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Article ; Online: Fingerprint of the oxido-reductase ERO1: A protein disulfide bond producer and supporter of cancer.

Zito, Ester / Guarrera, Luca / Janssen-Heininger, Yvonne M W

Biochimica et biophysica acta. Reviews on cancer

2023 Volume 1879, Issue 1, Page(s) 189027

Abstract: Endoplasmic reticulum oxidoreductin 1 (ERO1) alpha (ERO1A) is an endoplasmic reticulum (ER)-localized protein disulfide oxidoreductase, involved in the disulfide bond formation of proteins. ERO1's activity in oxidative protein folding is redundant in ... ...

Abstract	Endoplasmic reticulum oxidoreductin 1 (ERO1) alpha (ERO1A) is an endoplasmic reticulum (ER)-localized protein disulfide oxidoreductase, involved in the disulfide bond formation of proteins. ERO1's activity in oxidative protein folding is redundant in higher eukaryotes and its loss is well compensated. Although it is dispensable in non-cancer cells, high ERO1 levels are seen with different cancers and predict their malignant phenotype. ERO1 fosters tumor aggressiveness and the response to drug therapy in hypoxic and highly metastatic tumors. It regulates vascular endothelial growth factor (VEGF) levels, oxidative folding and N-glycosylation in hypoxic conditions, boosting tumor fitness and angiogenesis on multiple levels. In addition, ERO1 regulates protein death ligand-1 (PD-L1) on tumors, interfering with the related immune surveillance mechanism, hence acting on the tumors' response to immune check-point inhibitors (ICI). This all points to inhibition of ERO1 as an effective pharmacological tool, selectively targeting tumors while sparing non-cancer cells from cytotoxicity. The critical discussion here closely examines the molecular basis for ERO1's involvement in tumors and ERO1 inhibition strategies for their treatment.
MeSH term(s)	Humans ; Vascular Endothelial Growth Factor A/genetics ; Vascular Endothelial Growth Factor A/metabolism ; Oxidoreductases/genetics ; Oxidoreductases/metabolism ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Endoplasmic Reticulum ; Disulfides/metabolism
Chemical Substances	Vascular Endothelial Growth Factor A ; Oxidoreductases (EC 1.-) ; Disulfides
Language	English
Publishing date	2023-11-24
Publishing country	Netherlands
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2918802-7
ISSN	1879-2561 ; 0304-419X
ISSN (online)	1879-2561
ISSN	0304-419X
DOI	10.1016/j.bbcan.2023.189027
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Article ; Online: Identification of tyrosine brominated extracellular matrix proteins in normal and fibrotic lung tissues.

Cruz, Litiele Cezar / Habibovic, Aida / Dempsey, Bianca / Massafera, Mariana P / Janssen-Heininger, Yvonne M W / Lin, Miao-Chong Joy / Hoffman, Evan T / Weiss, Daniel J / Huang, Steven K / van der Vliet, Albert / Meotti, Flavia C

Redox biology

2024 Volume 71, Page(s) 103102

Abstract: Peroxidasin (PXDN) is a secreted heme peroxidase that catalyzes the oxidative crosslinking of collagen IV within the extracellular matrix (ECM) via intermediate hypobromous acid (HOBr) synthesis from hydrogen peroxide and bromide, but recent findings ... ...

