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Article ; Online: CGD: less is more.

Ligeti, Erzsébet / Geiszt, Miklós

2020 Volume 135, Issue 12, Page(s) 883–884

MeSH term(s)	Cell Wall ; Granulomatous Disease, Chronic ; Humans ; Leukotriene B4 ; NADPH Oxidases ; Neutrophil Infiltration ; Neutrophils
Chemical Substances	Leukotriene B4 (1HGW4DR56D) ; NADPH Oxidases (EC 1.6.3.-)
Language	English
Publishing date	2020-03-19
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood.2020005062
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Article ; Online: Imaging Intracellular H

Enyedi, Balázs / Geiszt, Miklós

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

2019 Volume 1982, Page(s) 275–282

Abstract: Hydrogen peroxide ( ... ...

Abstract	Hydrogen peroxide (H
MeSH term(s)	Biosensing Techniques ; Data Analysis ; Fluorescence Resonance Energy Transfer ; Gene Expression ; Genes, Reporter ; HeLa Cells ; Humans ; Hydrogen Peroxide/metabolism ; Image Processing, Computer-Assisted ; Intracellular Space ; Microscopy, Fluorescence ; Molecular Imaging/methods
Chemical Substances	Hydrogen Peroxide (BBX060AN9V)
Language	English
Publishing date	2019-06-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-9424-3_16
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Article ; Online: A novel monoclonal antibody reveals the enrichment of NADPH oxidase 5 in human splenic endothelial cells.

Szeles, Zsolt / Petheő, Gábor L / Szikora, Bence / Kacskovics, Imre / Geiszt, Miklós

Scientific reports

2023 Volume 13, Issue 1, Page(s) 17174

Abstract: Members of the NOX/DUOX family of NADPH oxidases are responsible for regulated ROS production in diverse cells and tissues. Detection of NOX/DUOX proteins at the protein level remains an important challenge in the field. Here we report the development ... ...

Abstract	Members of the NOX/DUOX family of NADPH oxidases are responsible for regulated ROS production in diverse cells and tissues. Detection of NOX/DUOX proteins at the protein level remains an important challenge in the field. Here we report the development and characterization of a novel anti-NOX5 monoclonal antibody, which recognizes the human NOX5 protein in both Western blot, immunocytochemistry, and histochemistry applications. With the help of the antibody we could successfully detect both heterologously and endogenously expressed NOX5 in mammalian cells. Furthermore, we could also detect NOX5 protein in the human spleen, testis, and ovary. Immunohistochemical studies on human testis revealed that NOX5 localized to spermatogenic cells. This expression pattern was also supported by the result of in silico analysis of single-cell RNA sequencing data that indicated that NOX5 protein is present in developing spermatids and spermatocytes. Mature spermatozoa, however, did not contain detectable NOX5. In the human ovary, both immunostaining and single-cell RNA sequencing suggest that NOX5 is expressed in interstitial fibroblasts and theca cells. We also analyzed vascular cells for the presence of NOX5 and we found that NOX5 expression is a fairly specific feature of splenic endothelial cells.
MeSH term(s)	Animals ; Female ; Humans ; Male ; NADPH Oxidase 5 ; Membrane Proteins/metabolism ; Antibodies, Monoclonal ; Endothelial Cells/metabolism ; Spleen/metabolism ; Testis/metabolism ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Reactive Oxygen Species/metabolism ; Mammals/metabolism
Chemical Substances	NADPH Oxidase 5 (EC 1.6.3.-) ; Membrane Proteins ; Antibodies, Monoclonal ; NADPH Oxidases (EC 1.6.3.-) ; Reactive Oxygen Species
Language	English
Publishing date	2023-10-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-023-44018-5
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Article ; Online: The Relationship of NADPH Oxidases and Heme Peroxidases: Fallin' in and Out.

Sirokmány, Gábor / Geiszt, Miklós

Frontiers in immunology

2019 Volume 10, Page(s) 394

Abstract: Peroxidase enzymes can oxidize a multitude of substrates in diverse biological processes. According to the latest phylogenetic analysis, there are four major heme peroxidase superfamilies. In this review, we focus on certain members of the cyclooxygenase- ...

