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Article: Case Report: Profound newborn leukopenia related to a novel RAC2 variant.

Hall, Geoffrey / Donkó, Ágnes / Pratt, Cristina / Kim-Chang, Julie J / Martin, Paul L / Stallings, Amy P / Sleasman, John W / Holland, Steven M / Hsu, Amy P / Leto, Thomas L / Mousallem, Talal

Frontiers in pediatrics

2024 Volume 12, Page(s) 1365187

Abstract: We report the case of a 1-week-old male born full-term, who had two inconclusive severe combined immunodeficiency (SCID) newborn screens and developed scalp cellulitis ... ...

Abstract	We report the case of a 1-week-old male born full-term, who had two inconclusive severe combined immunodeficiency (SCID) newborn screens and developed scalp cellulitis and
Language	English
Publishing date	2024-03-07
Publishing country	Switzerland
Document type	Case Reports
ZDB-ID	2711999-3
ISSN	2296-2360
ISSN	2296-2360
DOI	10.3389/fped.2024.1365187
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Article ; Online: Functional Characterization of DUOX Enzymes in Reconstituted Cell Models.

Korzeniowska, Agnieszka / Donkó, Ágnes P / Morand, Stanislas / Leto, Thomas L

Methods in molecular biology (Clifton, N.J.)

2019 Volume 1982, Page(s) 173–190

Abstract: Biosynthesis of active human dual oxidases (DUOX1 and DUOX2) requires maturation factors, a.k.a. DUOX activator proteins (DUOXA1 and DUOXA2), that form covalent complexes with DUOX; both chains together represent the mature catalytic unit that functions ... ...

Abstract	Biosynthesis of active human dual oxidases (DUOX1 and DUOX2) requires maturation factors, a.k.a. DUOX activator proteins (DUOXA1 and DUOXA2), that form covalent complexes with DUOX; both chains together represent the mature catalytic unit that functions as a dedicated hydrogen peroxide-generating enzyme. Genetic defects in DUOX2 or DUOXA2 can result in congenital hypothyroidism, whereas partial defects in DUOX2 activity also have been associated with very early-onset inflammatory bowel disease. Our understanding of the links between DUOX dysfunction and these diseases remains incomplete. An important challenge in developing a better understanding of the pathogenic roles of DUOX defects requires robust and reliable DUOX reconstitution cell models to examine the functional consequences of candidate DUOX missense mutations and polymorphisms. Here, we describe methods for efficient heterologous DUOX/DUOXA co-expression and functional characterization, including detailed assessments of posttranslational processing and subcellular translocation of DUOX that accompanies the maturation of these enzymes into catalytically active NADPH oxidases.
MeSH term(s)	Dual Oxidases/chemistry ; Dual Oxidases/genetics ; Dual Oxidases/metabolism ; Enzyme Activation ; Flow Cytometry ; Fluorescent Antibody Technique ; Gene Expression ; HEK293 Cells ; Humans ; Hydrogen Peroxide/metabolism ; Protein Multimerization ; Protein Transport
Chemical Substances	Hydrogen Peroxide (BBX060AN9V) ; Dual Oxidases (EC 1.11.1.-)
Language	English
Publishing date	2019-06-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-9424-3_11
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Article ; Online: Hydrogen peroxide production by epidermal dual oxidase 1 regulates nociceptive sensory signals.

Pató, Anna / Bölcskei, Kata / Donkó, Ágnes / Kaszás, Diána / Boros, Melinda / Bodrogi, Lilla / Várady, György / Pape, Veronika F S / Roux, Benoit T / Enyedi, Balázs / Helyes, Zsuzsanna / Watt, Fiona M / Sirokmány, Gábor / Geiszt, Miklós

Redox biology

2023 Volume 62, Page(s) 102670

Abstract: Keratinocytes of the mammalian skin provide not only mechanical protection for the tissues, but also transmit mechanical, chemical, and thermal stimuli from the external environment to the sensory nerve terminals. Sensory nerve fibers penetrate the ... ...

