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Article: Heme Oxygenase-1: An Anti-Inflammatory Effector in Cardiovascular, Lung, and Related Metabolic Disorders.

Ryter, Stefan W

2022 Volume 11, Issue 3

Abstract: The heme oxygenase (HO) enzyme system catabolizes heme to carbon monoxide (CO), ferrous iron, and biliverdin-IXα (BV), which is reduced to bilirubin-IXα (BR) by biliverdin reductase (BVR). HO activity is represented by two distinct isozymes, the ... ...

Abstract	The heme oxygenase (HO) enzyme system catabolizes heme to carbon monoxide (CO), ferrous iron, and biliverdin-IXα (BV), which is reduced to bilirubin-IXα (BR) by biliverdin reductase (BVR). HO activity is represented by two distinct isozymes, the inducible form, HO-1, and a constitutive form, HO-2, encoded by distinct genes (
Language	English
Publishing date	2022-03-15
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox11030555
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Targeting AMPK and the Nrf2/HO-1 axis: a promising therapeutic strategy in acute lung injury.

Ryter, Stefan W

The European respiratory journal

2021 Volume 58, Issue 6

MeSH term(s)	AMP-Activated Protein Kinases ; Acute Lung Injury/drug therapy ; Humans ; Lipopolysaccharides ; NF-E2-Related Factor 2
Chemical Substances	Lipopolysaccharides ; NF-E2-Related Factor 2 ; AMP-Activated Protein Kinases (EC 2.7.11.31)
Language	English
Publishing date	2021-12-23
Publishing country	England
Document type	Editorial ; Comment
ZDB-ID	639359-7
ISSN	1399-3003 ; 0903-1936
ISSN (online)	1399-3003
ISSN	0903-1936
DOI	10.1183/13993003.02238-2021
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Significance of Heme and Heme Degradation in the Pathogenesis of Acute Lung and Inflammatory Disorders.

Ryter, Stefan W

International journal of molecular sciences

2021 Volume 22, Issue 11

Abstract: The heme molecule serves as an essential prosthetic group for oxygen transport and storage proteins, as well for cellular metabolic enzyme activities, including those involved in mitochondrial respiration, xenobiotic metabolism, and antioxidant responses. ...

Abstract	The heme molecule serves as an essential prosthetic group for oxygen transport and storage proteins, as well for cellular metabolic enzyme activities, including those involved in mitochondrial respiration, xenobiotic metabolism, and antioxidant responses. Dysfunction in both heme synthesis and degradation pathways can promote human disease. Heme is a pro-oxidant via iron catalysis that can induce cytotoxicity and injury to the vascular endothelium. Additionally, heme can modulate inflammatory and immune system functions. Thus, the synthesis, utilization and turnover of heme are by necessity tightly regulated. The microsomal heme oxygenase (HO) system degrades heme to carbon monoxide (CO), iron, and biliverdin-IXα, that latter which is converted to bilirubin-IXα by biliverdin reductase. Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms. Therapeutic strategies targeting the heme/HO-1 pathway, including therapeutic modulation of heme levels, elevation (or inhibition) of HO-1 protein and activity, and application of CO donor compounds or gas show potential in inflammatory conditions including sepsis and pulmonary diseases.
MeSH term(s)	Animals ; Heme/metabolism ; Heme Oxygenase-1/metabolism ; Humans ; Inflammation/enzymology ; Inflammation/etiology ; Inflammation/metabolism ; Pneumonia/enzymology ; Pneumonia/etiology ; Pneumonia/metabolism ; Sepsis/etiology ; Sepsis/metabolism ; Systemic Inflammatory Response Syndrome/etiology ; Systemic Inflammatory Response Syndrome/metabolism
Chemical Substances	Heme (42VZT0U6YR) ; Heme Oxygenase-1 (EC 1.14.14.18)
Language	English
Publishing date	2021-05-24
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22115509
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Heme Oxgenase-1, a Cardinal Modulator of Regulated Cell Death and Inflammation.

Ryter, Stefan W

Cells

2021 Volume 10, Issue 3

Abstract: Heme oxygenase catalyzes the rate-limiting step in heme degradation in order to generate biliverdin, carbon monoxide (CO), and iron. The inducible form of the enzyme, heme oxygenase-1 (HO-1), exerts a central role in cellular protection. The substrate, ... ...