Abstract	Peroxidase enzymes can oxidize a multitude of substrates in diverse biological processes. According to the latest phylogenetic analysis, there are four major heme peroxidase superfamilies. In this review, we focus on certain members of the cyclooxygenase-peroxidase superfamily (also labeled as animal heme peroxidases) and their connection to specific NADPH oxidase enzymes which provide H
MeSH term(s)	Animals ; Eosinophils/metabolism ; Hemeproteins/metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Leukocytes/metabolism ; NADPH Oxidases/metabolism ; Oxidation-Reduction ; Peroxidase/metabolism ; Prostaglandin-Endoperoxide Synthases/metabolism
Chemical Substances	Hemeproteins ; Hydrogen Peroxide (BBX060AN9V) ; Peroxidase (EC 1.11.1.7) ; Prostaglandin-Endoperoxide Synthases (EC 1.14.99.1) ; NADPH Oxidases (EC 1.6.3.-)
Language	English
Publishing date	2019-03-05
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2019.00394
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Article ; Online: A novel monoclonal antibody reveals the enrichment of NADPH oxidase 5 in human splenic endothelial cells

Zsolt Szeles / Gábor L. Petheő / Bence Szikora / Imre Kacskovics / Miklós Geiszt

Scientific Reports, Vol 13, Iss 1, Pp 1-

2023 Volume 13

Abstract: Abstract Members of the NOX/DUOX family of NADPH oxidases are responsible for regulated ROS production in diverse cells and tissues. Detection of NOX/DUOX proteins at the protein level remains an important challenge in the field. Here we report the ... ...

Abstract	Abstract Members of the NOX/DUOX family of NADPH oxidases are responsible for regulated ROS production in diverse cells and tissues. Detection of NOX/DUOX proteins at the protein level remains an important challenge in the field. Here we report the development and characterization of a novel anti-NOX5 monoclonal antibody, which recognizes the human NOX5 protein in both Western blot, immunocytochemistry, and histochemistry applications. With the help of the antibody we could successfully detect both heterologously and endogenously expressed NOX5 in mammalian cells. Furthermore, we could also detect NOX5 protein in the human spleen, testis, and ovary. Immunohistochemical studies on human testis revealed that NOX5 localized to spermatogenic cells. This expression pattern was also supported by the result of in silico analysis of single-cell RNA sequencing data that indicated that NOX5 protein is present in developing spermatids and spermatocytes. Mature spermatozoa, however, did not contain detectable NOX5. In the human ovary, both immunostaining and single-cell RNA sequencing suggest that NOX5 is expressed in interstitial fibroblasts and theca cells. We also analyzed vascular cells for the presence of NOX5 and we found that NOX5 expression is a fairly specific feature of splenic endothelial cells.
Keywords	Medicine ; R ; Science ; Q
Subject code	616
Language	English
Publishing date	2023-10-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article ; Online: Autotaxin-lysophosphatidic acid receptor 5 axis evokes endothelial dysfunction via reactive oxygen species signaling.

Janovicz, Anna / Majer, Aliz / Kosztelnik, Mónika / Geiszt, Miklós / Chun, Jerold / Ishii, Satoshi / Tigyi, Gábor József / Benyó, Zoltán / Ruisanchez, Éva

Experimental biology and medicine (Maywood, N.J.)

2023 Volume 248, Issue 20, Page(s) 1887–1894

Abstract: Lysophosphatidylcholine (LPC) is a bioactive lipid that has been shown to attenuate endothelium-dependent vasorelaxation contributing to endothelial dysfunction; however, the underlying mechanisms are not well understood. In this study, we investigated ... ...

Abstract	Lysophosphatidylcholine (LPC) is a bioactive lipid that has been shown to attenuate endothelium-dependent vasorelaxation contributing to endothelial dysfunction; however, the underlying mechanisms are not well understood. In this study, we investigated the molecular mechanisms involved in the development of LPC-evoked impairment of endothelium-dependent vasorelaxation. In aortic rings isolated from wild-type (WT) mice, a 20-min exposure to LPC significantly reduced the acetylcholine chloride (ACh)-induced vasorelaxation indicating the impairment of normal endothelial function. Interestingly, pharmacological inhibition of autotaxin (ATX) by GLPG1690 partially reversed the endothelial dysfunction, suggesting that lysophosphatidic acid (LPA) derived from LPC may be involved in the effect. Therefore, the effect of LPC was also tested in aortic rings isolated from different LPA receptor knock-out (KO) mice. LPC evoked a marked reduction in ACh-dependent vasorelaxation in
MeSH term(s)	Animals ; Mice ; Endothelium/metabolism ; Hydrogen Peroxide ; Lysophosphatidylcholines/pharmacology ; Lysophosphatidylcholines/metabolism ; Lysophospholipids/pharmacology ; Lysophospholipids/metabolism ; Reactive Oxygen Species/metabolism ; Receptors, Lysophosphatidic Acid/metabolism
Chemical Substances	Hydrogen Peroxide (BBX060AN9V) ; Lysophosphatidylcholines ; Lysophospholipids ; Reactive Oxygen Species ; Receptors, Lysophosphatidic Acid ; LPAR5 protein, mouse ; alkylglycerophosphoethanolamine phosphodiesterase (EC 3.1.4.39)
Language	English
Publishing date	2023-10-14
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	4015-0
ISSN	1535-3699 ; 1525-1373 ; 0037-9727
ISSN (online)	1535-3699 ; 1525-1373
ISSN	0037-9727
DOI	10.1177/15353702231199081
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Article: Characterization of the Proprotein Convertase-Mediated Processing of Peroxidasin and Peroxidasin-like Protein.