Abstract	Keratinocytes of the mammalian skin provide not only mechanical protection for the tissues, but also transmit mechanical, chemical, and thermal stimuli from the external environment to the sensory nerve terminals. Sensory nerve fibers penetrate the epidermal basement membrane and function in the tight intercellular space among keratinocytes. Here we show that epidermal keratinocytes produce hydrogen peroxide upon the activation of the NADPH oxidase dual oxidase 1 (DUOX1). This enzyme can be activated by increasing cytosolic calcium levels. Using DUOX1 knockout animals as a model system we found an increased sensitivity towards certain noxious stimuli in DUOX1-deficient animals, which is not due to structural changes in the skin as evidenced by detailed immunohistochemical and electron-microscopic analysis of epidermal tissue. We show that DUOX1 is expressed in keratinocytes but not in the neural sensory pathway. The release of hydrogen peroxide by activated DUOX1 alters both the activity of neuronal TRPA1 and redox-sensitive potassium channels expressed in dorsal root ganglia primary sensory neurons. We describe hydrogen peroxide, produced by DUOX1 as a paracrine mediator of nociceptive signal transmission. Our results indicate that a novel, hitherto unknown redox mechanism modulates noxious sensory signals.
MeSH term(s)	Animals ; Dual Oxidases/genetics ; Hydrogen Peroxide/metabolism ; NADPH Oxidases/metabolism ; Peroxides ; Nociception ; NADPH Oxidase 1 ; Mammals/metabolism
Chemical Substances	Dual Oxidases (EC 1.11.1.-) ; Hydrogen Peroxide (BBX060AN9V) ; NADPH Oxidases (EC 1.6.3.-) ; Peroxides ; NADPH Oxidase 1 (EC 1.6.3.-)
Language	English
Publishing date	2023-03-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2023.102670
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Article ; Online: Nox/Duox Family of NADPH Oxidases: Lessons from Knockout Mouse Models.

Sirokmány, Gábor / Donkó, Ágnes / Geiszt, Miklós

Trends in pharmacological sciences

2016 Volume 37, Issue 4, Page(s) 318–327

Abstract: Nox/Duox NADPH oxidases are now considered the primary, regulated sources of reactive oxygen species (ROS). These enzymes are expressed in diverse cells and tissues, and their products are essential in several physiological settings. Knockout mouse ... ...

Abstract	Nox/Duox NADPH oxidases are now considered the primary, regulated sources of reactive oxygen species (ROS). These enzymes are expressed in diverse cells and tissues, and their products are essential in several physiological settings. Knockout mouse models are instrumental in identifying the physiological functions of Nox/Duox enzymes as well as in exploring the impact of their pharmacological targeting on disease progression. The currently available data from experiments on knockout animals suggest that the lack of non-phagocytic Nox/Duox enzymes often modifies the course and phenotype in many disease models. Nevertheless, as illustrated by studies on Nox4-deficient animals, the absence of Nox-derived ROS can also lead to aggravated disease manifestation, reinforcing the need for a more balanced view on the role of ROS in health and disease.
MeSH term(s)	Animals ; Humans ; Mice ; Mice, Knockout ; NADH, NADPH Oxidoreductases/deficiency ; NADH, NADPH Oxidoreductases/genetics ; NADH, NADPH Oxidoreductases/metabolism
Chemical Substances	NADH, NADPH Oxidoreductases (EC 1.6.-)
Language	English
Publishing date	2016-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	282846-7
ISSN	1873-3735 ; 0165-6147
ISSN (online)	1873-3735
ISSN	0165-6147
DOI	10.1016/j.tips.2016.01.006
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Article ; Online: Hydrogen peroxide production by epidermal dual oxidase 1 regulates nociceptive sensory signals

Anna Pató / Kata Bölcskei / Ágnes Donkó / Diána Kaszás / Melinda Boros / Lilla Bodrogi / György Várady / Veronika F.S. Pape / Benoit T. Roux / Balázs Enyedi / Zsuzsanna Helyes / Fiona M. Watt / Gábor Sirokmány / Miklós Geiszt

Redox Biology, Vol 62, Iss , Pp 102670- (2023)