Abstract	Peroxidasin (PXDN) is a secreted heme peroxidase that catalyzes the oxidative crosslinking of collagen IV within the extracellular matrix (ECM) via intermediate hypobromous acid (HOBr) synthesis from hydrogen peroxide and bromide, but recent findings have also suggested alternative ECM protein modifications by PXDN, including incorporation of bromide into tyrosine residues. In this work, we sought to identify the major target proteins for tyrosine bromination by HOBr or by PXDN-mediated oxidation in ECM from mouse teratocarcinoma PFHR9 cells. We detected 61 bromotyrosine (BrY)-containing peptides representing 23 proteins in HOBr-modified ECM from PFHR9 cells, among which laminins displayed the most prominent bromotyrosine incorporation. Moreover, we also found that laminin α1, laminin β1, and tubulointerstitial nephritis antigen-like (TINAGL1) contained BrY in untreated PFHR9 cells, which depended on PXDN. We extended these analyses to lung tissues from both healthy mice and mice with experimental lung fibrosis, and in lung tissues obtained from human subjects. Analysis of ECM-enriched mouse lung tissue extracts showed that 83 ECM proteins were elevated in bleomycin-induced fibrosis, which included various collagens and laminins, and PXDN. Similarly, mRNA and protein expression of PXDN and laminin α/β1 were enhanced in fibrotic mouse lung tissues, and also in mouse bone-marrow-derived macrophages or human fibroblasts stimulated with transforming growth factor β1, a profibrotic growth factor. We identified 11 BrY-containing ECM proteins, including collagen IV α2, collagen VI α1, TINAGL1, and various laminins, in both healthy and mouse fibrotic lung tissues, although the relative extent of tyrosine bromination of laminins was not significantly increased during fibrosis. Finally, we also identified 7 BrY-containing ECM proteins in human lung tissues, again including collagen IV α2, collagen VI α1, and TINAGL1. Altogether, this work demonstrates the presence of several bromotyrosine-modified ECM proteins, likely involving PXDN, even in normal lung tissues, suggesting a potential biological function for these modifications.
MeSH term(s)	Humans ; Animals ; Mice ; Extracellular Matrix Proteins/genetics ; Extracellular Matrix Proteins/metabolism ; Bromides/adverse effects ; Bromides/metabolism ; Laminin/genetics ; Laminin/metabolism ; Extracellular Matrix/metabolism ; Lung/metabolism ; Peroxidasin ; Collagen Type IV/metabolism ; Pulmonary Fibrosis/chemically induced ; Pulmonary Fibrosis/genetics ; Pulmonary Fibrosis/metabolism ; Tyrosine/metabolism ; Bromates
Chemical Substances	Extracellular Matrix Proteins ; hypobromous acid (GHT9BV419J) ; Bromides ; Laminin ; Peroxidasin ; Collagen Type IV ; Tyrosine (42HK56048U) ; Bromates
Language	English
Publishing date	2024-02-23
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2024.103102
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Article ; Online: Glutaredoxin attenuates glutathione levels via deglutathionylation of Otub1 and subsequent destabilization of system x

Aboushousha, Reem / van der Velden, Jos / Hamilton, Nicholas / Peng, Zhihua / MacPherson, Maximilian / Erickson, Cuixia / White, Sheryl / Wouters, Emiel F M / Reynaert, Niki L / Seward, David J / Li, Jianing / Janssen-Heininger, Yvonne M W

Science advances

2023 Volume 9, Issue 37, Page(s) eadi5192

Abstract: Glutathione (GSH) is a critical component of the cellular redox system that combats oxidative stress. The glutamate-cystine antiporter, system ... ...

Abstract	Glutathione (GSH) is a critical component of the cellular redox system that combats oxidative stress. The glutamate-cystine antiporter, system x
MeSH term(s)	Glutaredoxins ; Cystine ; Biological Transport ; Glutamic Acid ; Glutathione
Chemical Substances	Glutaredoxins ; Cystine (48TCX9A1VT) ; Glutamic Acid (3KX376GY7L) ; Glutathione (GAN16C9B8O)
Language	English
Publishing date	2023-09-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.adi5192
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Article ; Online: Local fractal dimension of collagen detects increased spatial complexity in fibrosis.

Casey, Dylan T / Lahue, Karolyn G / Mori, Vitor / Herrmann, Jacob / Hall, Joseph K / Suki, Béla / Janssen-Heininger, Yvonne M W / Bates, Jason H T

Histochemistry and cell biology

2023 Volume 161, Issue 1, Page(s) 29–42

Abstract: Increase of collagen content and reorganization characterizes fibrosis but quantifying the latter remains challenging. Spatially complex structures are often analyzed via the fractal dimension; however, established methods for calculating this quantity ... ...

Abstract	Increase of collagen content and reorganization characterizes fibrosis but quantifying the latter remains challenging. Spatially complex structures are often analyzed via the fractal dimension; however, established methods for calculating this quantity either provide a single dimension for an entire object or a spatially distributed dimension that only considers binary images. These neglect valuable information related to collagen density in images of fibrotic tissue. We sought to develop a fractal analysis that can be applied to 3-dimensional (3D) images of fibrotic tissue. A fractal dimension map for each image was calculated by determining a single fractal dimension for a small area surrounding each image pixel, using fiber thickness as the third dimension. We found that this local fractal dimension increased with age and with progression of fibrosis regardless of collagen content. Our new method of distributed 3D fractal analysis can thus distinguish between changes in collagen content and organization induced by fibrosis.
MeSH term(s)	Humans ; Fractals ; Fibrosis ; Collagen
Chemical Substances	Collagen (9007-34-5)
Language	English
Publishing date	2023-11-08
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1222930-1
ISSN	1432-119X ; 0301-5564 ; 0948-6143
ISSN (online)	1432-119X
ISSN	0301-5564 ; 0948-6143
DOI	10.1007/s00418-023-02248-8
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Article ; Online: Diet-induced obesity worsens allergen-induced type 2/type 17 inflammation in airways by enhancing DUOX1 activation.

