The DOI matches its Crossref record; 240 of the 240 references it cites were found in a registry or an index.
Mechanisms of Cell Protection by Heme Oxygenase-1
Abstract
Heme oxygenases (HO) catabolize free heme, that is, iron (Fe) protoporphyrin (IX), into equimolar amounts of Fe 2+ , carbon monoxide (CO), and biliverdin. The stress-responsive HO-1 isoenzyme affords protection against programmed cell death. The mechanism underlying this cytoprotective effect relies on the ability of HO-1 to catabolize free heme and prevent it from sensitizing cells to undergo programmed cell death. This cytoprotective effect inhibits the pathogenesis of a variety of immune-mediated inflammatory diseases.
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In the citing paper
“Thus, HO-1 exerts cytoprotective effects by reducing the pro-oxidative activity of heme and by re-programming metabolic traits, thereby limiting tissue damage in the course of inflammatory processes, including sepsis (Gozzelino et al., 2010; Weis et al., 2017).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Gozzelino et al., 2010
In the citing paper
“Presumably, this occurs via a mechanism driven via the Fenton reaction in which hydrogen peroxide (H 2 O 2 ) oxidizes Fe 2+ , either within the context of the tetrapyrrole ring or when Fe is released from heme, to produce highly reactive hydroxyl radicals (OH .) [38,212].”
From The Iron age of host–microbe interactions (2015) · cites this paper as [38]
In the citing paper
“Briefly, labile heme sensitizes parenchyma cells to undergo programmed cell death in response to proinflammatory cytokines such as TNF [106] as well as other agonists such as Fas as well as ROS and RNS [38,190].”
From The Iron age of host–microbe interactions (2015) · cites this paper as [38]
In the citing paper
“Once released from hemoglobin, the redox activity of labile heme becomes pro-oxidant and cytotoxic [38,106,107,190] (Fig 4).”
From The Iron age of host–microbe interactions (2015) · cites this paper as [38]
In the citing paper
“The pathogenic effects exerted by extracellular hemoglobin and labile heme are countered by adaptive responses that converge at the level of heme catabolism by HO-1 [38,219], providing tissue damage control and disease tolerance to systemic infections [103,105,106] (Fig 4).”
From The Iron age of host–microbe interactions (2015) · cites this paper as [38]
In the citing paper
“When coupled to other mechanisms regulating Fe homeostasis, HO-1 avoids tissue Fe overload and tissue damage while sustaining Fe supply to erythropoiesis to maintain Fe homeostasis during infection [38,54,219,220] (Fig 4).”
From The Iron age of host–microbe interactions (2015) · cites this paper as [38]
In the citing paper
“The most abundant pool of Fe in mammals are the prosthetic heme groups of hemoglobin in red blood cells (RBC), followed by the heme groups of myoglobin in muscle cells and those of cytochromes and other ubiquitously expressed hemoproteins in all cells[38,54].”
From The Iron age of host–microbe interactions (2015) · cites this paper as [38]
In the citing paper
“Moreover, recent studies demonstrate the mechanisms leading to the unfavorable effects of free hemoglobin including oxidation and production of ferryl hemoglobin and heme generation [36-38].”
From Free hemoglobin concentration in severe sepsis: methods of measurement and prediction of outcome (2012) · cites this paper as [38]
In the citing paper
“In addition, the reduced abundance of CO and bilirubin, two end-products of the HO-1 pathway, further contributes to increased or prolonged oxidative stress, as these molecules have radical scavenging capacities and anti-inflammatory activities (Gozzelino et al., 2010).”
From Heme oxygenase 1 controls early innate immune response of macrophages to Salmonella Typhimurium infection: Heme oxygenase 1 expression affects Salmonella infection (2016) · cites this paper as Gozzelino et al., 2010
In the citing paper
“Up-regulation of HO-1 during malaria or sepsis was demonstrated in association with infection tolerance and limitation of tissue damage resulting in an improved survival (Gozzelino et al., 2010; Larsen et al., 2010).”
From Heme oxygenase 1 controls early innate immune response of macrophages to Salmonella Typhimurium infection: Heme oxygenase 1 expression affects Salmonella infection (2016) · cites this paper as Gozzelino et al., 2010
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Metadata
- Authors
- Gozzelino, R., Jeney, V., & Soares, M. P.
- Affiliations
- Instituto Gulbenkian de Ciência (PT)
- Instituto Gulbenkian de Ciência, Oeiras, Portugal;
- Venue
- Annual Review of Pharmacology and Toxicology
- Publisher
- Annual Reviews
- Published
- 2010-02-01
- Volume
- 50
- Issue
- 1
- Pages
- 323-354
- ISSN
- 0362-1642 (ISSN-L)
- 1545-4304
- OpenAlex
- W2162853795
- Cited by
- 1,241
- References
- 237
- Citations by year
- 2026: 66 · 2025: 61 · 2024: 55 · 2023: 72 · 2022: 92 · 2021: 114 · 2020: 101 · 2019: 60 · 2018: 87 · 2017: 75 · 2016: 65 · 2015: 99 · 2014: 77 · 2013: 69 · 2012: 74
- FWCI
- 6.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Annual Review of Pharmacology and Toxicology (publishedVersion)
- PubMed (publishedVersion)
- University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
- Keywords
- heme oxygenase-1, heme degradation, carbon monoxide, biliverdin, bilirubin, programmed cell death, cytoprotection, immune-mediated inflammatory diseases, stress response
- MeSH terms
- Animals, Biliverdine, Carbon Monoxide, Heme, Humans, Inflammation, Tumor Necrosis Factor-alpha, Gene Expression Regulation, Enzymologic, Apoptosis, Cytoprotection, Heme Oxygenase-1
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