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Article: Novel sources of reactive oxygen species in the human body.

Orient, Anna / Donkó, Agnes / Szabó, Attila / Leto, Thomas L / Geiszt, Miklós

Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association

2007 Volume 22, Issue 5, Page(s) 1281–1288

MeSH term(s)	Gene Expression Regulation, Enzymologic ; Humans ; Kidney/enzymology ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Phagocytes/enzymology ; Phagocytes/physiology ; Reactive Oxygen Species/metabolism ; Superoxides/metabolism
Chemical Substances	Reactive Oxygen Species ; Superoxides (11062-77-4) ; NADPH Oxidases (EC 1.6.3.-)
Language	English
Publishing date	2007-05
Publishing country	England
Document type	Editorial ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	90594-x
ISSN	1460-2385 ; 0931-0509
ISSN (online)	1460-2385
ISSN	0931-0509
DOI	10.1093/ndt/gfm077
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Zs.A 2198: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 329: Show issues

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Article ; Online: Urothelial cells produce hydrogen peroxide through the activation of Duox1.

Donkó, Agnes / Ruisanchez, Eva / Orient, Anna / Enyedi, Balázs / Kapui, Réka / Péterfi, Zalán / de Deken, Xavier / Benyó, Zoltán / Geiszt, Miklós

Free radical biology & medicine

2010 Volume 49, Issue 12, Page(s) 2040–2048

Abstract: Hydrogen peroxide (H(2)O(2)) has important messenger and effector functions in the plant and animal kingdom. Phagocytes produce H(2)O(2) to kill pathogens, and epithelial cells of large airways have also been reported to produce H(2)O(2) for signaling ... ...

Abstract	Hydrogen peroxide (H(2)O(2)) has important messenger and effector functions in the plant and animal kingdom. Phagocytes produce H(2)O(2) to kill pathogens, and epithelial cells of large airways have also been reported to produce H(2)O(2) for signaling and host defense purposes. In this report, we show for the first time that urothelial cells produce H(2)O(2) in response to a calcium signal. Using a gene-deficient mouse model we also demonstrate that H(2)O(2) is produced by the NADPH oxidase Duox1, which is expressed in the mouse urothelium. In contrast, we found no evidence for the expression of lactoperoxidase, an enzyme that has been shown to cooperate with Duox enzymes. We also found that specific activation of TRPV4 calcium channels elicits a calcium signal and stimulates H(2)O(2) production in urothelial cells. Furthermore, we detected altered pressure responses in the urinary bladders of Duox1 knockout animals. Our results raise the possibility that mechanosensing in epithelial cells involves calcium-dependent H(2)O(2) production similar to that observed in plants.
MeSH term(s)	Animals ; Calcium Signaling/drug effects ; Dual Oxidases ; Enzyme Activation ; Epithelial Cells/enzymology ; Epithelial Cells/metabolism ; Escherichia coli/growth & development ; Hydrogen Peroxide/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Microbial Viability ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; TRPV Cation Channels/metabolism ; Thapsigargin/pharmacology ; Urinary Bladder/cytology ; Urinary Bladder/microbiology ; Urinary Bladder/physiology ; Urothelium/cytology ; Urothelium/physiology
Chemical Substances	TRPV Cation Channels ; Trpv4 protein, mouse ; Thapsigargin (67526-95-8) ; Hydrogen Peroxide (BBX060AN9V) ; Dual Oxidases (EC 1.11.1.-) ; NADPH Oxidases (EC 1.6.3.-) ; Duox1 protein, mouse (EC 1.6.3.1)
Language	English
Publishing date	2010-12-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2010.09.027
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Zs.A 2109: Show issues

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Article ; Online: Molecular and functional characterization of Hv1 proton channel in human granulocytes.

Petheo, Gábor L / Orient, Anna / Baráth, Mónika / Kovács, István / Réthi, Bence / Lányi, Arpád / Rajki, Anikó / Rajnavölgyi, Eva / Geiszt, Miklós

PloS one

2010 Volume 5, Issue 11, Page(s) e14081

Abstract: Voltage-gated proton current (I(Hv)) has been characterized in several cell types, but the majority of the data was collected in phagocytes, especially in human granulocytes. The prevailing view about the role of I(Hv) in phagocytes is that it is an ... ...