Habibovic, Aida / Hristova, Milena / Morris, Carolyn R / Lin, Miao-Chong Joy / Cruz, Litiele C / Ather, Jennifer L / Geiszt, Miklós / Anathy, Vikas / Janssen-Heininger, Yvonne M W / Poynter, Matthew E / Dixon, Anne E / van der Vliet, Albert

American journal of physiology. Lung cellular and molecular physiology

2023 Volume 324, Issue 2, Page(s) L228–L242

Abstract: More than 50% of people with asthma in the United States are obese, and obesity often worsens symptoms of allergic asthma and impairs response to treatment. Based on previously established roles of the epithelial NADPH oxidase DUOX1 in allergic airway ... ...

Abstract	More than 50% of people with asthma in the United States are obese, and obesity often worsens symptoms of allergic asthma and impairs response to treatment. Based on previously established roles of the epithelial NADPH oxidase DUOX1 in allergic airway inflammation, we addressed the potential involvement of DUOX1 in altered allergic inflammation in the context of obesity. Intranasal house dust mite (HDM) allergen challenge of subjects with allergic asthma induced rapid secretion of IL-33, then IL-13, into the nasal lumen, responses that were significantly enhanced in obese asthmatic subjects (BMI >30). Induction of diet-induced obesity (DIO) in mice by high-fat diet (HFD) feeding similarly enhanced acute airway responses to intranasal HDM challenge, particularly with respect to secretion of IL-33 and type 2/type 3 cytokines, and this was associated with enhanced epithelial DUOX1 expression and was avoided in DUOX1-deficient mice. DIO also enhanced DUOX1-dependent features of chronic HDM-induced allergic inflammation. Although DUOX1 did not affect overall weight gain by HFD feeding, it contributed to glucose intolerance, suggesting a role in glucose metabolism. However, glucose intolerance induced by short-term HFD feeding, in the absence of adiposity, was not sufficient to alter HDM-induced acute airway responses. DIO was associated with enhanced presence of the adipokine leptin in the airways, and leptin enhanced DUOX1-dependent IL-13 and mucin production in airway epithelial cells. In conclusion, augmented inflammatory airway responses to HDM in obesity are associated with increases in airway epithelial DUOX1, and by increased airway epithelial leptin signaling.
MeSH term(s)	Animals ; Mice ; Allergens ; Asthma/metabolism ; Diet ; Disease Models, Animal ; Dual Oxidases ; Glucose Intolerance ; Inflammation ; Interleukin-13 ; Interleukin-33 ; Leptin ; Obesity ; Pyroglyphidae
Chemical Substances	Allergens ; Dual Oxidases (EC 1.11.1.-) ; Duox1 protein, mouse (EC 1.6.3.1) ; Interleukin-13 ; Interleukin-33 ; Leptin ; DUOX1 protein, human (EC 1.6.3.1)
Language	English
Publishing date	2023-01-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00331.2022
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Uc I Zs.89: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.A 2749: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Oxidation of peroxiredoxin-4 induces oligomerization and promotes interaction with proteins governing protein folding and endoplasmic reticulum stress.

Elko, Evan A / Manuel, Allison M / White, Sheryl / Zito, Ester / van der Vliet, Albert / Anathy, Vikas / Janssen-Heininger, Yvonne M W

The Journal of biological chemistry

2021 Volume 296, Page(s) 100665

Abstract: Peroxiredoxins (PRDXs) catalyze the reduction of hydrogen peroxide ( ... ...

Abstract	Peroxiredoxins (PRDXs) catalyze the reduction of hydrogen peroxide (H
MeSH term(s)	Animals ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum Stress ; Epithelial Cells/metabolism ; Lung/metabolism ; Mice ; Peroxiredoxins/chemistry ; Peroxiredoxins/metabolism ; Protein Folding ; Protein Interaction Domains and Motifs ; Protein Multimerization
Chemical Substances	Peroxiredoxins (EC 1.11.1.15) ; Prdx4 protein, mouse (EC 1.11.1.15)
Language	English
Publishing date	2021-04-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.100665
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Article ; Online: Oxidative stress in chronic lung disease: From mitochondrial dysfunction to dysregulated redox signaling.

van der Vliet, Albert / Janssen-Heininger, Yvonne M W / Anathy, Vikas

Molecular aspects of medicine

2018 Volume 63, Page(s) 59–69

Abstract: The lung is a delicate organ with a large surface area that is continuously exposed to the external environment, and is therefore highly vulnerable to exogenous sources of oxidative stress. In addition, each of its approximately 40 cell types can also ... ...