Abstract	Heme oxygenase catalyzes the rate-limiting step in heme degradation in order to generate biliverdin, carbon monoxide (CO), and iron. The inducible form of the enzyme, heme oxygenase-1 (HO-1), exerts a central role in cellular protection. The substrate, heme, is a potent pro-oxidant that can accelerate inflammatory injury and promote cell death. HO-1 has been implicated as a key mediator of inflammatory cell and tissue injury, as validated in preclinical models of acute lung injury and sepsis. A large body of work has also implicated HO-1 as a cytoprotective molecule against various forms of cell death, including necrosis, apoptosis and newly recognized regulated cell death (RCD) programs such as necroptosis, pyroptosis, and ferroptosis. While the antiapoptotic potential of HO-1 and its reaction product CO in apoptosis regulation has been extensively characterized, relatively fewer studies have explored the regulatory role of HO-1 in other forms of necrotic and inflammatory RCD (i.e., pyroptosis, necroptosis and ferroptosis). HO-1 may provide anti-inflammatory protection in necroptosis or pyroptosis. In contrast, in ferroptosis, HO-1 may play a pro-death role via enhancing iron release. HO-1 has also been implicated in co-regulation of autophagy, a cellular homeostatic program for catabolic recycling of proteins and organelles. While autophagy is primarily associated with cell survival, its occurrence can coincide with RCD programs. This review will summarize the roles of HO-1 and its reaction products in co-regulating RCD and autophagy programs, with its implication for both protective and detrimental tissue responses, with emphasis on how these impact HO-1 as a candidate therapeutic target in disease.
MeSH term(s)	Apoptosis/physiology ; Autophagy/physiology ; Heme Oxygenase-1/metabolism ; Humans ; Inflammation/genetics ; Necroptosis/physiology ; Pyroptosis/physiology ; Regulated Cell Death/genetics
Chemical Substances	Heme Oxygenase-1 (EC 1.14.14.18)
Language	English
Publishing date	2021-02-28
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10030515
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Article: Heme Oxygenase-1: An Anti-Inflammatory Effector in Cardiovascular, Lung, and Related Metabolic Disorders

Ryter, Stefan W.

Antioxidants. 2022 Mar. 15, v. 11, no. 3

2022

Abstract	The heme oxygenase (HO) enzyme system catabolizes heme to carbon monoxide (CO), ferrous iron, and biliverdin-IXα (BV), which is reduced to bilirubin-IXα (BR) by biliverdin reductase (BVR). HO activity is represented by two distinct isozymes, the inducible form, HO-1, and a constitutive form, HO-2, encoded by distinct genes (HMOX1, HMOX2, respectively). HO-1 responds to transcriptional activation in response to a wide variety of chemical and physical stimuli, including its natural substrate heme, oxidants, and phytochemical antioxidants. The expression of HO-1 is regulated by NF-E2-related factor-2 and counter-regulated by Bach-1, in a heme-sensitive manner. Additionally, HMOX1 promoter polymorphisms have been associated with human disease. The induction of HO-1 can confer protection in inflammatory conditions through removal of heme, a pro-oxidant and potential catalyst of lipid peroxidation, whereas iron released from HO activity may trigger ferritin synthesis or ferroptosis. The production of heme-derived reaction products (i.e., BV, BR) may contribute to HO-dependent cytoprotection via antioxidant and immunomodulatory effects. Additionally, BVR and BR have newly recognized roles in lipid regulation. CO may alter mitochondrial function leading to modulation of downstream signaling pathways that culminate in anti-apoptotic, anti-inflammatory, anti-proliferative and immunomodulatory effects. This review will present evidence for beneficial effects of HO-1 and its reaction products in human diseases, including cardiovascular disease (CVD), metabolic conditions, including diabetes and obesity, as well as acute and chronic diseases of the liver, kidney, or lung. Strategies targeting the HO-1 pathway, including genetic or chemical modulation of HO-1 expression, or application of BR, CO gas, or CO donor compounds show therapeutic potential in inflammatory conditions, including organ ischemia/reperfusion injury. Evidence from human studies indicate that HO-1 expression may represent a biomarker of oxidative stress in various clinical conditions, while increases in serum BR levels have been correlated inversely to risk of CVD and metabolic disease. Ongoing human clinical trials investigate the potential of CO as a therapeutic in human disease.
Keywords	antioxidants ; biomarkers ; blood serum ; carbon monoxide ; catalysts ; diabetes ; ferritin ; ferroptosis ; heme ; heme oxygenase (biliverdin-producing) ; human diseases ; humans ; iron ; ischemia ; isozymes ; kidneys ; lipid peroxidation ; lipids ; liver ; lungs ; mitochondria ; obesity ; oxidative stress ; phytochemicals ; reperfusion injury ; therapeutics ; transcriptional activation
Language	English
Dates of publication	2022-0315
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox11030555
Database	NAL-Catalogue (AGRICOLA)

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Article: Therapeutic Potential of Heme Oxygenase-1 and Carbon Monoxide in Acute Organ Injury, Critical Illness, and Inflammatory Disorders.

