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1.

001-es BibID:BIBFORM004854
Első szerző:Andrásfalvy Márton
Cím:The beta subunit of the type I Fcepsilon receptor is a target for peptides inhibiting IgE-mediated secretory response of mast cells / Andrasfalvy, M., Peterfy, H., Toth, G., Matko, J., Abramson, J., Kerekes, K., Vamosi, G., Pecht, I., Erdei, A.
Dátum:2005
ISSN:0022-1767
Megjegyzések:Peptides originally derived from complement component C3a were earlier shown to inhibit the type I FcepsilonR (FcepsilonRI)-mediated degranulation of mucosal type mast cells. In the present study, we show that C3a7, a peptide with a natural sequence, and its modified derivative, C3a9, are powerful inhibitors of the above response of both serosal and mucosal type mastocytes. We demonstrate that these peptides inhibit FcepsilonRI-induced membrane proximal events, suppress phosphorylation of the FcepsilonRI beta subunit, the protein tyrosine kinase Lyn, as well as the transient rise in free cytosolic Ca2+ level. The late phase of cellular response was also inhibited, as demonstrated by the reduced TNF-alpha secretion. Experiments using two independent methods provided evidence that the interaction site of complement-derived peptides is the FcepsilonRI beta-chain. This was further supported by fluorescence confocal microscopic colocalization and resonance energy transfer measurements. Taken together, these results suggest the presence of distinct "activating" and "inhibitory" motifs in the C3a sequence. Response to both is in balance under physiologic conditions. Furthermore, present data predict that such inhibitory peptides may serve as potent agents for future therapeutic intervention.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
1-Phosphatidylinositol 3-Kinase
Animals
antagonists & inhibitors
Calcium
Cells
chemistry
Complement
Complement C3a
Energy Transfer
Fluorescence
Hungary
Immunoglobulin E
immunology
Mast Cells
metabolism
methods
Mice
Mice,Inbred BALB C
Necrosis
Oligopeptides
Peptides
pharmacology
Phosphorylation
physiology
Protein Subunits
Receptors,IgE
Research
secretion
Support
Tumor Necrosis Factor-alpha
Tyrosine
Megjelenés:The Journal of Immunology. - 175 : 5 (2005), p. 2801-2806. -
További szerzők:Péterfy Hajna Tóth Gábor (Szeged) Matkó János (1952-) (biológus) Abramson, Jakub Kerekes Krisztina Vámosi György (1967-) (biofizikus) Pecht, Israel Erdei Anna
Internet cím:elektronikus változat
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2.

001-es BibID:BIBFORM013246
Első szerző:Beck Zoltán (molekuláris biológus, mikrobiológus)
Cím:New cholesterol-specific antibodies remodel HIV-1 target cells' surface and inhibit their in vitro virus production / Zoltán Beck, Andrea Balogh, Andrea Kis, Emese Izsépi, László Cervenak, Glória László, Adrienn Bíró, Károly Liliom, Gábor Mocsár, György Vámosi, George Füst, Janos Matko
Dátum:2010
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Lipid Research. - 51 : 2 (2010), p. 286-296. -
További szerzők:Balogh Andrea Kis Andrea (1981-) (molekuláris biológus, mikrobiológus) Izsépi Emese Cervenak László László Glória Bíró Adrienn Liliom Károly Mocsár Gábor (1981-) (biofizikus) Vámosi György (1967-) (biofizikus) Füst György (Budapest) Matkó János (1952-) (biológus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
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3.

001-es BibID:BIBFORM004836
Első szerző:Gombos Imre
Cím:Rafting MHC-II domains in the APC (presynaptic) plasma membrane and the thresholds for T-cell activation and immunological synapse formation / Gombos, I., Detre, C., Vamosi, G., Matko, J.
