Heme Oxygenase-1 Signaling and Redox Homeostasis in Physiopathological Conditions

被引:196
作者
Consoli, Valeria [1 ]
Sorrenti, Valeria [1 ]
Grosso, Salvo [1 ]
Vanella, Luca [1 ]
机构
[1] Univ Catania, Biochem Sect, Dept Drug & Hlth Sci, I-95124 Catania, Italy
关键词
heme oxygenase; Nrf2; GSH; TIGAR; FERROPTOSIS;
D O I
10.3390/biom11040589
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Heme-oxygenase is the enzyme responsible for degradation of endogenous iron protoporphyirin heme; it catalyzes the reaction's rate-limiting step, resulting in the release of carbon monoxide (CO), ferrous ions, and biliverdin (BV), which is successively reduced in bilirubin (BR) by biliverdin reductase. Several studies have drawn attention to the controversial role of HO-1, the enzyme inducible isoform, pointing out its implications in cancer and other diseases development, but also underlining the importance of its antioxidant activity. The contribution of HO-1 in redox homeostasis leads to a relevant decrease in cells oxidative damage, which can be reconducted to its cytoprotective effects explicated alongside other endogenous mechanisms involving genes like TIGAR (TP53-induced glycolysis and apoptosis regulator), but also to the therapeutic functions of heme main transformation products, especially carbon monoxide (CO), which has been shown to be effective on GSH levels implementation sustaining body's antioxidant response to oxidative stress. The aim of this review was to collect most of the knowledge on HO-1 from literature, analyzing different perspectives to try and put forward a hypothesis on revealing yet unknown HO-1-involved pathways that could be useful to promote development of new therapeutical strategies, and lay the foundation for further investigation to fully understand this important antioxidant system.
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页数:23
相关论文
共 213 条
[31]   Ferroptosis in Liver Diseases: An Overview [J].
Capelletti, Martina Maria ;
Manceau, Hana ;
Puy, Herve ;
Peoc'h, Katell .
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2020, 21 (14) :1-23
[32]   Heme oxygenase-1 mediates BAY 11-7085 induced ferroptosis [J].
Chang, Ling-Chu ;
Chiang, Shih-Kai ;
Chen, Shuen-Ei ;
Yu, Yung-Luen ;
Chou, Ruey-Hwang ;
Chang, Wei-Chao .
CANCER LETTERS, 2018, 416 :124-137
[33]   Heme oxygenase-1: emerging target of cancer therapy [J].
Chau, Lee-Young .
JOURNAL OF BIOMEDICAL SCIENCE, 2015, 22
[34]   TIGAR Is Required for Efficient Intestinal Regeneration and Tumorigenesis [J].
Cheung, Eric C. ;
Athineos, Dimitris ;
Lee, Pearl ;
Ridgway, Rachel A. ;
Lambie, Wendy ;
Nixon, Colin ;
Strathdee, Douglas ;
Blyth, Karen ;
Sansom, Owen J. ;
Vousden, Karen H. .
DEVELOPMENTAL CELL, 2013, 25 (05) :463-477
[35]   A Dual Role of Heme Oxygenase-1 in Cancer Cells [J].
Chiang, Shih-Kai ;
Chen, Shuen-Ei ;
Chang, Ling-Chu .
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2019, 20 (01)
[36]   Evidence of Redox Unbalance in Post-Acute Ischemic Stroke Patients [J].
Ciancarelli, Irene ;
Di Massimo, Caterina ;
De Amicis, Daniela ;
Carolei, Antonio ;
Ciancarelli, Maria Giuliana Tozzi .
CURRENT NEUROVASCULAR RESEARCH, 2012, 9 (02) :85-90
[37]  
Converso DP, 2006, FASEB J, V20, P1236, DOI 10.1096/fj.05-4204fje
[38]   The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: chemical mechanism and physiological significance [J].
Cooper, Chris E. ;
Brown, Guy C. .
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 2008, 40 (05) :533-539
[39]   Cysteine Depletion, a Key Action to Challenge Cancer Cells to Ferroptotic Cell Death [J].
Daher, Boutaina ;
Vucetic, Milica ;
Pouyssegur, Jacques .
FRONTIERS IN ONCOLOGY, 2020, 10
[40]   Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis [J].
De Nicola, Gina M. ;
Karreth, Florian A. ;
Humpton, Timothy J. ;
Gopinathan, Aarthi ;
Wei, Cong ;
Frese, Kristopher ;
Mangal, Dipti ;
Yu, Kenneth H. ;
Yeo, Charles J. ;
Calhoun, Eric S. ;
Scrimieri, Francesca ;
Winter, Jordan M. ;
Hruban, Ralph H. ;
Iacobuzio-Donahue, Christine ;
Kern, Scott E. ;
Blair, Ian A. ;
Tuveson, David A. .
NATURE, 2011, 475 (7354) :106-U128