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001-es BibID:	BIBFORM028890
Első szerző:	Lányi Árpád (biológus, immunológus)
Cím:	The homolog of the five SH3-domain protein (HOFI/SH3PXD2B) regulates lamellipodia formation and cell spreading / Lányi Á., Baráth M., Péterfi Z., Bogel G., Orient A., Simon T., Petrovszki E., Kis-Tóth K., Sirokmány G., Rajnavölgyi É., Terhorst C., Buday L., Geiszt M.
Dátum:	2011
ISSN:	1932-6203
Megjegyzések:	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.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk lamellipodia, podosome scaffold protein
Megjelenés:	PLoS One. - 6 : 8 (2011), p. e23653. -
További szerzők:	Baráth Mónika (1980-) (Phd hallgató) Péterfi Zalán Bogel Gábor Orient Anna Simon Tünde (1984-) (biokémikus, molekuláris biológus) Petrovszki Enikő Kis-Tóth Katalin (1975-) (immunológus) Sirokmány Gábor Rajnavölgyi Éva (1950-) (immunológus) Terhorst, Cox Buday László Geiszt Miklós
Pályázati támogatás:	TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Molekuláris immunológia
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat Szerző által megadott URL
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001-es BibID:	BIBFORM082984
035-os BibID:	(Cikkazonosító)14363 (WOS)000489011600008 (Scopus)85073077992
Első szerző:	Méhes Előd
Cím:	Enhanced endothelial motility and multicellular sprouting is mediated by the scaffold protein TKS4 / Elod Mehes, Monika Barath, Marton Gulyas, Edina Bugyik, Miklos Geiszt, Arpad Szoor, Arpad Lanyi, Andras Czirok
Dátum:	2019
ISSN:	2045-2322
Megjegyzések:	Endothelial cell motility has fundamental role in vasculogenesis and angiogenesis during developmental or pathological processes. Tks4 is a scaffold protein known to organize the cytoskeleton of lamellipodia and podosomes, and thus modulating cell motility and invasion. In particular, Tks4 is required for the localization and activity of membrane type 1-matrix metalloproteinase, a key factor for extracellular matrix (ECM) cleavage during cell migration. While its role in transformed cells is well established, little is known about the function of Tks4 under physiological conditions. In this study we examined the impact of Tks4 gene silencing on the functional activity of primary human umbilical vein endothelial cells (HUVEC) and used time-lapse videomicrosopy and quantitative image analysis to characterize cell motility phenotypes in culture. We demonstrate that the absence of Tks4 in endothelial cells leads to impaired ECM cleavage and decreased motility within a 3-dimensional ECM environment. Furthermore, absence of Tks4 also decreases the ability of HUVEC cells to form multicellular sprouts, a key requirement for angiogenesis. To establish the involvement of Tks4 in vascular development in vivo, we show that loss of Tks4 leads sparser vasculature in the fetal chorion in the Tks4-deficient 'nee' mouse strain.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk endothelial motility Tks4 podosome endothel sprouting
Megjelenés:	Scientific Reports. - 9 : 1 (2019), p. 1-13. -
További szerzők:	Baráth Mónika (1980-) (Phd hallgató) Gulyás Márton Bugyik Edina Geiszt Miklós Szöőr Árpád (1984-) (orvos) Lányi Árpád (1962-) (biológus, immunológus) Czirok András
Pályázati támogatás:	OTKA-109444 OTKA GINOP-2.3.2-15-2016-00050
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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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
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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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
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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