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1.

001-es BibID:BIBFORM004858
Első szerző:Bene László (biofizikus)
Cím:Detection of receptor trimers on the cell surface by flow cytometric fluorescence energy homotransfer measurements / László Bene, János Szöllősi, Gergely Szentesi, László Damjanovich, Rezső Gaspar, Thomas A. Waldmann, Sándor Damjanovich
Dátum:2005
ISSN:0006-3002
Megjegyzések:Fluorescence energy homotransfer offers a powerful tool for the investigation of the state of oligomerization of cell surface receptors on a cell-by-cell basis by measuring the polarized components of fluorescence intensity of cells labeled with fluorescently stained antibodies. Here we describe homotransfer-based methods for the flow cytometric detection and analysis of hetero- and homo-associations of cell surface receptors. Homotransfer efficiencies for two- and three-body energy transfer interactions are defined and their frequency distribution curves are computed from the fluorescence anisotropy distributions of multiple-labeled cells. The fractions of receptors involved in homo-clustering is calculated based on the dependence of the fluorescence anisotropy on the surface concentration of the fluorescently stained antibodies. A homotransfer analysis of the homo- and hetero-clustering of the MHCI and MHCII glycoproteins, the cytokine receptor IL-2Ralpha, transferrin receptor and the receptor-type tyrosine phosphatase CD45 on JY B and Kit-225-K6 T cells is presented. We investigated how various factors such as the type of dye, rotational mobility of the dye and dye-targeting antibody, as well as the wavelength of the exciting light affect the homotransfer. We show that the homotransfer technique combined with the high statistical resolution of flow cytometry is an effective tool for detecting different oligomeric states of receptors by using fluorophores having restricted rotational mobility on the time scale of fluorescence
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Fluorescence anisotropy
Receptor clustering
MHCI and MHCII glycoprotein
IL-2Rα
Transferrin receptor
CD45
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1744 : 2 (2005), p. 176-198. -
További szerzők:Szöllősi János (1953-) (biofizikus) Szentesi Gergely (1976-) (kémia-fizika tanár) Damjanovich László (1960-) (általános sebész) Gáspár Rezső (1944-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
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2.

001-es BibID:BIBFORM060604
035-os BibID:(scopus)0035871630 (wos)000170948300037
Első szerző:Gáspár Rezső (biofizikus)
Cím:Clustering of class I HLA oligomers with CD8 and TCR: three-dimensional models based on fluorescence resonance energy transfer and crystallographic data / Rezső Gáspár Jr., Péter Bagossi, László Bene, János Matkó, János Szöllősi, József Tőzsér, László Fésüs, Thomas A. Waldmann, Sándor Damjanovich
Dátum:2001
Megjegyzések:Fluorescence resonance energy transfer (FRET) data, in accordance with lateral mobility measurements, suggested the existence of class I HLA dimers and oligomers at the surface of live human cells, including the B lymphoblast cell line (JY) used in the present study. Intra- and intermolecular class I HLA epitope distances were measured on JY B cells by FRET using fluorophoreconjugated Ag-binding fragments of mAbs W6/32 and L368 directed against structurally well-characterized heavy and light chain epitopes, respectively. Out-of-plane location of these epitopes relative to the membrane-bound BODIPY-PC (2-(4,4-difluoro-5-(4- phenyl-1,3-butadienyl)-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycero-3-phosphocholine) was also determined by FRET. Computer-simulated docking of crystallographic structures of class I HLA and epitope-specific Ag-binding fragments, with experimentally determined interepitope and epitope to cell surface distances as constraints, revealed several sterically allowed and FRET-compatible class I HLA dimeric and tetrameric arrangements. Extension of the tetrameric class I HLA model with interacting TCR and CD8 resulted in a model of a supramolecular cluster that may exist physiologically and serve as a functionally significant unit for a network of CD8-HLA-I complexes providing enhanced signaling efficiency even at low MHC-peptide concentrations at the interface of effector and APCs.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal of immunology. - 166 : 8 (2001), p. 5078-5086. -
További szerzők:Bagossi Péter (1966-2011) (biokémikus, vegyész) Bene László (1963-) (biofizikus) Matkó János (1952-) (biológus) Szöllősi János (1953-) (biofizikus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Fésüs László (1947-) (orvos biokémikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
Pályázati támogatás:T029947
OTKA
F020590
OTKA
T019372
OTKA
T030399
OTKA
T023873
OTKA
T030411
OTKA
FKFP 327/2000
Egyéb
ETT T05/102/2000
Egyéb
FKFP 0518/99
Egyéb
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

3.

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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4.