Abstract	Voltage-gated proton current (I(Hv)) has been characterized in several cell types, but the majority of the data was collected in phagocytes, especially in human granulocytes. The prevailing view about the role of I(Hv) in phagocytes is that it is an essential supporter of the intense and sustained activity of Nox2 (the core enzyme of the phagocyte NADPH oxidase complex) during respiratory burst. Recently H(v)1, a voltage-gated proton channel, was cloned, and leukocytes from H(v)1 knockout mice display impaired respiratory burst. On the other hand, hardly anything is known about H(v)1 in human granulocytes. Using qPCR and a self made antibody, we detected a significant amount of H(v)1 in human eosinophil and neutrophil granulocytes and in PLB-985 leukemia cells. Using different crosslinking agents and detergents in reducing and non-reducing PAGE, significant expression of H(v)1 homodimers, but not that of higher-order multimers, could be detected in granulocytes. Results of subcellular fractionation and confocal imaging indicate that H(v)1 is resident in both plasmalemmal and granular membrane compartments of resting neutrophils. Furthermore, it is also demonstrated that H(v)1 accumulates in phagosome wall during zymosan engulfment together with, but independently of Nox2. During granulocytic differentiation early and parallel upregulation of H(v)1 and Nox2 expression was observed in PLB-985 cells. The upregulation of H(v)1 or Nox2 expression did not require the normal expression of the other molecule. Using RNA interference, we obtained strong correlation between H(v)1 expression and I(Hv) density in PLB-985 cells. It is also demonstrated that a massive reduction in H(v)1 expression can limit the Nox2 mediated superoxide production of PLB-985 granulocytes. In summary, beside monomers native H(v)1 forms stable proton channel dimer in resting and activated human granulocytes. The expression pattern of H(v)1 in granulocytes is optimized to support intense NADPH oxidase activity.
MeSH term(s)	Animals ; Blotting, Western ; COS Cells ; Cell Differentiation ; Cell Line, Tumor ; Cells, Cultured ; Chlorocebus aethiops ; Eosinophils/cytology ; Eosinophils/metabolism ; Gene Expression ; Granulocytes/cytology ; Granulocytes/metabolism ; Humans ; Intracellular Membranes/metabolism ; Ion Channels/chemistry ; Ion Channels/genetics ; Ion Channels/metabolism ; Jurkat Cells ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Microscopy, Confocal ; NADPH Oxidase 2 ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Neutrophils/cytology ; Neutrophils/metabolism ; Phagosomes/metabolism ; Protein Multimerization ; RNA Interference ; Reverse Transcriptase Polymerase Chain Reaction ; Superoxides/metabolism
Chemical Substances	HVCN1 protein, human ; Ion Channels ; Membrane Glycoproteins ; Superoxides (11062-77-4) ; CYBB protein, human (EC 1.6.3.-) ; NADPH Oxidase 2 (EC 1.6.3.-) ; NADPH Oxidases (EC 1.6.3.-)
Language	English
Publishing date	2010-11-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0014081
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Article ; Online: Mechanisms of angiotensin II-mediated regulation of aldosterone synthase expression in H295R human adrenocortical and rat adrenal glomerulosa cells.

Szekeres, Mária / Turu, Gábor / Orient, Anna / Szalai, Bence / Süpeki, Katinka / Cserzo, Miklós / Várnai, Péter / Hunyady, László

Molecular and cellular endocrinology

2009 Volume 302, Issue 2, Page(s) 244–253

Abstract: In adrenal zona glomerulosa cells angiotensin II (Ang II) is a key regulator of steroidogenesis. Our purpose was to compare the mechanisms of Ang II-induced changes in the expression level of early transcription factors NR4A1 (NGFIB) and NR4A2 (Nurr1) ... ...

