CCL

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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:BIBFORM006027
Első szerző:Bene László (biofizikus)
Cím:Lateral organization of the ICAM-1 molecule at the surface of human lymphoblasts : a possible model for its co-distribution with the IL-2 receptor, class I and class II HLA molecules / Bene L., Balázs M., Matkó J., Möst J., Dierich M. P., Szöllösi J., Damjanovich S.
Dátum:1994
Megjegyzések:Lateral distribution of the ICAM-1 molecule and its topological relationship (mutual proximity) to the heavy and light chains of class I HLA molecules, HLA-DR and interleukin-2 receptor alpha-chain (IL-2R alpha) were studied in the plasma membrane of HUT-102B2 T and JY B lymphoblastoid cell lines by the technique of flow cytometric energy transfer (FCET). Effects of adherency and treatments with recombinant interferon-gamma or tumor necrosis factor-alpha on the relative expression level of ICAM-1 to the above cell surface proteins were also investigated. While the cytokines did not significantly affect the ICAM-1 level of either cell line, an increased ICAM-1 expression was found on adherent JY cells. The ICAM-1 expression varied significantly with the cell cycle and culture conditions, as well. The statistical analysis of the differences observed in the energy transfer efficiency histograms resulted in a possible model of lateral co-distribution of these proteins in the plasma membrane. These two-dimensional patterns proved to be different for T and B lymphoma lines. ICAM-1 molecules showed a high degree of self-association on HUT-102B2 (T) cells, while they were mainly expressed as monomers on the surface of JY (B) cells. Both cells showed a significant (ca. 30%) difference between densities of the heavy and light chains of class I HLA antigen, suggesting a substantial amount of beta 2-microglobulin free heavy chains on these cell lines. The class I HLA molecules also showed partial self-association, but on both cell lines. The beta 2-microglobulin and the heavy chain of the class I HLA showed strongly different proximities to the IL-2R alpha, HLA-DR and ICAM-1 molecules, indicating that their orientations relative to the other proteins are dissimilar. IL-2R alpha molecules of the HUT-102B2 (T) cells are located mostly in the vicinity of the beta 2-microglobulin. In contrast, the local density of HLA-DR antigens is higher in the proximity of the heavy chain than in the vicinity of the beta 2-microglobulin. The possible functional significance of these protein patterns is also discussed herein.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Antibodies,Monoclonal
B-Lymphocyte Subsets
beta 2-Microglobulin
Cell Adhesion
Cell Adhesion Molecules
Cell Cycle
Cell Line
Energy Transfer
Flow Cytometry
Histocompatibility Antigens Class I
HLA Antigens
HLA-D Antigens
HLA-DR Antigens
Human
Hungary
immunology
Intercellular Adhesion Molecule-1
Interferon Type II
Interleukin-2
Light
physiology
Receptors,Interleukin-2
Support,Non-U.S.Gov't
Support,U.S.Gov't,Non-P.H.S.
T-Lymphocyte Subsets
Tumor Necrosis Factor
Megjelenés:European Journal of Immunology. - 24 : 9 (1994), p. 2115-2123. -
További szerzők:Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Matkó János (1952-) (biológus) Most, J. Dierich, Manfred P. Szöllősi János (1953-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:DOI
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3.

001-es BibID:BIBFORM005968
035-os BibID:(scopus)0023260317
Első szerző:Damjanovich Sándor (biofizikus)
Cím:Cyclosporin depolarizes human lymphocytes : earliest observed effect on cell metabolism / S. Damjanovich, A. Aszalos, S. A. Mulhern, J. Szollosi, M. Balazs, L. Tron, M. J. Fulwyler
Dátum:1987
Megjegyzések:Cyclosporin A (CsA) produced dose-dependent membrane depolarization of human peripheral blood lymphocytes. The phenomenon was investigated applying the membrane potential probe dihexyloxacarbocyanine iodide in a flow cytometer in combination with ionophores, hormones and monoclonal antibodies binding to different subclasses of lymphocytes and the anti-interleukin 2 receptor antibody. Human interferon-gamma abolished the depolarizing effect of cyclosporin on lymphocytes. Interleukin 2 caused depolarization and also enhanced the effect of CsA. OKT4 and OKT8 monoclonal antibodies slightly hindered depolarization by CsA while OKT3, OKT11 and OKIa1 antibodies had no such effect. Valinomycin decreased CsA's effect on the membrane potential while the ionophore A-23187 and ionomycin caused depolarizations that were additive with CsA's. CsA treatment released the isotope from 42K-loaded human lymphocytes in a dose-dependent fashion. CsA addition increased intracellular calcium content. CsA decreased the motional freedom of a spin probe in the membrane, but did not hinder the binding of fluoresceinated antibodies to the cell surface. These results suggest immediate alteration in membrane structure upon CsA treatment, causing potassium leakage and calcium ion uptake. These are the earliest detected effects of CsA on cells so far.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Antibodies,Monoclonal
blood
Calcium
Carbocyanines
Cell Membrane
classification
Cyclosporins
Cytoplasm
Dimethyl Sulfoxide
drug effects
Electron Spin Resonance Spectroscopy
Flow Cytometry
Human
immunology
Interferon Type II
Interleukin-2
Intracellular Membranes
Ion Channels
Ionomycin
Ionophores
Lymphocytes
Membrane Fluidity
Membrane Potentials
metabolism
methods
pharmacology
Potassium
Potassium Radioisotopes
Spectrometry,Fluorescence
ultrastructure
Valinomycin
Megjelenés:European Journal of Immunology. - 17 : 6 (1987), p. 763-768. -
További szerzők:Aszalos Adorján Mulhern, Sally Szöllősi János (1953-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Trón Lajos (1941-) (biofizikus) Fulwyler, Mack J.
Internet cím:elektronikus változat
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4.