001-es BibID:BIBFORM004736
Első szerző:Panyi György (biofizikus)
Cím:Colocalization and nonrandom distribution of Kv1.3 potassium channels and CD3 molecules in the plasma membrane of human T lymphocytes / Panyi, G., Bagdany, M., Bodnar, A., Vamosi, G., Szentesi, G., Jenei, A., Matyus, L., Varga, S., Waldmann, T. A., Gaspar, R., Damjanovich, S.
Dátum:2003
ISSN:027-8424 (Print)
Megjegyzések:Distribution and lateral organization of Kv1.3 potassium channels and CD3 molecules were studied by using electron microscopy, confocal laser scanning microscopy, and fluorescence resonance energy transfer. Immunogold labeling and electron microscopy showed that the distribution of FLAG epitope-tagged Kv1.3 channels (Kv1.3/FLAG) significantly differs from the stochastic Poisson distribution in the plasma membrane of human T lymphoma cells. Confocal laser scanning microscopy images showed that Kv1.3/FLAG channels and CD3 molecules accumulated in largely overlapping membrane areas. The numerical analysis of crosscorrelation of the spatial intensity distributions yielded a high correlation coefficient (C = 0.64). A different hierarchical level of molecular proximity between Kv1.3/FLAG and CD3 proteins was reported by a high fluorescence resonance energy transfer efficiency (E = 51%). These findings implicate that reciprocal regulation of ion-channel activity, membrane potential, and the function of receptor complexes may contribute to the proper functioning of the immunological synapse.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
Antigens, CD3
Biophysics
biosynthesis
Cell Membrane
Cells
chemistry
Electrophysiology
Energy Transfer
Epitopes
Fluorescence
Fluorescence Resonance Energy Transfer
Human
Humans
Hungary
Immunohistochemistry
immunology
Jurkat Cells
Kv1.3 Potassium Channel
Lymphocytes
Lymphoma
metabolism
Mice
Microscopy
Microscopy, Confocal
Microscopy, Electron
Models, Statistical
Potassium
Potassium Channels
Potassium Channels, Voltage-Gated
Proteins
Research
Support
T-Lymphocytes
Transfection
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 100 : 5 (2003), p. 2592-2597. -
További szerzők:Bagdány Miklós Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus) Szentesi Gergely (1976-) (kémia-fizika tanár) Jenei Attila (1966-) (biofizikus) Mátyus László (1956-) (biofizikus) Varga Sándor (1943-) (biofizikus) Waldmann, Thomas A. Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:DOI
elektronikus változat
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5.

001-es BibID:BIBFORM004884
Első szerző:Rubovszky Bálint (élettanász)
Cím:Detection of channel proximity by nanoparticle-assisted delaying of toxin binding : a combined patch-clamp and flow cytometric energy transfer study / Rubovszky, B., Hajdu, P., Krasznai, Z., Gaspar, R., Waldmann, T. A., Damjanovich, S., Bene, L.
Dátum:2005
ISSN:0175-7571
Megjegyzések:Gold nanoparticles of 30 nm diameter bound to cell-surface receptor major histocompatibility complex glycoproteins (MHCI and MHCII), interleukin-2 receptor alpha subunit (IL-2Ralpha), very late antigen-4 (VLA-4) integrin, transferrin receptor, and the receptor-type protein tyrosin phosphatase CD45 are shown by the patch-clamp technique to selectively modulate binding characteristics of Pi(2) toxin, an efficient blocker of K(v)1.3 channels. After correlating the electrophysiological data with those on the underlying receptor clusters obtained by simultaneously conducted flow cytometric energy transfer measurements, the modulation was proved to be sensitive to the density and size of the receptor clusters, and to the locations of the receptors as well. Based on the observation that engagement of MHCII by a monoclonal antibody down-regulates channel current and based on the close nanometer-scale proximity of the MHCI and MHCII glycoproteins, an analogous experiment was carried out when gold nanoparticles bound to MHCI delayed down-regulation of the K(v)1.3 current initiated by ligation of MHCII. Localization of K(v)1.3 channels in the nanometer-scale vicinity of the MHC-containing lipid rafts is demonstrated for the first time. A method is proposed for detecting receptor-channel or receptor-receptor proximity by observing nanoparticle-induced increase in relaxation times following concentration jumps of ligands binding to channels or to receptors capable of regulating channel currents.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Antibodies
Biophysics
Cell Line
chemistry
drug effects
Energy Transfer
Flow Cytometry
Glycoproteins
Gold
Human
Humans
Interleukin-2
Interleukin-2 Receptor alpha Subunit
Ion Channel Gating
Kv1.3 Potassium Channel
Ligands
Major Histocompatibility Complex
methods
Nanotubes
Particle Size
Patch-Clamp Techniques
pharmacokinetics
physiology
Potassium
Potassium Channels
Potassium Channels,Voltage-Gated
Protein Binding
Research
Scorpion Venoms
Support
T-Lymphocytes
Megjelenés:European Biophysics Journal. - 34 : 2 (2005), p. 127-143. -
További szerzők:Hajdu Péter (1975-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Bene László (1963-) (biofizikus)
Internet cím:elektronikus változat
DOI
Borító:

6.

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)
Internet cím:elektronikus változat
elektronikus változat
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