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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:BIBFORM036993
Első szerző:Borbásné Sebestyén Veronika (biofizikus)
Cím:Membrane potential influences mobility, interactions and signaling of interleukin-2 and-15 receptors in T cells / Sebestyén Veronika, Nagy Éva, Mocsár Gábor, Papp Ferenc, Hajdú Péter, Panyi György, Tóth Katalin, Thomas A. Waldmann, Damjanovich Sándor, Bodnár Andrea, Vámosi György
Dátum:2011
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
MHC I
interleukin-2 receptor
IL-15 receptor
protein cluster
FRET
IL-2 signaling
Molekuláris Medicina
Molekuláris Medicina
Megjelenés:European Biophysics Journal with Biophysics Letters. - 40 : 1 (2011), p. 86. -
További szerzők:Nagy Éva (1980-) (molekuláris biológus) Mocsár Gábor (1981-) (biofizikus) Papp Ferenc (1979-) (biofizikus) Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Tóth Katalin Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:K77600
OTKA
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Receptor tirozin kinázok mint terápiás célpontok: működésük szabályozásának, és a közöttük fellépő molekuláris kölcsönhatások vizsgálata
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
K+ csatornák élettani szerepe az immunrendszer sejtjeiben
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM004940
Első szerző:Damjanovich Sándor (biofizikus)
Cím:Preassembly of interleukin 2 (IL-2) receptor subunits on resting Kit 225 K6 T cells and their modulation by IL-2, IL-7, and IL-15 : a fluorescence resonance energy transfer study / Damjanovich, S., Bene, L., Matko, J., Alileche, A., Goldman, C. K., Sharrow, S., Waldmann, T. A.
Dátum:1997
ISSN:0027-8424
Megjegyzések:Assembly and mutual proximities of alpha, beta, and gamma(c) subunits of the interleukin 2 receptors (IL-2R) in plasma membranes of Kit 225 K6 T lymphoma cells were investigated by fluorescence resonance energy transfer (FRET) using fluorescein isothiocyanate- and Cy3-conjugated monoclonal antibodies (mAbs) that were directed against the IL-2R alpha, IL-2R beta, and gamma(c) subunits of IL-2R. The cell-surface distribution of subunits was analyzed at the nanometer scale (2-10 nm) by FRET on a cell-by-cell basis. The cells were probed in resting phase and after coculture with saturating concentrations of IL-2, IL-7, and IL-15. FRET data from donor- and acceptor-labeled IL-2R beta-alpha, gamma-alpha, and gamma-beta pairs demonstrated close proximity of all subunits to each other in the plasma membrane of resting T cells. These mutual proximities do not appear to represent mAb-induced microaggregation, because FRET measurements with Fab fragments of the mAbs gave similar results. The relative proximities were meaningfully modulated by binding of IL-2, IL-7, and IL-15. Based on FRET analysis the topology of the three subunits at the surface of resting cells can be best described by a "triangular model" in the absence of added interleukins. IL-2 strengthens the bridges between the subunits, making the triangle more compact. IL-7 and IL-15 act in the opposite direction by opening the triangle possibly because they associate their private specific alpha receptors with the beta and/or gamma(c) subunits of the IL-2R complex. These data suggest that IL-2R subunits are already colocalized in resting T cells and do not require cytokine-induced redistribution. This colocalization is significantly modulated by binding of relevant interleukins in a cytokine-specific manner.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Adult
analysis
Cell Membrane
chemistry
Energy Transfer
Fluorescence
Human
Interleukin-15
Interleukin-2
Interleukin-7
metabolism
pharmacology
Protein Conformation
Receptors,Interleukin-2
T-Lymphocytes
Tumor Cells,Cultured
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 94 : 24 (1997), p. 13134-13139. -
További szerzők:Bene László (1963-) (biofizikus) Matkó János (1952-) (biológus) Alileche, Abdelkrim Goldman, Caroline K. Sharrow, Susan Waldmann, Thomas A.
Internet cím:elektronikus változat
elektronikus változat
Borító:

4.

