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1.

001-es BibID:BIBFORM036713
Első szerző:Bögel Gábor
Cím:Frank-ter Haar syndrome protein Tks4 regulates EGF-dependent cell migration / Gábor Böge, Annamária Gujdár, Miklós Geiszt, Árpád Lányi, Anna Fekete, Szabolcs Sipeki, Julian Downward, László Buday
Dátum:2012
ISSN:0021-9258
Megjegyzések:Mutations in the SH3PXD2B gene coding for the Tks4 protein are responsible for the autosomal-recessive Frank-ter Haar syndrome. Tks4, a substrate of Src tyrosine kinase is implicated in the regulation of podosome formation. Here, we report a novel role for Tks4 in the EGF signalling pathway. In EGF-treated cells, Tks4 is tyrosine phosphorylated and associated with the activated EGF receptor. This association is not direct but requires the presence of Src tyrosine kinase. In addition, treatment of cells with LY294002, an inhibitor of PI 3-kinase, or mutations of the PX domain reduces tyrosine phosphorylation and membrane translocation of Tks4. Furthermore, a PX domain mutant (R43W) Tks4 carrying a reported point mutation in a Frank-ter Haar syndrome patient showed aberrant intracellular expression and reduced phosphoinositide binding. Finally, silencing of Tks4 was shown to markedly inhibit HeLa cell migration in a Boyden chamber assay in response to EGF or serum. Our results therefore reveal a new function for Tks4 in the regulation of growth factor-dependent cell migration.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
EGF receptor
Tks4
cell migration
Frank-ter Haar syndrome
PX domain
Molekuláris Medicina
Megjelenés:Journal Of Biological Chemistry. - 287 : 37 (2012), p. 31321-31329. -
További szerzők:Gujdár Annamária Geiszt Miklós Lányi Árpád (1962-) (biológus, immunológus) Fekete Anna Sipeki Szabolcs Downward, Julian Buday László
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
A HOFI/SH3PXD2B aktin citoszkeletont szabályozó új adaptor fehérje funkcionális vizsgálata
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2.

001-es BibID:BIBFORM069283
035-os BibID:(Cikkazonosító)34280 (WOS)000385169900001 (Scopus)84990245095
Első szerző:Dülk, Metta
Cím:The scaffold protein Tks4 is required for the differentiation of mesenchymal stromal cells (MSCs) into adipogenic and osteogenic lineages / Dülk Metta, Kudlik Gyöngyi, Fekete Anna, Ernszt Dávid, Kvell Krisztián, Pongrácz Judit E., Merő Balázs L., Szeder Bálint, Radnai László, Geiszt Miklós, Csécsy Dalma E., Kovács Tamás, Uher Ferenc, Lányi Árpád, Vas Virag, Buday László
Dátum:2016
ISSN:2045-2322
Megjegyzések:The protein product of the SH3PXD2B gene is known as Tks4 (tyrosine kinase substrate with 4 SH3 domains)6,a scaffold protein. Upon phosphorylation by Src kinase, it has the ability to interact with signaling molecules toregulate the actin cytoskeleton7. Tks4 was also shown to play an important role in the formation of podosomes8,production of reactive oxygen species (ROS) by tumor cells9, and also involved in EGFR signaling10,11. Althoughwe have some knowledge of the possible function of Tks4, the detailed mechanism of how Tks4 impacts FTHSaffected tissues is less clear.Mesenchymal stromal cells (MSCs) as multipotent adult stem cells are able to form multiple cell types ofmesenchymal origin, e.g. adipocytes and osteoblasts12,13, therefore it is tempting to speculate that Tks4 may affectosteogenesis and lipogenesis of MSCs. Moreover, there are some hints for the possible role of Tks4 in MSC biology.For example, membrane type-1 matrix metalloproteinase (MT1-MMP), which is a binding partner of Tks4,is known to play a role in MSCs differentiation and trafficking14. Moreover, it has been described that Tks4 isinvolved in ROS production and ROS modulates several signaling pathways regulating MSC differentiation15.Therefore, we hypothesized that Tks4 may play a role in the process necessary for MSC differentiation and oneof the underlying mechanisms causing the FTHS phenotype could be the impaired stem cell functions of Tks4deficient MSCs.Here we present a novel Tks4?/? mouse strain on C57Bl/6 background with the complete loss of Tks4 protein.The adult Tks4 deficient mice have reduced fat tissue mass and altered craniofacial and skeletal bones. Wecompared the phenotype and differentiation potential of BM-MSCs (bone marrow mesenchymal stromal cells)isolated from Tks4?/? and wild type mice. Our data demonstrate that in the absence of Tks4, adipogenic and osteogenicdifferentiation of BM-MSCs is impaired; therefore, we concluded that Tks4 is necessary for the adipogenicand osteogenic mesenchymal differentiation pathways.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Tks4
adipogenesis
osteogenesis
mesenchymal differentiation
Megjelenés:Scientific Reports. - 6 : 1 (2016), p. 1-9. -
További szerzők:Kudlik Gyöngyi Fekete Anna Ernszt Dávid Kvell Krisztián Pongrácz Judit Merő Balázs L. Szeder Bálint Radnai László Geiszt Miklós Csécsy Dalma E. Kovács Tamás (Budapest) Uher Ferenc Lányi Árpád (1962-) (biológus, immunológus) Vas Virág Buday László
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Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM065616
Első szerző:Kovács István (Budapest)
Cím:Reactive oxygen species-mediated bacterial killing by B lymphocytes / István Kovács, Magdolna Horvath, Árpád Lányi, Gabor L. Petheő, Miklós Geiszt
Dátum:2015
ISSN:0741-5400
Megjegyzések:Regulated production of ROS is mainly attributed to Nox family enzymes. In neutrophil granulocytes and macrophages, Nox2 has a crucial role in bacterial killing, and the absence of phagocytic ROS production leads to the development of CGD. Expression of Nox2 was also described in B lymphocytes, where the role of the enzyme is still poorly understood. Here, we show that peritoneal B cells, which were shown recently to possess phagocytic activity, have a high capacity to produce ROS in a Nox2-dependent manner. In phagocytosing B cells, intense intraphagosomal ROS production is detected. Finally, by studying 2 animal models of CGD, we demonstrate that phagocyte oxidase-deficient B cells have a reduced capacity to kill bacteria. Our observations extend the number of immune cell types that produce ROS to kill pathogens.? Society for Leukocyte Biology.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
NADPH oxidase
Nox2
chronic granulomatous disease
p22phox
phagocytosis
Megjelenés:Journal Of Leukocyte Biology. - 97 : 6 (2015), p. 1133-1137. -
További szerzők:Horváth Magdolna Lányi Árpád (1962-) (biológus, immunológus) Petheő Gábor L. Geiszt Miklós
Pályázati támogatás:K106138
OTKA
K81676
OTKA
K109444
OTKA
OMFB-01680/2009
Egyéb
TÁMOP 4.2.2.A-11/1/KONV-2012-0023
Egyéb
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Intézményi repozitóriumban (DEA) tárolt változat
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4.

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
lamellipodia, podosome
scaffold protein
Megjelenés:PLoS One. - 6 : 8 (2011), p. e23653. -
További szerzők:Baráth Mónika 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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5.

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 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
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Intézményi repozitóriumban (DEA) tárolt változat
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6.

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, Isvan 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
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 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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