Abstract	In adrenal zona glomerulosa cells angiotensin II (Ang II) is a key regulator of steroidogenesis. Our purpose was to compare the mechanisms of Ang II-induced changes in the expression level of early transcription factors NR4A1 (NGFIB) and NR4A2 (Nurr1) genes, and the CYP11B2 gene encoding aldosterone synthase in H295R human adrenocortical tumor cells and in primary rat adrenal glomerulosa cells. Real-time PCR studies have demonstrated that Ang II increased the expression levels of NR4A1 and NR4A2 in H295R cells within 1 h after stimulation, which persisted up to 6 h; whereas in rat adrenal glomerulosa cells the kinetics of the expression of these genes were more rapid and transient. Ang II also induced prolonged nuclear translocation of Nurr1 and NGFIB proteins in both cell types. Studies using MEK inhibitor (PD98059, 20 microM), protein kinase C inhibitor (BIM1, 3 microM) and calmodulin kinase (CAMK) inhibitor (KN93, 10 microM) revealed that in rat adrenal glomerulosa cells CAMK-mediated mechanisms play a predominant role in the regulation of CYP11B2. In accordance with earlier findings, in H295R cells MEK inhibition increased the expression of NR4A1, NR4A2 and CYP11B2 genes, however, it decreased the Ang II-induced gene expression levels, suggesting that ERK activation has a role in control of expression of these genes. No such mechanism was detected in rat glomerulosa cells. Sar1-Ile4-Ile8-AngII, which can cause G protein-independent ERK activation, also stimulated the expression of CYP11B2 in H295R cells. These data suggest that the previously reported CAMK-mediated stimulation of early transcription factors NGFIB and Nurr1 has a predominant role in Ang II-induced CYP11B2 activation in rat adrenal glomerulosa cells, whereas in H295R cells ERK activation and G protein-independent mechanisms also contribute to this process.
MeSH term(s)	Active Transport, Cell Nucleus ; Adrenal Cortex/cytology ; Angiotensin II/pharmacology ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases ; Cell Line ; Cytochrome P-450 CYP11B2/genetics ; Extracellular Signal-Regulated MAP Kinases ; Gene Expression Profiling ; Gene Expression Regulation/drug effects ; Humans ; Rats ; Transcription Factors/genetics ; Zona Glomerulosa/cytology
Chemical Substances	Transcription Factors ; Angiotensin II (11128-99-7) ; Cytochrome P-450 CYP11B2 (EC 1.14.15.4) ; Calcium-Calmodulin-Dependent Protein Kinases (EC 2.7.11.17) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
Language	English
Publishing date	2009-03-24
Publishing country	Ireland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	187438-x
ISSN	1872-8057 ; 0303-7207
ISSN (online)	1872-8057
ISSN	0303-7207
DOI	10.1016/j.mce.2008.12.015
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Zs.A 1127: Show issues

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Article ; Online: The homolog of the five SH3-domain protein (HOFI/SH3PXD2B) regulates lamellipodia formation and cell spreading.

Lányi, Árpád / Baráth, Mónika / Péterfi, Zalán / Bogel, Gábor / Orient, Anna / Simon, Tünde / Petrovszki, Eniko / Kis-Tóth, Katalin / Sirokmány, Gábor / Rajnavölgyi, Éva / Terhorst, Cox / Buday, László / Geiszt, Miklós

PloS one

2011 Volume 6, Issue 8, Page(s) e23653

Abstract: Motility of normal and transformed cells within and across tissues requires specialized subcellular structures, e.g. membrane ruffles, lamellipodia and podosomes, which are generated by dynamic rearrangements of the actin cytoskeleton. Because the ... ...

Abstract	Motility of normal and transformed cells within and across tissues requires specialized subcellular structures, e.g. membrane ruffles, lamellipodia and podosomes, which are generated by dynamic rearrangements of the actin cytoskeleton. Because the formation of these sub-cellular structures is complex and relatively poorly understood, we evaluated the role of the adapter protein SH3PXD2B [HOFI, fad49, Tks4], which plays a role in the development of the eye, skeleton and adipose tissue. Surprisingly, we find that SH3PXD2B is requisite for the development of EGF-induced membrane ruffles and lamellipodia, as well as for efficient cellular attachment and spreading of HeLa cells. Furthermore, SH3PXD2B is present in a complex with the non-receptor protein tyrosine kinase Src, phosphorylated by Src, which is consistent with SH3PXD2B accumulating in Src-induced podosomes. Furthermore, SH3PXD2B closely follows the subcellular relocalization of cortactin to Src-induced podosomes, EGF-induced membrane ruffles and lamellipodia. Because SH3PXD2B also forms a complex with the C-terminal region of cortactin, we propose that SH3PXD2B is a scaffold protein that plays a key role in regulating the actin cytoskeleton via Src and cortactin.
MeSH term(s)	Actins/metabolism ; Adaptor Proteins, Signal Transducing/metabolism ; Cell Movement ; Cortactin/metabolism ; ErbB Receptors/metabolism ; Fibroblasts/cytology ; Fibroblasts/metabolism ; HeLa Cells ; Human Umbilical Vein Endothelial Cells/cytology ; Human Umbilical Vein Endothelial Cells/metabolism ; Humans ; Macrophages/cytology ; Macrophages/metabolism ; Phosphatidylinositols/metabolism ; Protein Binding ; Protein Transport ; Pseudopodia/metabolism ; Sequence Homology, Amino Acid ; src Homology Domains
Chemical Substances	Actins ; Adaptor Proteins, Signal Transducing ; CTTN protein, human ; Cortactin ; Phosphatidylinositols ; SH3PXD2B protein, human ; ErbB Receptors (EC 2.7.10.1)
Language	English
Publishing date	2011-08-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0023653
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Article ; Online: Molecular and functional characterization of Hv1 proton channel in human granulocytes.