001-es BibID:BIBFORM005177
Első szerző:de Bakker, Bärbel I.
Cím:Nanometer-scale organization of the alpha subunits of the receptors for IL2 and IL15 in human T lymphoma cells / de Bakker, B. I., Bodnar, A., van Dijk, E. M. H. P., Vamosi, G., Damjanovich, S., Waldmann, T. A., van Hulst, N. F., Jenei, A., Garcia-Parajo, M. F.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Cells
Human
Lymphoma
Biophysics
Hungary
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal of Cell Science. - 121 : 5 (2008), p. 627-633. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Dijk, Erik M. H. P., van Vámosi György (1967-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A. Hulst, Niek F., van Jenei Attila (1966-) (biofizikus) Garcia-Parajo, Maria F.
Internet cím:elektronikus változat
Intézményi repozitóriumban (DEA) tárolt változat
DOI
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5.

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
elektronikus változat
DOI
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6.

001-es BibID:BIBFORM005975
Első szerző:Edidin, Michael
Cím:Lateral diffusion measurements give evidence for association of the Tac peptide of the IL-2 receptor with the T27 peptide in the plasma membrane of HUT-102-B2 T cells / M. Edidin, A. Aszalos, S. Damjanovich, T.A. Waldmann
Dátum:1988
Megjegyzések:Fluorescence photobleaching recovery measurements show that the F1-IgG-labeled Tac peptide of the IL-2R can diffuse in the plane of the membrane of HUT-102-B2 T lymphocytes, with a mean diffusion coefficient of 2 to 3 x 10(-10) cm2s-1. Although only a fraction (mean 37%) of the Tac peptides is mobile on any given cell, lateral diffusion of the Tac peptide can be measured in 94% of cells examined. In contrast, the 95-kDa peptide, T27, is 90 to 100% immobilized in cells labeled with OKT27. Immobilization of T27 also affects the lateral diffusion of the Tac peptide, because the Tac peptide is immobile in more than 30% of cells pretreated with OKT27 and then labeled with anti-Tac IgG. The effect is specific for OKT27 to the extent that pretreatment with an anti-HLA mAb does not immobilize the Tac peptide. It appears, then, that Tac and T27 peptide not only are in proximity on HUT-102-B2 lymphocyte membranes but also interact physically in situ.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Antibodies,Monoclonal
Antigens,CD27
Antigens,Surface
Cell Line
Diffusion
Fluorescence
HLA Antigens
Human
immunology
Interleukin-2
Lymphocytes
Membrane Proteins
metabolism
Peptides
physiology
Receptors,Immunologic
Receptors,Interleukin-2
Support,U.S.Gov't,P.H.S.
T-Lymphocytes
Megjelenés:The Journal of Immunology. - 141 : 4 (1988), p. 1206-1210. -
További szerzők:Aszalos Adorján Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A.
Internet cím:elektronikus változat
Borító:

7.

001-es BibID:BIBFORM004706
Első szerző:Eicher, Donald M.
Cím:Oligomerization of IL-2Ralpha / Eicher, D. M., Damjanovich, S., Waldmann, T. A.
Dátum:2002
Megjegyzések:Interleukin (IL) 2 receptor subunit alpha (IL-2Ralpha) increases the affinity of the IL-2 receptor complex while hetero-association of IL-2Rbeta and gamma(c) chains initiates a proliferative signal. We show here that IL-2Ralpha is necessary for receptor clustering required for augmentation of IL-2 signalling. Cells expressing chimeras incorporating the extracellular domain of IL-2Ralpha demonstrated IL-2 independent homo-association of the IL-2Ralpha chimera. Singly or co-transfected IL-2Rbeta and gamma(c) chimeras showed no spontaneous or IL-2-inducible oligomerization. Co-transfection of IL-2Ralpha and IL-2Rbeta (plus minusgamma(c)) chimeras diminished spontaneous IL-2Ralpha chimera oligomerization and permitted IL-2-inducible hetero-oligomerization of receptor components. Homo-association of IL-2Ralpha was also demonstrated by fluorescence resonance energy transfer (FRET). The spontaneous homo-oligomerization property of IL-2Ralpha required the membrane proximal region of the receptor (exon 6) by deletion analysis; the IL-2 inducible oligomerization property of IL-2Ralpha required the second "sushi" domain (exon 4). This work provides insight into the mechanics of this complex receptor system and to other receptor complexes in the immune system that send signals by clustering receptor subunits
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Energy Transfer
Fluorescence
Megjelenés:Cytokine. - 17 : 2 (2002), p. 82-90. -
További szerzők:Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A.
Internet cím:elektronikus változat
DOI
Borító:

8.

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:

9.

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
Borító:

10.

001-es BibID:BIBFORM065104
035-os BibID:(WoS)000380371400013 (Scopus)84993661764
Első szerző:Mocsár Gábor (biofizikus)
Cím:MHC I expression regulates co-clustering and mobility of interleukin-2 and -15 receptors in T cells / G. Mocsár, J. Volkó, D. Rönnlund, J. Widengren, P. Nagy, J. Szöllősi, K. Tóth, C. K. Goldman, S. Damjanovich, T. A. Waldmann, A. Bodnár, G. Vámosi
Dátum:2016
ISSN:0006-3495
Megjegyzések:MHC glycoproteins form supramolecular clusters with interleukin-2 and -15 receptors in lipid rafts of T cells.The role of highly expressed MHC I in maintaining these clusters is unknown. We knocked down MHC I inFT7.10 human T cells, and studied protein clustering at two hierarchic levels: molecular aggregations andmobility by FRET and fluorescence correlation spectroscopy, and segregation into larger domains orsuperclusters by superresolution STED microscopy. FCS based molecular brightness analysis revealed thatthe studied molecules diffused as tight aggregates of several proteins of a kind. Knockdown reduced thenumber of MHC I containing molecular aggregates and their average MHC I content, and decreased theheteroassociation of MHC I with IL-2R?/IL-15R?. The mobility of not only MHC I but also that of IL-2R?/IL-15R? increased, corroborating the general size decrease of tight aggregates. A multifaceted analysis of STEDimages revealed that the diameter of MHC I superclusters diminished from 400-600 to 200-300 nm, whereasthose of IL-2R?/IL-15R? hardly changed. MHC I and IL-2R?/IL-15R? colocalized with GM1 gangliosiderichlipid rafts, but MHC I clusters retracted to smaller subsets of GM1- and IL-2R?/IL-15R?-rich areas uponknockdown. Our results prove that changes in expression level may significantly alter the organization andmobility of interacting membrane proteins.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biophysical Journal. - 111 : 1 (2016), p. 100-112. -
További szerzők:Volkó Julianna (1983-) (biotechnológus) Rönnlund, Daniel Widengren, Jerker Nagy Péter (1971-) (biofizikus) Szöllősi János (1953-) (biofizikus) Tóth Katalin (Heidelberg) Goldman, Caroline K. Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A. Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

11.