2023

Abstract	Keratinocytes of the mammalian skin provide not only mechanical protection for the tissues, but also transmit mechanical, chemical, and thermal stimuli from the external environment to the sensory nerve terminals. Sensory nerve fibers penetrate the epidermal basement membrane and function in the tight intercellular space among keratinocytes. Here we show that epidermal keratinocytes produce hydrogen peroxide upon the activation of the NADPH oxidase dual oxidase 1 (DUOX1). This enzyme can be activated by increasing cytosolic calcium levels. Using DUOX1 knockout animals as a model system we found an increased sensitivity towards certain noxious stimuli in DUOX1-deficient animals, which is not due to structural changes in the skin as evidenced by detailed immunohistochemical and electron-microscopic analysis of epidermal tissue. We show that DUOX1 is expressed in keratinocytes but not in the neural sensory pathway. The release of hydrogen peroxide by activated DUOX1 alters both the activity of neuronal TRPA1 and redox-sensitive potassium channels expressed in dorsal root ganglia primary sensory neurons. We describe hydrogen peroxide, produced by DUOX1 as a paracrine mediator of nociceptive signal transmission.Our results indicate that a novel, hitherto unknown redox mechanism modulates noxious sensory signals.
Keywords	NADPH oxidase ; Hydrogen peroxide ; Dual oxidase 1 ; DUOX1 ; Skin ; Nociception ; Medicine (General) ; R5-920 ; Biology (General) ; QH301-705.5
Subject code	571
Language	English
Publishing date	2023-06-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: A Novel RAC2 Variant Presenting as Severe Combined Immunodeficiency.

Stern, Heather / Donkó, Agnes / Shapiro, Teresa / Hsu, Amy P / Leto, Thomas L / Holland, Steven M / Andreae, Doerthe Adriana

Journal of clinical immunology

2020 Volume 41, Issue 2, Page(s) 473–476

MeSH term(s)	Adenylate Kinase/genetics ; Humans ; Infant, Newborn ; Male ; Mutation/genetics ; Severe Combined Immunodeficiency/genetics ; T-Lymphocytes/metabolism
Chemical Substances	Adenylate Kinase (EC 2.7.4.3) ; adenylate kinase 2 (EC 2.7.4.3)
Language	English
Publishing date	2020-11-13
Publishing country	Netherlands
Document type	Case Reports ; Letter
ZDB-ID	779361-3
ISSN	1573-2592 ; 0271-9142
ISSN (online)	1573-2592
ISSN	0271-9142
DOI	10.1007/s10875-020-00915-2
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Article ; Online: BTK drives neutrophil activation for sterilizing antifungal immunity.

Desai, Jigar V / Zarakas, Marissa A / Wishart, Andrew L / Roschewski, Mark / Aufiero, Mariano A / Donkó, Ágnes / Wigerblad, Gustaf / Shlezinger, Neta / Plate, Markus / James, Matthew R / Lim, Jean K / Uzel, Gulbu / Bergerson, Jenna Re / Fuss, Ivan / Cramer, Robert A / Franco, Luis M / Clark, Emily S / Khan, Wasif N / Yamanaka, Daisuke /

Chamilos, Georgios / El-Benna, Jamel / Kaplan, Mariana J / Staudt, Louis M / Leto, Thomas L / Holland, Steven M / Wilson, Wyndham H / Hohl, Tobias M / Lionakis, Michail S

The Journal of clinical investigation

2024

Abstract: We describe a previously-unappreciated role for Bruton's tyrosine kinase (BTK) in fungal immune surveillance against aspergillosis, an unforeseen complication of BTK inhibitors (BTKi) used for treating B-cell lymphoid malignancies. We studied BTK- ... ...

Abstract	We describe a previously-unappreciated role for Bruton's tyrosine kinase (BTK) in fungal immune surveillance against aspergillosis, an unforeseen complication of BTK inhibitors (BTKi) used for treating B-cell lymphoid malignancies. We studied BTK-dependent fungal responses in neutrophils from diverse populations, including healthy donors, BTKi-treated patients, and X-linked agammaglobulinemia patients. Upon fungal exposure, BTK was activated in human neutrophils in a TLR2-, Dectin-1-, and FcγR-dependent manner, triggering the oxidative burst. BTK inhibition selectively impeded neutrophil-mediated damage to Aspergillus hyphae, primary granule release, and the fungus-induced oxidative burst by abrogating NADPH oxidase subunit p40phox and GTPase RAC2 activation. Moreover, neutrophil-specific Btk deletion in mice enhanced aspergillosis susceptibility by impairing neutrophil function, not recruitment or lifespan. Conversely, GM-CSF partially mitigated these deficits by enhancing p47phox activation. Our findings underline the crucial role of BTK signaling in neutrophils for antifungal immunity and provide a rationale for GM-CSF use to offset these deficits in susceptible patients.
Language	English
Publishing date	2024-05-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	3067-3
ISSN	1558-8238 ; 0021-9738
ISSN (online)	1558-8238
ISSN	0021-9738
DOI	10.1172/JCI176142
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Article ; Online: Spatial and temporal analysis of NADPH oxidase-generated hydrogen peroxide signals by novel fluorescent reporter proteins.