Abstract	The lung is a delicate organ with a large surface area that is continuously exposed to the external environment, and is therefore highly vulnerable to exogenous sources of oxidative stress. In addition, each of its approximately 40 cell types can also generate reactive oxygen species (ROS), as byproducts of cellular metabolism and in a more regulated manner by NOX enzymes with functions in host defense, immune regulation, and cell proliferation or differentiation. To effectively regulate the biological actions of exogenous and endogenous ROS, various enzymatic and non-enzymatic antioxidant defense systems are present in all lung cell types to provide adequate protection against their injurious effects and to allow for appropriate ROS-mediated biological signaling. Acute and chronic lung diseases are commonly thought to be associated with increased oxidative stress, evidenced by altered cellular or extracellular redox status, increased irreversible oxidative modifications in proteins or DNA, mitochondrial dysfunction, and altered expression or activity of NOX enzymes and antioxidant enzyme systems. However, supplementation strategies with generic antioxidants have been minimally successful in prevention or treatment of lung disease, most likely due to their inability to distinguish between harmful and beneficial actions of ROS. Recent studies have attempted to identify specific redox-based mechanisms that may mediate chronic lung disease, such as allergic asthma or pulmonary fibrosis, which provide opportunities for selective redox-based therapeutic strategies that may be useful in treatment of these diseases.
MeSH term(s)	Animals ; Biomarkers ; Chronic Disease ; Humans ; Lung Diseases/metabolism ; Mitochondria/metabolism ; Oxidation-Reduction ; Oxidative Stress ; Reactive Oxygen Species/metabolism ; Signal Transduction
Chemical Substances	Biomarkers ; Reactive Oxygen Species
Language	English
Publishing date	2018-08-22
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	197640-0
ISSN	1872-9452 ; 0098-2997
ISSN (online)	1872-9452
ISSN	0098-2997
DOI	10.1016/j.mam.2018.08.001
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Article ; Online: Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal their differential oxidation susceptibility.

Corteselli, Elizabeth M / Sharafi, Mona / Hondal, Robert / MacPherson, Maximilian / White, Sheryl / Lam, Ying-Wai / Gold, Clarissa / Manuel, Allison M / van der Vliet, Albert / Schneebeli, Severin T / Anathy, Vikas / Li, Jianing / Janssen-Heininger, Yvonne M W

Nature communications

2023 Volume 14, Issue 1, Page(s) 4550

Abstract: Protein-S-glutathionylation is a post-translational modification involving the conjugation of glutathione to protein thiols, which can modulate the activity and structure of key cellular proteins. Glutaredoxins (GLRX) are oxidoreductases that regulate ... ...

Abstract	Protein-S-glutathionylation is a post-translational modification involving the conjugation of glutathione to protein thiols, which can modulate the activity and structure of key cellular proteins. Glutaredoxins (GLRX) are oxidoreductases that regulate this process by performing deglutathionylation. However, GLRX has five cysteines that are potentially vulnerable to oxidative modification, which is associated with GLRX aggregation and loss of activity. To date, GLRX cysteines that are oxidatively modified and their relative susceptibilities remain unknown. We utilized molecular modeling approaches, activity assays using recombinant GLRX, coupled with site-directed mutagenesis of each cysteine both individually and in combination to address the oxidizibility of GLRX cysteines. These approaches reveal that C8 and C83 are targets for S-glutathionylation and oxidation by hydrogen peroxide in vitro. In silico modeling and experimental validation confirm a prominent role of C8 for dimer formation and aggregation. Lastly, combinatorial mutation of C8, C26, and C83 results in increased activity of GLRX and resistance to oxidative inactivation and aggregation. Results from these integrated computational and experimental studies provide insights into the relative oxidizability of GLRX's cysteines and have implications for the use of GLRX as a therapeutic in settings of dysregulated protein glutathionylation.
MeSH term(s)	Animals ; Cysteine/metabolism ; Glutaredoxins/genetics ; Glutaredoxins/metabolism ; Glutathione/metabolism ; Mammals/metabolism ; Oxidation-Reduction ; Proteins/metabolism
Chemical Substances	Cysteine (K848JZ4886) ; Glutaredoxins ; Glutathione (GAN16C9B8O) ; Proteins
Language	English
Publishing date	2023-07-28
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-39664-2
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Article ; Online: Macrophage-intrinsic DUOX1 contributes to type 2 inflammation and mucus metaplasia during allergic airway disease.