001-es BibID:BIBFORM075364
035-os BibID:(WoS)000432700300024 (Scopus)85046862526
Első szerző:Nagy Éva (molekuláris biológus)
Cím:Membrane Potential Distinctly Modulates Mobility and Signaling of IL-2 and IL-15 Receptors in T Cells / Éva Nagy, Gábor Mocsár, Veronika Sebestyén, Julianna Volkó, Ferenc Papp, Katalin Tóth, Sándor Damjanovich, György Panyi, Thomas A. Waldmann, Andrea Bodnár, György Vámosi
Dátum:2018
ISSN:0006-3495
Megjegyzések:The high electric ?eld across the plasma membrane might in?uence the conformation and behavior of transmembrane proteins that have uneven charge distributions in or near their transmembrane regions. Membrane depolarization of T cells occurs in the tumor microenvironment and in in?amed tissues because of K ? release from necrotic cells and hypoxia affecting the expression of K ? channels. However, little attention has been given to the effect of membrane potential (MP) changes on membrane receptor function. Therefore, we studied the in?uence of membrane de- and hyperpolarization on the biophysical properties and signaling of interleukin-2 (IL-2) and interleukin-15 (IL-15) receptors, which play important roles in T cell function. We investigated the mobility, clustering, and signaling of these receptors and major histocompatibility complex (MHC) I/II glycoproteins forming coclusters in lipid rafts of T cells. Depolarization by high K ? buffer or K channel blockers resulted in a decrease in the mobility of IL-2Ra and MHC glycoproteins, as shown by ?uorescence correlation spectroscopy, whereas hyperpolarization by the K ? ionophore valinomycin increased their mobility. Contrary to this, the mobility of IL-15Ra decreased upon both de- and hyperpolarization. These changes in protein mobility are not due to an alteration of membrane ?uidity, as evidenced by ?uorescence anisotropy measurements. Fo ? rster resonance energy transfer measurements showed that most homo- or heteroassociations of IL-2R, IL-15R, and MHC I did not change considerably, either. MP changes modulated signaling by the two cytokines in distinct ways: depolarization caused a signi?cant increase in the IL-2-induced phosphorylation of signal transducer and activator of transcription 5, whereas hyperpolarization evoked a decrease only in the IL-15-induced signal. Our data imply that the MP may be an important modulator of interleukin receptor signaling and dynamics. Enhanced IL-2 signaling in depolarized T reg ? cells highly expressing IL-2R may contribute to suppression of antitumor immune surveillance
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biophysical Journal. - 114 : 10 (2018), p. 2473-2482. -
További szerzők:Mocsár Gábor (1981-) (biofizikus) Borbásné Sebestyén Veronika (1990-) (biofizikus) Volkó Julianna (1983-) (biotechnológus) Papp Ferenc (1979-) (biofizikus) Tóth Katalin (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Panyi György (1966-) (biofizikus) Waldmann, Thomas A. Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00026
GINOP
GINOP-2.3.3-15-2016-00003
GINOP
GINOP-2.3.3-15-2016-00030
GINOP
K103965
OTKA
EFOP-3.6.1-16-2016-00022
EFOP
K119417
OTKA
TÁMOP-4.2.4.A/2-11/1-2012-0001
TÁMOP
EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
Internet cím:Szerző által megadott URL
DOI
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12.

001-es BibID:BIBFORM057902
Első szerző:Nizsalóczki Enikő
Cím:Distinct spatial relationship of the interleukin-9 receptor with interleukin-2 receptor and major histocompatibility complex glycoproteins in human T lymphoma cells / Enikő Nizsalóczki, István Csomós, Péter Nagy, Zsolt Fazekas, Carolyn K. Goldman, Thomas A. Waldmann, Sándor Damjanovich, György Vámosi, László Mátyus, Andrea Bodnár
Dátum:2014
ISSN:1439-4235
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
confocal microscopy
membrane proteins
FRET
protein protein interactions
receptors
Molekuláris Medicina
Doktori iskola
Megjelenés:Chemphyschem. - 15 : 18 (2014), p. 3969-3978. -
További szerzők:Csomós István (1983-) (molekuláris biológus) Nagy Péter (1971-) (biofizikus) Fazekas Zsolt (1971-) (biofizikus) Goldman, Caroline K. Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Sejtfelszíni fehérjék szerveződése: az MHC I. szerepe
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Molekuláris Orvostudomány Doktori Iskola
TÁMOP-4.2.2.A-11/1/KONV-2012-0023
TÁMOP
TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
TÁMOP-4.2.4.A/2-11/1-2012-0001
TÁMOP
CK 78179
OTKA
K 103965
OTKA
K 103906
OTKA
NK 101337
OTKA
Baross Gábor Program REG-EA-09-1-2009-0010
Egyéb
Internal Research Program of the University of Debrecen RH/885/2013
Egyéb
Intramural Research Program of the National Cancer Institute, National Institutes of Health
Egyéb
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DOI
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