Dátum:2004
Megjegyzések:Glycosphingolipid- and cholesterol-rich membrane microdomains (rafts) in T-cells are important in triggering and regulation of T(H)-cell activation in immunological synapses (IS), which in turn may control the T-cell repertoire in lymph nodes and at the periphery. It is less known, however, how the "presynaptic side" controls formation and function of IS. We investigated here activation signals and synapse formation frequency of murine IP12-7 T(H) hybridoma cell specific to influenza virus HA-peptide upon stimulation with two B-lymphoma cells, A20 and 2PK3, pulsed with peptide antigen. Confocal microscopic colocalization and FRET data consonantly revealed clustered distribution and constitutive raft-association of a major fraction of MHC-II molecules in both APCs. Costimulatory molecules (CD80 and CD86), not associated constitutively with rafts, were expressed at much lower level in A20 cells. T-cells responded to 2PK3 APC with much higher signal strength than to A20 cells, in good correlation with the frequency of IS formation, as assessed by microscopic conjugation assay. Disruption of rafts by cholesterol depletion in 2PK3 cells largely decreased the magnitude of T(H) cell activation signals, especially at low peptide antigen doses, similarly to masking CD4 with mAb on T-cells. The frequency of IS formation was reduced by blocking LFA-1 on T-cells and CD80 on APCs, by lowering the temperature below the phase transition of the membrane or by disrupting actin cytoskeleton. These data together suggest that the surface density and affinity/stability of peptide-MHC-II complexes and the costimulatory level are primary determinants for an efficient TCR recognition and the strength of the subsequent T-cell signals, as well as of the IS formation, which additionally requires a cytoskeleton-dependent remodeling of APC surface after the initial TCR signal. The threshold of T-cell activation can be further set by rafting MHC-II domains via concentrating high affinity ligands and promoting thereby T-cells for sensing low density antigen. Our data also demonstrate that B-cells, similarly to dendritic cells, could also provide T-cells with antigen-independent weak survival signals, likely associated with integrin engagement.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animals
Antigen-Presenting Cells
Antigens
Cell Membrane
Cells
Cholesterol
Cytoskeleton
Dendritic Cells
Histocompatibility Antigens
Histocompatibility Antigens Class II
Hungary
immunology
Ligands
Lymph Nodes
Lymphocyte Activation
Lymphoma,B-Cell
Membrane Microdomains
Mice
Peptide Fragments
Research
Support
Synapses
T-Lymphocytes
Temperature
Time Factors
Tumor Cells,Cultured
ultrastructure
Megjelenés:Immunology Letters. - 92 : 1-2 (2004), p. 117-124. -
További szerzők:Detre, Cynthia Vámosi György (1967-) (biofizikus) Matkó János (1952-) (biológus)
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DOI
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4.

001-es BibID:BIBFORM005182
Első szerző:Gombos Imre
Cím:Some new faces of membrane microdomains : a complex confocal fluorescence, differential polarization, and FCS imaging study on live immune cells / Gombos, I., Steinbach, G., Pomozi, I., Balogh, A., Vamosi, G., Gansen, A., Laszlo, G., Garab, G., Matko, J.