Gábor L Petheo / Anna Orient / Mónika Baráth / István Kovács / Bence Réthi / Arpád Lányi / Anikó Rajki / Eva Rajnavölgyi / Miklós Geiszt

PLoS ONE, Vol 5, Iss 11, p e

2010 Volume 14081

Abstract	Voltage-gated proton current (I(Hv)) has been characterized in several cell types, but the majority of the data was collected in phagocytes, especially in human granulocytes. The prevailing view about the role of I(Hv) in phagocytes is that it is an essential supporter of the intense and sustained activity of Nox2 (the core enzyme of the phagocyte NADPH oxidase complex) during respiratory burst. Recently H(v)1, a voltage-gated proton channel, was cloned, and leukocytes from H(v)1 knockout mice display impaired respiratory burst. On the other hand, hardly anything is known about H(v)1 in human granulocytes. Using qPCR and a self made antibody, we detected a significant amount of H(v)1 in human eosinophil and neutrophil granulocytes and in PLB-985 leukemia cells. Using different crosslinking agents and detergents in reducing and non-reducing PAGE, significant expression of H(v)1 homodimers, but not that of higher-order multimers, could be detected in granulocytes. Results of subcellular fractionation and confocal imaging indicate that H(v)1 is resident in both plasmalemmal and granular membrane compartments of resting neutrophils. Furthermore, it is also demonstrated that H(v)1 accumulates in phagosome wall during zymosan engulfment together with, but independently of Nox2. During granulocytic differentiation early and parallel upregulation of H(v)1 and Nox2 expression was observed in PLB-985 cells. The upregulation of H(v)1 or Nox2 expression did not require the normal expression of the other molecule. Using RNA interference, we obtained strong correlation between H(v)1 expression and I(Hv) density in PLB-985 cells. It is also demonstrated that a massive reduction in H(v)1 expression can limit the Nox2 mediated superoxide production of PLB-985 granulocytes. In summary, beside monomers native H(v)1 forms stable proton channel dimer in resting and activated human granulocytes. The expression pattern of H(v)1 in granulocytes is optimized to support intense NADPH oxidase activity.
Keywords	Medicine ; R ; Science ; Q
Subject code	572
Language	English
Publishing date	2010-11-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Online: Detection of hydrogen peroxide by lactoperoxidase-mediated dityrosine formation.

Donkó, Agnes / Orient, Anna / Szabó, Pál T / Németh, Gábor / Vántus, Tibor / Kéri, György / Orfi, László / Hunyady, László / Buday, László / Geiszt, Miklós

Free radical research

2009 Volume 43, Issue 5, Page(s) 440–445

Abstract: The aim of this work was to study the dityrosine-forming activity of lactoperoxidase (LPO) and its potential application for measuring hydrogen peroxide (H2O2). It was observed that LPO was able to form dityrosine at low H2O2 concentrations. Since ... ...

Abstract	The aim of this work was to study the dityrosine-forming activity of lactoperoxidase (LPO) and its potential application for measuring hydrogen peroxide (H2O2). It was observed that LPO was able to form dityrosine at low H2O2 concentrations. Since dityrosine concentration could be measured in a simple fluorimetric reaction, this activity of the enzyme was utilized for the measurement of H2O2 production in different systems. These experiments successfully measured the activity of NADPH oxidase 4 (Nox4) by this method. It was concluded that LPO-mediated dityrosine formation offers a simple way for H2O2 measurement.
MeSH term(s)	Animals ; Cattle ; Cell Line ; Chromatography, High Pressure Liquid ; Fluorometry/methods ; Glucose/metabolism ; Glucose Oxidase/metabolism ; Humans ; Hydrogen Peroxide/analysis ; Hydrogen Peroxide/metabolism ; In Vitro Techniques ; Lactoperoxidase/isolation & purification ; Lactoperoxidase/metabolism ; Mass Spectrometry ; Milk/enzymology ; NADPH Oxidase 4 ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Reactive Oxygen Species/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Transfection ; Tyrosine/analogs & derivatives ; Tyrosine/biosynthesis
Chemical Substances	Reactive Oxygen Species ; Recombinant Proteins ; Tyrosine (42HK56048U) ; Hydrogen Peroxide (BBX060AN9V) ; dityrosine (CJ9XG8HS20) ; Glucose Oxidase (EC 1.1.3.4) ; Lactoperoxidase (EC 1.11.1.-) ; NADPH Oxidase 4 (EC 1.6.3.-) ; NADPH Oxidases (EC 1.6.3.-) ; NOX4 protein, human (EC 1.6.3.-) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2009-03-18
Publishing country	England
Document type	Evaluation Studies ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1194130-3
ISSN	1029-2470 ; 1071-5762
ISSN (online)	1029-2470
ISSN	1071-5762
DOI	10.1080/10715760902859069
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Zs.A 2236: Show issues

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Article ; Online: Peroxidasin is secreted and incorporated into the extracellular matrix of myofibroblasts and fibrotic kidney.

