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001-es BibID:BIBFORM120484
035-os BibID:(Scopus)85105309592 (WoS)000646018700009
Első szerző:Petheő Gábor L.
Cím:Disruption of the NOX5 Gene Aggravates Atherosclerosis in Rabbits / Petheő Gábor L., Kerekes Andrea, Mihálffy Máté, Donkó Ágnes, Bodrogi Lilla, Skoda Gabriella, Baráth Mónika, Hoffmann Orsolya Ivett, Szeles Zsolt, Balázs Bernadett, Sirokmány Gábor, Fábián Júlia R., Tóth Zsuzsanna E., Baksa Ivett, Kacskovics Imre, Hunyady László, Hiripi László, Bősze Zsuzsanna, Geiszt Miklós
Dátum:2021
ISSN:0009-7330
Megjegyzések:Members of the NOX/DUOX family of NADPH oxidases are primarily responsible for the regulated production of reactive oxygen species (ROS), and the biological functions attributed to these enzymes are growing exponentially. Compared with other NOXes, our knowledge of NOX5 is minimal. NOX5 was first identified in testis and lymphoid tissues, but more recently, NOX5 was also detected in blood vessels. Our limited understanding of NOX5 function is largely due to its absence in rodents. The NOX5 gene is present in rabbits, and we could confirm its expression in testis, lymph nodes, and aorta. Therefore, we disrupted the NOX5 gene in New-Zealand White rabbits using the CRISPR/Cas9 technique. Since NOX enzymes have been implicated in the modulation of atherosclerosis in mice, we investigated the development of atherosclerosis induced by a cholesterol-rich diet. Significantly more plaques developed in the thoracic aortas of NOX5-deficient animals suggesting a protective role for NOX5 against atherosclerosis in young male rabbits.
Tárgyszavak:Orvostudományok Elméleti orvostudományok levél
folyóiratcikk
atherosclerosis
blood vessels
NADPH oxidase 5
rabbits
reactive oxygen species
Megjelenés:Circulation Research. - 128 : 9 (2021), p. 1320-1322. -
További szerzők:Kerekes Andrea Mihálffy Máté Donkó Ágnes Bodrogi Lilla Skoda Gabriella Baráth Mónika (1980-) (Phd hallgató) Hoffmann Orsolya I. Széles Zsolt Balázs Bernadett Sirokmány Gábor Fábián Júlia R. Tóth Zsuzsanna (1977-) (kardiológus) Baksa Ivett Kacskovics Imre Hunyady László Hiripi László Bősze Zsuzsanna Geiszt Miklós
Pályázati támogatás:NVKP_16-1-2016-0039
Egyéb
VEKOP-2.3.2-16-2016-00002
Egyéb
2020-4.1.1.-TKP2020
Egyéb
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2.

001-es BibID:BIBFORM014046
Első szerző:Petheő Gábor L.
Cím:Molecular and Functional Characterization of H(v)1 Proton Channel in Human Granulocytes / Petheo Gabor L., Anna Orient, Monika Barath, Istvan Kovacs, Bence Rethi, Arpad Lanyi, Aniko Rajki, Eva Rajnavolgyi, Miklos Geiszt
Dátum:2010
Megjegyzések: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.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Chronic Granulomatous-Disease
Phagocyte Respiratory Burst
Human-Neutrophilis
Superoxide-Production
Reactive Oxygen
Voltage Sensor
2 Pores
HV1
Conductance
Currents
Megjelenés:PloS One. - 5 : 11 (2010), p. e14081. -
További szerzők:Orient Anna Baráth Mónika (1980-) (Phd hallgató) Kovács István (Budapest) Réthi Bence (1973-) (biológus, immunológus) Lányi Árpád (1962-) (biológus, immunológus) Rajki Anikó Rajnavölgyi Éva (1950-) (immunológus) Geiszt Miklós
Pályázati támogatás:K 63700
OTKA
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Intézményi repozitóriumban (DEA) tárolt változat
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