Dátum:2008
ISSN:552-4930 (Electronic)
Megjegyzések:Lipid rafts are cholesterol- and glycosphingolipid-rich plasma membrane microdomains, which control signal transduction, cellular contacts, pathogen recognition, and internalization processes. Their stability/lifetime, heterogeneity remained still controversial, mostly due to the high diversity of raft markers and cellular models. The correspondence of the rafts of living cells to liquid ordered (Lo) domains of model membranes and the effect of modulating rafts on the structural dynamics of their bulk membrane environment are also yet unresolved questions. Spatial overlap of various lipid and protein raft markers on live cells was studied by confocal laser scanning microscopy, while fluorescence polarization of DiIC18(3) and Bodipy-phosphatidylcholine was imaged with differential polarization CLSM (DP-CLSM). Mobility of the diI probe under different conditions was assessed by fluorescence correlation spectroscopic (FCS). GM1 gangliosides highly colocalized with GPI-linked protein markers of rafts and a new anti-cholesterol antibody (AC8) in various immune cells. On the same cells, albeit not fully excluded from rafts, diI colocalized much less with raft markers of both lipid and protein nature, suggesting the Lo membrane regions are not equivalents to lipid rafts. The DP-CLSM technique was capable of imaging probe orientation and heterogeneity of polarization in the plasma membrane of live cells, reflecting differences in lipid order/packing. This property--in accordance with diI mobility assessed by FCS--was sensitive to modulation of rafts either through their lipids or proteins. Our complex imaging analysis demonstrated that two lipid probes--G(M1) and a new anti-cholesterol antibody--equivocally label the membrane rafts on a variety of cell types, while some raft-associated proteins (MHC-II, CD48, CD59, or CD90) do not colocalize with each other. This indicates the compositional heterogeneity of rafts. Usefulness of the DP-CLSM technique in imaging immune cell surface, in terms of lipid order/packing heterogeneities, was also shown together with its sensitivity to monitor biological modulation of lipid rafts.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
Antibodies
article
Cell Line,Tumor
Cells
Cells,Cultured
chemistry
Cholesterol
Comparative Study
Confocal
Fluorescence
Fluorescence Polarization
Humans
Hungary
immunology
Lipids
Membrane Microdomains
methods
Mice
Mice, Inbred BALB C
Mice, Inbred C3H
Microscopy
Microscopy, Confocal
Microscopy, Fluorescence
Microscopy, Polarization
Proteins
Rats
Rats, Sprague-Dawley
Research
Research Support
Signal Transduction
Spectrometry, Fluorescence
Support
Megjelenés:Cytometry. Part A. - 73 : 3 (2008), p. 220-229. -
További szerzők:Steinbach Gábor Pomozi István Balogh Andrea Vámosi György (1967-) (biofizikus) Gansen, Alexander László Glória Garab Győző Matkó János (1952-) (biológus)
Internet cím:DOI
elektronikus változat
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5.

001-es BibID:BIBFORM039514
Első szerző:Matkó János (biológus)
Cím:GPI-microdomains (membrane rafts) and signaling of the multi-chain interleukin-2 receptor in human lymphoma/leukemia T cell lines / Matko, J., Bodnar, A., Vereb, G., Bene, L., Vamosi, G., Szentesi, G., Szollosi, J., Gaspar, R., Horejsi, V., Waldmann, T. A., Damjanovich, S.
Dátum:2002
ISSN:0014-2956
Megjegyzések:Subunits (alpha, beta and gamma) of the interleukin-2 receptor complex (IL-2R) are involved in both proliferative and activation-induced cell death (AICD) signaling of T cells. In addition, the signaling beta and gamma chains are shared by other cytokines (e.g. IL-7, IL-9, IL-15). However, the molecular mechanisms responsible for recruiting/sorting the alpha chains to the signaling chains at the cell surface are not clear. Here we show, in four cell lines of human adult T cell lymphoma/leukemia origin, that the three IL-2R subunits are compartmented together with HLA glycoproteins and CD48 molecules in the plasma membrane, by means of fluorescence resonance energy transfer (FRET), confocal microscopy and immuno-biochemical techniques. In addition to the beta and gamma(c) chains constitutively expressed in detergent-resistant membrane fractions (DRMs) of T cells, IL-2Ralpha (CD25) was also found in DRMs, independently of its ligand-occupation. Association of CD25 with rafts was also confirmed by its colocalization with GM-1 ganglioside. Depletion of membrane cholesterol using methyl-beta-cyclodextrin substantially reduced co-clustering of CD25 with CD48 and HLA-DR, as well as the IL-2 stimulated tyrosine-phosphorylation of STATs (signal transducer and activator of transcription). These data indicate a GPI-microdomain (raft)-assisted recruitment of CD25 to the vicinity of the signaling beta and gamma(c) chains. Rafts may promote rapid formation of a high affinity IL-2R complex, even at low levels of IL-2 stimulus, and may also form a platform for the regulation of IL-2 induced signals by GPI-proteins (e.g. CD48). Based on these data, the integrity of these GPI-microdomains seems critical in signal transduction through the IL-2R complex.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:European Journal Of Biochemistry. - 269 : 4 (2002), p. 1199-1208. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Bene László (1963-) (biofizikus) Vámosi György (1967-) (biofizikus) Szentesi Gergely (1976-) (kémia-fizika tanár) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Horejsi, Václav Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:BIBFORM086418
Első szerző:Péterfy Hajna
Cím:The β subunit of the type I Fce receptor is a target for complement-derived peptides inhibiting IgE-mediated secretory response of mast cells / Peterfy H., Andrasfalvy M., Toth G., Matkó J., Abramson J., Vámosi G., Pecht I., Erdei A.