Ryter, Stefan W

Antioxidants (Basel, Switzerland)

2020 Volume 9, Issue 11

Abstract: Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase. HO-1 has been ... ...

Abstract	Heme oxygenase-1 (HO-1) is an inducible stress protein that catalyzes the oxidative conversion of heme to carbon monoxide (CO), iron, and biliverdin (BV), the latter of which is converted to bilirubin (BR) by biliverdin reductase. HO-1 has been implicated as a cytoprotectant in various models of acute organ injury and disease (i.e., lung, kidney, heart, liver). Thus, HO-1 may serve as a general therapeutic target in inflammatory diseases. HO-1 may function as a pleiotropic modulator of inflammatory signaling, via the removal of heme, and generation of its enzymatic degradation-products. Iron release from HO activity may exert pro-inflammatory effects unless sequestered, whereas BV/BR have well-established antioxidant properties. CO, derived from HO activity, has been identified as an endogenous mediator that can influence mitochondrial function and/or cellular signal transduction programs which culminate in the regulation of apoptosis, cellular proliferation, and inflammation. Much research has focused on the application of low concentration CO, whether administered in gaseous form by inhalation, or via the use of CO-releasing molecules (CORMs), for therapeutic benefit in disease. The development of novel CORMs for their translational potential remains an active area of investigation. Evidence has accumulated for therapeutic effects of both CO and CORMs in diseases associated with critical care, including acute lung injury/acute respiratory distress syndrome (ALI/ARDS), mechanical ventilation-induced lung injury, pneumonias, and sepsis. The therapeutic benefits of CO may extend to other diseases involving aberrant inflammatory processes such as transplant-associated ischemia/reperfusion injury and chronic graft rejection, and metabolic diseases. Current and planned clinical trials explore the therapeutic benefit of CO in ARDS and other lung diseases.
Language	English
Publishing date	2020-11-19
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox9111153
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Article ; Online: Heme oxygenase-1/carbon monoxide as modulators of autophagy and inflammation.

Ryter, Stefan W

Archives of biochemistry and biophysics

2019 Volume 678, Page(s) 108186

Abstract: Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXα, carbon monoxide (CO), and iron. The HO-1/CO system confers cytoprotection in animal models of organ injury and disease, via modulation of inflammation and apoptosis. Recent ... ...

Abstract	Heme oxygenase-1 (HO-1) catalyzes heme degradation to generate biliverdin-IXα, carbon monoxide (CO), and iron. The HO-1/CO system confers cytoprotection in animal models of organ injury and disease, via modulation of inflammation and apoptosis. Recent studies have uncovered novel anti-inflammatory targets of HO-1/CO including regulation of the autophagy and inflammasome pathways. Autophagy is a lysosome-dependent program for the turnover of cellular organelles such as mitochondria, proteins, and pathogens; which may downregulate inflammatory processes. Therapeutic modulation of autophagy by CO has been demonstrated in models of sepsis. The nucleotide-binding domain, leucine-rich-containing family, pyrin domain-containing-3 (NLRP3) inflammasome regulates the maturation of pro-inflammatory cytokines. CO can regulate NLRP3 inflammasome activation and associated pro-inflammatory cytokines production and promote the resolution of inflammation by upregulating the synthesis of specialized pro-resolving mediators (SPMs). Mitochondria may represent a proximal target of HO-1/CO action. HO-1 may localize to mitochondria in response to stress, while CO can moderate mitochondrial dysfunction and regulate mitochondrial autophagy (mitophagy) and biogenesis. The interplay between mitochondrial autophagy, mitochondrial dysfunction, and the regulation and resolution of inflammation may make important contributions to the protection afforded by HO-1/CO in cellular and organ injury models. Recent studies have continued to explore the potential of CO for clinical applications.
MeSH term(s)	Animals ; Autophagy ; Carbon Monoxide/metabolism ; Carbon Monoxide/therapeutic use ; Heme Oxygenase-1/metabolism ; Humans ; Inflammation/drug therapy ; Inflammation/metabolism ; Inflammation/pathology ; Mitochondria/pathology
Chemical Substances	Carbon Monoxide (7U1EE4V452) ; Heme Oxygenase-1 (EC 1.14.14.18)
Language	English
Publishing date	2019-11-05
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2019.108186
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Article ; Online: Withdrawal: Carbon monoxide protects against hyperoxia-induced endothelial cell apoptosis by inhibiting reactive oxygen species formation.

