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1.

001-es BibID:BIBFORM005175
Első szerző:Dóczy-Bodnár Andrea (biofizikus)
Cím:A biophysical approach to IL-2 and IL-15 receptor function : localization, conformation and interactions / Bodnar, A., Nizsaloczki, E., Mocsar, G., Szaloki, N., Waldmann, T. A., Damjanovich, S., Vamosi, G.
Dátum:2008
Megjegyzések:Interleukin-2 and interleukin-15 (IL-2, IL-15) are key participants in T and NK cell activation and function. Sharing the beta and gamma receptor subunits results in several common functions: e.g. the promotion of T cell proliferation. On the other hand, due to their distinct alpha receptor subunits, they also play opposing roles in immune processes such as activation induced cell death and immunological memory. Divergence of signaling pathways must ensue already at the plasma membrane where the cytokines interact with their receptors. Therefore understanding molecular details of receptor organization and mapping interactions with other membrane proteins that might influence receptor conformation and function, are of key importance. Biophysical/advanced microscopic methods (fluorescence resonance energy transfer (FRET), fluorescence crosscorrelation spectroscopy (FCCS), near-field scanning optical microscopy (NSOM), X-ray crystallography, surface plasmon resonance, NMR spectroscopy) have been instrumental in clarifying the details of receptor structure and organization from the atomic level to the assembly and dynamics of supramolecular clusters. In this short review some important contributions shaping our current view of IL-2 and IL-15 receptors are presented.
Tárgyszavak:Orvostudományok Elméleti orvostudományok Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Antibodies
Apoptosis
Biophysics
blood
Carcinoma
Cell Differentiation
Cell Fusion
Cell Line
Cell Membrane
Cell Proliferation
Cells
Complement
Confocal microscopy
Dendritic Cells
Diffusion
Energy Transfer
Epidermal Growth Factor
Fibroblasts
Fluorescence
Fluorescence correlation spectroscopy
Fluorescence Resonance Energy Transfer
FRET
Homeostasis
Human
Hungary
IL-2 and IL-15 receptors
In Vitro
Insulin
Interleukin-15
Interleukin-2
Kinetics
Lymphocytes
Lymphoma
Melanoma
Membrane Microdomains
Membrane Proteins
metabolism
methods
Mice
Microscopy
Near-field scanning optical microscopy
Phagocytosis
Phosphorylation
Photobleaching
Protein-protein interactions
Proteins
Receptor patterns
Research
Signal Transduction
Structure determination
Support
therapy
transmembrane signaling
Tyrosine
X-ray crystallography
Megjelenés:Immunology Letters. - 116 : 2 (2008), p. 117-125. -
További szerzők:Nizsalóczki Enikő Mocsár Gábor (1981-) (biofizikus) Szalóki Nikoletta (1981-) (biológus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Vámosi György (1967-) (biofizikus)
Internet cím:elektronikus változat
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DOI
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2.

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)
Internet cím:elektronikus változat
DOI
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3.

001-es BibID:BIBFORM016137
Első szerző:Mádi András (biológus)
Cím:Altered sialylation on the cell-surface proteins of dexamethasone-treated human macrophages contributes to augmented uptake of apoptotic neutrophils / András Mádi, Gyöngyike Majai, Cornelia Koy, György Vámosi, Attila Szántó, Michael O. Glocker, László Fésüs
Dátum:2011
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Molekuláris Medicina
Megjelenés:Immunology letters 135 : 1-2 (2011), p. 88-95. -
További szerzők:Majai Gyöngyike (1977-) (belgyógyász, immunológus) Koy, Cornelia Vámosi György (1967-) (biofizikus) Szántó Attila (1976-) (orvos, biokémikus) Glocker, Michael O. Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Fehérje-fehérje kölcsönhatások limfociták membránjában és a sejtmagban
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
elektronikus változat
DOI
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4.

001-es BibID:BIBFORM005107
Első szerző:Vámosi György (biofizikus)
Cím:The role of supramolecular protein complexes and membrane potential in transmembrane signaling processes of lymphocytes / Vamosi, G., Bodnar, A., Damjanovich, S., Nagy, P., Varga, Z., Damjanovich, L.
Dátum:2006
ISSN:165-2478 (Print)
Megjegyzések:The formation of protein patterns in lymphocyte plasma membranes is analyzed in the light of past and, also, very recent experiments. The analysis surveys the lateral organization of major histocompatibility complex glycoproteins, intercellular adhesion molecule-1, interleukin-2 and -15 receptors, Kv1.3 K+ ion channels and the T-cell receptor as well as their behavior under different conditions. These molecules form small- and large-scale clusters in the membrane of human lymphocytes. Many of the association motifs occur in other investigated cell types. The conclusions point toward a possible role for ion channel activities, membrane potential changes and alterations of the lateral organization of proteins in transmembrane signaling and cytotoxic interactions. In our outlook new factors that potentially affect membrane protein cluster formation and interactions are discussed. A role for MHC glycoproteins in concentrating membrane proteins and organizing protein patterns is suggested, and the possibility that the membrane potential may modulate protein conformation and, thereby, affect protein-protein interactions is pointed out. A well-defined role for the presence of ion channels in the immune synapse is offered, which could explain the significance of ion channel accumulation in the immune synapse together with the T-cell receptor.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
Biophysics
Cell Membrane
Glycoproteins
Human
Humans
Hungary
immunology
Intercellular Adhesion Molecule-1
Interleukin-2
Ion Channels
Light
Lymphocytes
Major Histocompatibility Complex
Membrane Potentials
Membrane Proteins
metabolism
Multiprotein Complexes
physiology
Protein Conformation
Proteins
Research
Signal Transduction
Support
T-Lymphocytes
Megjelenés:Immunology Letters. - 104 : 1-2 (2006), p. 53-58. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Nagy Péter (1971-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító) Damjanovich László (1960-) (általános sebész)
Internet cím:DOI
elektronikus változat
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