Enyedi, Balázs / Zana, Melinda / Donkó, Ágnes / Geiszt, Miklós

Antioxidants & redox signaling

2013 Volume 19, Issue 6, Page(s) 523–534

Abstract: Aims: Hydrogen peroxide (H2O2) is an emerging signaling molecule with diverse regulatory functions. Despite its significance, the spatial and temporal organization of H2O2 signals within cells is basically unknown. Our limited knowledge about H2O2 ... ...

Abstract	Aims: Hydrogen peroxide (H2O2) is an emerging signaling molecule with diverse regulatory functions. Despite its significance, the spatial and temporal organization of H2O2 signals within cells is basically unknown. Our limited knowledge about H2O2 signals is largely due to the lack of appropriate techniques for measuring intracellular H2O2. The aim of the current study was to develop novel fluorescent reporter proteins for the measurement of intracellular H2O2. Results: We developed two novel, fluorescence resonance energy transfer-based redox probes that undergo opposite emission ratio changes upon exposure to H2O2. We have successfully used these sensors to measure H2O2 production by NADPH oxidases (Nox). Moreover, we targeted these probes to specific cellular compartments or incorporated them into oxidase complexes to detect H2O2 at different, well-defined loci. Innovation: Studying Nox2- and dual oxidase 1 (Duox1)-expressing cells, we provide the first analysis of how NADPH-oxidase generated H2O2 signals radiate within and between cells. Conclusion: Our results suggest that H2O2 produced by Noxs can induce redox changes in the intracellular milieu of Nox/Duox-expressing cells while simultaneously transmitting paracrine effects to neighboring cells.
MeSH term(s)	Animals ; Biosensing Techniques ; COS Cells ; Cercopithecus aethiops ; Dual Oxidases ; Fluorescence Resonance Energy Transfer ; Glutathione Peroxidase/biosynthesis ; Glutathione Peroxidase/genetics ; Green Fluorescent Proteins/biosynthesis ; Green Fluorescent Proteins/genetics ; HeLa Cells ; Humans ; Hydrogen Peroxide/metabolism ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Knockout ; NADPH Oxidase 2 ; NADPH Oxidases/metabolism ; Oxidation-Reduction ; Paracrine Communication ; Protein Transport ; Recombinant Fusion Proteins/biosynthesis ; Recombinant Fusion Proteins/genetics ; Saccharomyces cerevisiae Proteins/biosynthesis ; Saccharomyces cerevisiae Proteins/genetics ; Signal Transduction ; Transcription Factors/biosynthesis ; Transcription Factors/genetics
Chemical Substances	Membrane Glycoproteins ; Recombinant Fusion Proteins ; Saccharomyces cerevisiae Proteins ; Transcription Factors ; YAP1 protein, S cerevisiae ; Green Fluorescent Proteins (147336-22-9) ; Hydrogen Peroxide (BBX060AN9V) ; Dual Oxidases (EC 1.11.1.-) ; Glutathione Peroxidase (EC 1.11.1.9) ; HYR1 protein, S cerevisiae (EC 1.11.1.9) ; CYBB protein, human (EC 1.6.3.-) ; NADPH Oxidase 2 (EC 1.6.3.-) ; NADPH Oxidases (EC 1.6.3.-) ; DUOX1 protein, human (EC 1.6.3.1)
Language	English
Publishing date	2013-08-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1483836-9
ISSN	1557-7716 ; 1523-0864
ISSN (online)	1557-7716
ISSN	1523-0864
DOI	10.1089/ars.2012.4594
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Article ; Online: Epidermal growth factor-induced hydrogen peroxide production is mediated by dual oxidase 1.

