givenname: Ling-Chu orcidid: 0000-0002-7905-580X surname: Chang fullname: Chang, Ling-Chu |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30583467$$D View this record in MEDLINE/PubMed |
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| Snippet | Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate... Excessive ROS can induce oxidative damage of DNA, and, to a higher degree, gene mutation and carcinogenesis [2,3,4]. [...]lipid peroxidation by excessive ROS... |
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| SubjectTerms | Animals Apoptosis Cancer therapies Cell Death Cell growth Cell Line, Tumor Disease Models, Animal Drug Therapy Ferroptosis Glutathione Heme - metabolism Heme Oxygenase-1 - metabolism Humans Iron - metabolism Lipid Peroxidation Neoplasms - metabolism Oxidation Reactive Oxygen Species - metabolism Review Xenograft Model Antitumor Assays |
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| Title | A Dual Role of Heme Oxygenase-1 in Cancer Cells |
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