Dátum:2005
ISSN:1742-464X
Tárgyszavak:Orvostudományok Klinikai orvostudományok idézhető absztrakt
folyóiratcikk
Megjelenés:Febs Journal. - 272 : Suppl1 (2005), p. 286-287. -
További szerzők:Andrásfalvy Márton Tóth G. Matkó János (1952-) (biológus) Abramson, Jakub Vámosi György (1967-) (biofizikus) Pecht, Israel Erdei A.
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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7.

001-es BibID:BIBFORM004673
Első szerző:Vereb György (biofizikus, orvos)
Cím:Cholesterol-dependent clustering of IL-2Ralpha and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts / Vereb, G., Matko, J., Vamosi, G., Ibrahim, S. M., Magyar, E., Varga, S., Szollosi, J., Jenei, A., Gaspar, R., Waldmann, T. A., Damjanovich, S.
Dátum:2000
Megjegyzések:Immunogold staining and electron microscopy show that IL-2 receptor alpha-subunits exhibit nonrandom surface distribution on human T lymphoma cells. Analysis of interparticle distances reveals that this clustering on the scale of a few hundred nanometers is independent of the presence of IL-2 and of the expression of the IL-2R beta-subunit. Clustering of IL-2Ralpha is confirmed by confocal microscopy, yielding the same average cluster size, approximately 600-800 nm, as electron microscopy. HLA class I and II and CD48 molecules also form clusters of the same size. Disruption of cholesterol-rich lipid rafts with filipin or depletion of membrane cholesterol with methyl-beta-cyclodextrin results in the blurring of cluster boundaries and an apparent dispersion of clusters for all four proteins. Interestingly, the transferrin receptor, which is thought to be located outside lipid rafts, exhibits clusters that are only 300 nm in size and are less affected by modifying the membrane cholesterol content. Furthermore, transferrin receptor clusters hardly colocalize with IL-2Ralpha, HLA, and CD48 molecules (crosscorrelation coefficient is 0.05), whereas IL-2Ralpha colocalizes with both HLA and CD48 (crosscorrelation coefficient is between 0.37 and 0.46). This coclustering is confirmed by electron microscopy. The submicron clusters of IL-2Ralpha chains and their coclustering with HLA and CD48, presumably associated with lipid rafts, could underlie the efficiency of signaling in lymphoid cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
analysis
Antigens,CD
Biophysics
Cells
Cholesterol
HLA Antigens
Human
Hungary
Immunohistochemistry
Interleukin-2
Lymphoma
Lymphoma,T-Cell
Membrane Fluidity
Membrane Lipids
metabolism
Microscopy
Microscopy,Confocal
Microscopy,Immunoelectron
Neoplasm Proteins
pathology
physiology
Proteins
Receptors,Interleukin-2
Support,Non-U.S.Gov't
T-Lymphocytes
Tumor Cells,Cultured
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 97 : 11 (2000), p. 6013-6018. -
További szerzők:Matkó János (1952-) (biológus) Vámosi György (1967-) (biofizikus) Ibrahim, Shehu M. Magyar Erika Varga Sándor (1943-) (biofizikus) Szöllősi János (1953-) (biofizikus) Jenei Attila (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
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elektronikus változat
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