Kovács, Hajnal A / Lázár, Enikő / Várady, György / Sirokmány, Gábor / Geiszt, Miklós

Antioxidants (Basel, Switzerland)

2021 Volume 10, Issue 10

Abstract: Peroxidasin (PXDN) and peroxidasin-like protein (PXDNL) are members of the peroxidase-cyclooxygenase superfamily. PXDN functions in basement membrane synthesis by forming collagen IV crosslinks, while the function of PXDNL remains practically unknown. In ...

Abstract	Peroxidasin (PXDN) and peroxidasin-like protein (PXDNL) are members of the peroxidase-cyclooxygenase superfamily. PXDN functions in basement membrane synthesis by forming collagen IV crosslinks, while the function of PXDNL remains practically unknown. In this work, we characterized the post-translational proteolytic processing of PXDN and PXDNL. Using a novel knock-in mouse model, we demonstrate that the proteolytic cleavage of PXDN occurs in vivo. With the help of furin-specific siRNA we also demonstrate that the proprotein-convertase, furin participates in the proteolytic processing of PXDN. Furthermore, we demonstrate that only the proteolytically processed PXDN integrates into the extracellular matrix, highlighting the importance of the proteolysis step in PXDN's collagen IV-crosslinking activity. We also provide multiple lines of evidence for the importance of peroxidase activity in the proteolytic processing of PXDN. Finally, we show that PXDNL does not undergo proteolytic processing, despite containing sequence elements efficiently recognized by proprotein convertases. Collectively, our observations suggest a previously unknown protein quality control during PXDN synthesis and the importance of the peroxidase activity of PXDN in this process.
Language	English
Publishing date	2021-09-30
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox10101565
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Article: NADPH oxidases: new kids on the block.

Geiszt, Miklós

Cardiovascular research

2006 Volume 71, Issue 2, Page(s) 289–299

Abstract: Reactive oxygen species (ROS) play a pivotal role in many physiological processes including host defense, hormone biosynthesis, fertilization and cellular signaling. Altered production of ROS has been implicated in the development of immunodeficiency, ... ...

Abstract	Reactive oxygen species (ROS) play a pivotal role in many physiological processes including host defense, hormone biosynthesis, fertilization and cellular signaling. Altered production of ROS has been implicated in the development of immunodeficiency, hypothyroidism and cardiovascular pathologies. In the last few years, several enzymes were identified at the molecular level, which are now thought to be responsible for ROS production observed in diverse tissues. These enzymes show a high degree of homology to the phagocytic NADPH oxidase and are now designated the Nox family of NADPH oxidases. This review updates our knowledge on six new members of the Nox family: Nox1, Nox3, Nox4, Nox5, Duox1 and Duox2.
MeSH term(s)	Dual Oxidases ; Flavoproteins/metabolism ; Humans ; Membrane Proteins/metabolism ; Muscle, Smooth, Vascular/enzymology ; NADPH Oxidase 1 ; NADPH Oxidase 4 ; NADPH Oxidase 5 ; NADPH Oxidases/metabolism ; NADPH Oxidases/physiology ; Thyroid Gland/enzymology
Chemical Substances	Flavoproteins ; Membrane Proteins ; Dual Oxidases (EC 1.11.1.-) ; NADPH Oxidase 1 (EC 1.6.3.-) ; NADPH Oxidase 4 (EC 1.6.3.-) ; NADPH Oxidase 5 (EC 1.6.3.-) ; NADPH Oxidases (EC 1.6.3.-) ; NOX1 protein, human (EC 1.6.3.-) ; NOX4 protein, human (EC 1.6.3.-) ; NOX5 protein, human (EC 1.6.3.-) ; Nox3 protein, human (EC 1.6.3.-) ; DUOX1 protein, human (EC 1.6.3.1) ; DUOX2 protein, human (EC 1.6.3.1)
Language	English
Publishing date	2006-07-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80340-6
ISSN	1755-3245 ; 0008-6363
ISSN (online)	1755-3245
ISSN	0008-6363
DOI	10.1016/j.cardiores.2006.05.004
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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: 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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