Péterfi, Zalán / Donkó, Agnes / Orient, Anna / Sum, Adrienn / Prókai, Agnes / Molnár, Beáta / Veréb, Zoltán / Rajnavölgyi, Eva / Kovács, Krisztina J / Müller, Veronika / Szabó, Attila J / Geiszt, Miklós

The American journal of pathology

2009 Volume 175, Issue 2, Page(s) 725–735

Abstract: Mammalian peroxidases are heme-containing enzymes that serve diverse biological roles, such as host defense and hormone biosynthesis. A mammalian homolog of Drosophila peroxidasin belongs to the peroxidase family; however, its function is currently ... ...

Abstract	Mammalian peroxidases are heme-containing enzymes that serve diverse biological roles, such as host defense and hormone biosynthesis. A mammalian homolog of Drosophila peroxidasin belongs to the peroxidase family; however, its function is currently unknown. In this study, we show that peroxidasin is present in the endoplasmic reticulum of human primary pulmonary and dermal fibroblasts, and the expression of this protein is increased during transforming growth factor-beta1-induced myofibroblast differentiation. Myofibroblasts secrete peroxidasin into the extracellular space where it becomes organized into a fibril-like network and colocalizes with fibronectin, thus helping to form the extracellular matrix. We also demonstrate that peroxidasin expression is increased in a murine model of kidney fibrosis and that peroxidasin localizes to the peritubular space in fibrotic kidneys. In addition, we show that this novel pathway of extracellular matrix formation is unlikely mediated by the peroxidase activity of the protein. Our data indicate that peroxidasin secretion represents a previously unknown pathway in extracellular matrix formation with a potentially important role in the physiological and pathological fibrogenic response.
MeSH term(s)	Animals ; COS Cells ; Chlorocebus aethiops ; Disease Models, Animal ; Extracellular Matrix/metabolism ; Extracellular Matrix Proteins/metabolism ; Fibroblasts/metabolism ; Fibrosis ; Humans ; Kidney/metabolism ; Kidney/pathology ; Mice ; Myoblasts/metabolism ; Peroxidase/metabolism ; Peroxidasin
Chemical Substances	Extracellular Matrix Proteins ; Peroxidase (EC 1.11.1.7)
Language	English
Publishing date	2009-07-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2943-9
ISSN	1525-2191 ; 0002-9440
ISSN (online)	1525-2191
ISSN	0002-9440
DOI	10.2353/ajpath.2009.080693
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Article ; Online: The homolog of the five SH3-domain protein (HOFI/SH3PXD2B) regulates lamellipodia formation and cell spreading.

Árpád Lányi / Mónika Baráth / Zalán Péterfi / Gábor Bogel / Anna Orient / Tünde Simon / Eniko Petrovszki / Katalin Kis-Tóth / Gábor Sirokmány / Éva Rajnavölgyi / Cox Terhorst / László Buday / Miklós Geiszt

PLoS ONE, Vol 6, Iss 8, p e

2011 Volume 23653

Abstract	Motility of normal and transformed cells within and across tissues requires specialized subcellular structures, e.g. membrane ruffles, lamellipodia and podosomes, which are generated by dynamic rearrangements of the actin cytoskeleton. Because the formation of these sub-cellular structures is complex and relatively poorly understood, we evaluated the role of the adapter protein SH3PXD2B [HOFI, fad49, Tks4], which plays a role in the development of the eye, skeleton and adipose tissue. Surprisingly, we find that SH3PXD2B is requisite for the development of EGF-induced membrane ruffles and lamellipodia, as well as for efficient cellular attachment and spreading of HeLa cells. Furthermore, SH3PXD2B is present in a complex with the non-receptor protein tyrosine kinase Src, phosphorylated by Src, which is consistent with SH3PXD2B accumulating in Src-induced podosomes. Furthermore, SH3PXD2B closely follows the subcellular relocalization of cortactin to Src-induced podosomes, EGF-induced membrane ruffles and lamellipodia. Because SH3PXD2B also forms a complex with the C-terminal region of cortactin, we propose that SH3PXD2B is a scaffold protein that plays a key role in regulating the actin cytoskeleton via Src and cortactin.
Keywords	Medicine ; R ; Science ; Q
Subject code	612
Language	English
Publishing date	2011-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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