Morris, Carolyn R / Habibovic, Aida / Dustin, Christopher M / Schiffers, Caspar / Lin, Miao-Chong / Ather, Jennifer L / Janssen-Heininger, Yvonne M W / Poynter, Matthew E / Utermohlen, Olaf / Krönke, Martin / van der Vliet, Albert

Mucosal immunology

2022 Volume 15, Issue 5, Page(s) 977–989

Abstract: The NADPH oxidase DUOX1 contributes to epithelial production of alarmins, including interleukin (IL)-33, in response to injurious triggers such as airborne protease allergens, and mediates development of mucus metaplasia and airway remodeling in chronic ... ...

Abstract	The NADPH oxidase DUOX1 contributes to epithelial production of alarmins, including interleukin (IL)-33, in response to injurious triggers such as airborne protease allergens, and mediates development of mucus metaplasia and airway remodeling in chronic allergic airways diseases. DUOX1 is also expressed in non-epithelial lung cell types, including macrophages that play an important role in airway remodeling during chronic lung disease. We therefore conditionally deleted DUOX1 in either lung epithelial or monocyte/macrophage lineages to address its cell-specific actions in innate airway responses to acute airway challenge with house dust mite (HDM) allergen, and in chronic HDM-driven allergic airway inflammation. As expected, acute responses to airway challenge with HDM, as well as type 2 inflammation and related features of airway remodeling during chronic HDM-induced allergic inflammation, were largely driven by DUOX1 with the respiratory epithelium. However, in the context of chronic HDM-driven inflammation, DUOX1 deletion in macrophages also significantly impaired type 2 cytokine production and indices of mucus metaplasia. Further studies revealed a contribution of macrophage-intrinsic DUOX1 in macrophage recruitment upon chronic HDM challenge, as well as features of macrophage activation that impact on type 2 inflammation and remodeling.
MeSH term(s)	Airway Remodeling ; Allergens ; Animals ; Antigens, Dermatophagoides ; Dual Oxidases ; Hypersensitivity ; Inflammation ; Lung ; Macrophages ; Metaplasia ; Mucus ; Pyroglyphidae
Chemical Substances	Allergens ; Antigens, Dermatophagoides ; Dual Oxidases (EC 1.11.1.-)
Language	English
Publishing date	2022-06-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2411370-0
ISSN	1935-3456 ; 1933-0219
ISSN (online)	1935-3456
ISSN	1933-0219
DOI	10.1038/s41385-022-00530-x
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Article ; Online: Hydrogen peroxide as a damage signal in tissue injury and inflammation: murderer, mediator, or messenger?

van der Vliet, Albert / Janssen-Heininger, Yvonne M W

Journal of cellular biochemistry

2014 Volume 115, Issue 3, Page(s) 427–435

Abstract: Tissue injury and inflammation are associated with increased production of reactive oxygen species (ROS), which have the ability to induce oxidative injury to various biomolecules resulting in protein dysfunction, genetic instability, or cell death. ... ...

Abstract	Tissue injury and inflammation are associated with increased production of reactive oxygen species (ROS), which have the ability to induce oxidative injury to various biomolecules resulting in protein dysfunction, genetic instability, or cell death. However, recent observations indicate that formation of hydrogen peroxide (H2 O2 ) during tissue injury is also an essential feature of the ensuing wound healing response, and functions as an early damage signal to control several critical aspects of the wound healing process. Because innate oxidative wound responses must be tightly coordinated to avoid chronic inflammation or tissue injury, a more complete understanding is needed regarding the origins and dynamics of ROS production, and their critical biological targets. This prospect highlights the current experimental evidence implicating H2 O2 in early epithelial wound responses, and summarizes technical advances and approaches that may help distinguish its beneficial actions from its more deleterious actions in conditions of chronic tissue injury or inflammation.
MeSH term(s)	Cell Movement/genetics ; Chemotaxis/genetics ; Cysteine/metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Inflammation/metabolism ; Inflammation/pathology ; Oxidative Stress ; Reactive Oxygen Species/metabolism ; Signal Transduction/genetics ; Wound Healing/genetics
Chemical Substances	Reactive Oxygen Species ; Hydrogen Peroxide (BBX060AN9V) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2014-04-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	392402-6
ISSN	1097-4644 ; 0730-2312
ISSN (online)	1097-4644
ISSN	0730-2312
DOI	10.1002/jcb.24683
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