Wang, Xue / Wang, Yong / Kim, Hong Pyo / Nakahira, Kiichi / Ryter, Stefan W / Choi, Augustine M K

The Journal of biological chemistry

2024 Volume 300, Issue 3, Page(s) 105758

Language	English
Publishing date	2024-02-19
Publishing country	United States
Document type	Published Erratum
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2024.105758
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Article ; Online: Heme Oxgenase-1, a Cardinal Modulator of Regulated Cell Death and Inflammation

Stefan W. Ryter

Cells, Vol 10, Iss 515, p

2021 Volume 515

Abstract	Heme oxygenase catalyzes the rate-limiting step in heme degradation in order to generate biliverdin, carbon monoxide (CO), and iron. The inducible form of the enzyme, heme oxygenase-1 (HO-1), exerts a central role in cellular protection. The substrate, heme, is a potent pro-oxidant that can accelerate inflammatory injury and promote cell death. HO-1 has been implicated as a key mediator of inflammatory cell and tissue injury, as validated in preclinical models of acute lung injury and sepsis. A large body of work has also implicated HO-1 as a cytoprotective molecule against various forms of cell death, including necrosis, apoptosis and newly recognized regulated cell death (RCD) programs such as necroptosis, pyroptosis, and ferroptosis. While the antiapoptotic potential of HO-1 and its reaction product CO in apoptosis regulation has been extensively characterized, relatively fewer studies have explored the regulatory role of HO-1 in other forms of necrotic and inflammatory RCD (i.e., pyroptosis, necroptosis and ferroptosis). HO-1 may provide anti-inflammatory protection in necroptosis or pyroptosis. In contrast, in ferroptosis, HO-1 may play a pro-death role via enhancing iron release. HO-1 has also been implicated in co-regulation of autophagy, a cellular homeostatic program for catabolic recycling of proteins and organelles. While autophagy is primarily associated with cell survival, its occurrence can coincide with RCD programs. This review will summarize the roles of HO-1 and its reaction products in co-regulating RCD and autophagy programs, with its implication for both protective and detrimental tissue responses, with emphasis on how these impact HO-1 as a candidate therapeutic target in disease.
Keywords	apoptosis ; autophagy ; carbon monoxide ; cell death ; ferroptosis ; heme oxygenase ; Biology (General) ; QH301-705.5
Subject code	610
Language	English
Publishing date	2021-02-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Significance of Heme and Heme Degradation in the Pathogenesis of Acute Lung and Inflammatory Disorders

Stefan W. Ryter

International Journal of Molecular Sciences, Vol 22, Iss 5509, p

2021 Volume 5509

Abstract	The heme molecule serves as an essential prosthetic group for oxygen transport and storage proteins, as well for cellular metabolic enzyme activities, including those involved in mitochondrial respiration, xenobiotic metabolism, and antioxidant responses. Dysfunction in both heme synthesis and degradation pathways can promote human disease. Heme is a pro-oxidant via iron catalysis that can induce cytotoxicity and injury to the vascular endothelium. Additionally, heme can modulate inflammatory and immune system functions. Thus, the synthesis, utilization and turnover of heme are by necessity tightly regulated. The microsomal heme oxygenase (HO) system degrades heme to carbon monoxide (CO), iron, and biliverdin-IXα, that latter which is converted to bilirubin-IXα by biliverdin reductase. Heme degradation by heme oxygenase-1 (HO-1) is linked to cytoprotection via heme removal, as well as by activity-dependent end-product generation (i.e., bile pigments and CO), and other potential mechanisms. Therapeutic strategies targeting the heme/HO-1 pathway, including therapeutic modulation of heme levels, elevation (or inhibition) of HO-1 protein and activity, and application of CO donor compounds or gas show potential in inflammatory conditions including sepsis and pulmonary diseases.
Keywords	acute lung injury ; carbon monoxide ; heme ; heme oxygenase ; inflammation ; lung disease ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	570
Language	English
Publishing date	2021-05-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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