Sirokmány, Gábor / Pató, Anna / Zana, Melinda / Donkó, Ágnes / Bíró, Adrienn / Nagy, Péter / Geiszt, Miklós

Free radical biology & medicine

2016 Volume 97, Page(s) 204–211

Abstract: Stimulation of mammalian cells by epidermal growth factor (EGF) elicits complex signaling events, including an increase in hydrogen peroxide (H2O2) production. Understanding the significance of this response is limited by the fact that the source of EGF- ... ...

Abstract	Stimulation of mammalian cells by epidermal growth factor (EGF) elicits complex signaling events, including an increase in hydrogen peroxide (H2O2) production. Understanding the significance of this response is limited by the fact that the source of EGF-induced H2O2 production is unknown. Here we show that EGF-induced H2O2 production in epidermal cell lines is dependent on the agonist-induced calcium signal. We analyzed the expression of NADPH oxidase isoforms and found both A431 and HaCaT cells to express the calcium-sensitive NADPH oxidase, Dual oxidase 1 (Duox1) and its protein partner Duox activator 1 (DuoxA1). Inhibition of Duox1 expression by small interfering RNAs eliminated EGF-induced H2O2 production in both cell lines. We also demonstrate that H2O2 production by Duox1 leads to the oxidation of thioredoxin-1 and the cytosolic peroxiredoxins. Our observations provide evidence for a new signaling paradigm in which changes of intracellular calcium concentration are transformed into redox signals through the calcium-dependent activation of Duox1.
Language	English
Publishing date	2016-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2016.05.028
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Article ; Online: Peroxidasin-mediated crosslinking of collagen IV is independent of NADPH oxidases.

Sirokmány, Gábor / Kovács, Hajnal A / Lázár, Enikő / Kónya, Krisztina / Donkó, Ágnes / Enyedi, Balázs / Grasberger, Helmut / Geiszt, Miklós

Redox biology

2018 Volume 16, Page(s) 314–321

Abstract: Collagen IV is a major component of the basement membrane in epithelial tissues. The NC1 domains of collagen IV protomers are covalently linked together through sulfilimine bonds, the formation of which is catalyzed by peroxidasin. Although hydrogen ... ...

Abstract	Collagen IV is a major component of the basement membrane in epithelial tissues. The NC1 domains of collagen IV protomers are covalently linked together through sulfilimine bonds, the formation of which is catalyzed by peroxidasin. Although hydrogen peroxide is essential for this reaction, the exact source of the oxidant remains elusive. Members of the NOX/DUOX NADPH oxidase family are specifically devoted to the production of superoxide and hydrogen peroxide. Our aim in this study was to find out if NADPH oxidases contribute in vivo to the formation of collagen IV sulfilimine crosslinks. We used multiple genetically modified in vivo model systems to provide a detailed assessment of this question. Our data indicate that in various peroxidasin-expressing tissues sulfilimine crosslinks between the NC1 domains of collagen IV can be readily detected in the absence of functioning NADPH oxidases. We also analyzed how subatmospheric oxygen levels influence the collagen IV network in collagen-producing cultured cells with rapid matrix turnover. We showed that collagen IV crosslinks remain intact even under strongly hypoxic conditions. Our hypothesis is that during collagen IV network formation PXDN cooperates with a NOX/DUOX-independent H
MeSH term(s)	Basement Membrane/metabolism ; Catalysis ; Cell Line ; Collagen Type IV/metabolism ; Dual Oxidases/metabolism ; Epithelial Cells/metabolism ; Extracellular Matrix ; Extracellular Matrix Proteins/metabolism ; Humans ; Hydrogen Peroxide/metabolism ; NADPH Oxidases/metabolism ; Oxygen/metabolism ; Peroxidase/metabolism ; Superoxides/metabolism ; Peroxidasin
Chemical Substances	Collagen Type IV ; Extracellular Matrix Proteins ; Superoxides (11062-77-4) ; Hydrogen Peroxide (BBX060AN9V) ; Dual Oxidases (EC 1.11.1.-) ; Peroxidase (EC 1.11.1.7) ; NADPH Oxidases (EC 1.6.3.-) ; Oxygen (S88TT14065)
Language	English
Publishing date	2018-03-14
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2018.03.009
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