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:

5.

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:

6.

001-es BibID:BIBFORM057538
035-os BibID:(scopus)84910122146 (wos)000345023400059
Első szerző:Govers, Coen
Cím:TCRs genetically linked to CD28 and CD3[epszilon] do not mispair with endogenous TCR chains and mediate enhanced t cell persistence and anti-melanoma activity / Coen Govers, Zsolt Sebestyén, János Roszik, Mandy van Brakel, Cor Berrevoets, Árpád Szöőr, Konstantina Panoutsopoulou, Marieke Broertjes, Tan Van, György Vereb, János Szöllősi, Reno Debets
Dátum:2014
ISSN:0022-1767 1550-6606
Megjegyzések:Adoptive transfer of T cells that are gene engineered to express a defined TCR represents a feasible and promising therapy for patients with tumors. However, TCR gene therapy is hindered by the transient presence and effectiveness of transferred T cells, which are anticipated to be improved by adequate T cell costimulation. In this article, we report the identification and characterization of a novel two-chain TCR linked to CD28 and CD3[epszilon] (i.e., TCR:28[epszilon]). This modified TCR demonstrates enhanced binding of peptide-MHC and mediates enhanced T cell function following stimulation with peptide compared with wild-type TCR. Surface expression of TCR:28[epszilon] depends on the transmembrane domain of CD28, whereas T cell functions depend on the intracellular domains of both CD28 and CD3[epszilon], with IL-2 production showing dependency on CD28:LCK binding. TCR:28[epszilon], but not wild-type TCR, induces detectable immune synapses in primary human T cells, and such immune synapses show significantly enhanced accumulation of TCR transgenes and markers of early TCR signaling, such as phosphorylated LCK and ERK. Importantly, TCR:28[epszilon] does not show signs of off-target recognition, as evidenced by lack of TCR mispairing, as well as preserved specificity. Notably, when testing TCR:28[epszilon] in immune-competent mice, we observed a drastic increase in T cell survival, which was accompanied by regression of large melanomas with limited recurrence. Our data argue that TCR transgenes that contain CD28, and, thereby, may provide T cell costimulation in an immune-suppressive environment, represent candidate receptors to treat patients with tumors.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
TCR
T Cell
Megjelenés:Journal Of Immunology. - 193 : 10 (2014), p. 5315-5326. -
További szerzők:Sebestyén Zsolt Roszik János (1979-) (biofizikus) van Brakel, Mandy Berrevoets, Cor Szöőr Árpád (1984-) (orvos) Panoutsopoulou, Konstantina Broertjes, Marieke Van, Tan Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus) Debets, Reno
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
TÁMOP-4.2.2/B-10/1/2010-0024
TÁMOP
TÁMOP-4.2.2/A-11/1/KONV-20120025
TÁMOP
OTKA-NK101337
OTKA
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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7.

001-es BibID:BIBFORM006038
Első szerző:Hochman, J. H.
Cím:Endocytosis and dissociation of class I MHC molecules labeled with fluorescent beta-2 microglobulin / J. H. Hochman, H. Jiang, L. Matyus, M. Edidin, B. Pernis
Dátum:1991
Megjegyzések:Membrane class I MHC molecules of Con-A activated and lymphoma murine cells have been labeled by exchange of the cell's beta 2m with soluble fl-beta 2m. It has previously been shown that this method of labeling is specific and does not affect the biologic properties of class I MHC Ag. With this labeling it has been possible to demonstrate the constitutive endocytosis of class I MHC by fluorescence microscopy and by measuring the resistance to quenching by crystal violet of the internalized fl-beta 2m molecules. We could also follow the kinetics of beta 2m dissociation from the class I molecules at different pH. At pH 5.5, that is the average pH of endosomes, there is considerable dissociation within 15 to 20 min, that is the average recycling half time of class I MHC containing endosomes in activated T cells. Inasmuch as the process is reversible it is likely that, in the recycling endosomes of T cells, class I MHC molecules undergo conformational changes with beta 2m going off and on and with consequent changes of the peptide binding site. This process might be involved in Ag presentation, but, because it is apparently limited to T cells, it would play a role in the presentation of the cell's own TCR in idiotypic interactions between T cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
beta 2-Microglobulin
diagnostic use
Endocytosis
Fluorescein
Fluoresceins
Fluorescence
Fluorescent Antibody Technique
Histocompatibility Antigens
Histocompatibility Antigens Class I
Human
Hydrogen-Ion Concentration
Kinetics
Lymphocyte Transformation
Lymphoma
metabolism
Microscopy
physiology
Support,Non-U.S.Gov't
Support,U.S.Gov't,P.H.S.
T-Lymphocytes
Tumor Cells,Cultured
Megjelenés:The Journal of Immunology. - 146 : 6 (1991), p. 1862-1867. -
További szerzők:Jiang, H. Mátyus László (1956-) (biofizikus) Edidin, Michael Pernis, B.
Internet cím:Intézményi repozitóriumban (DEA) tárolt változa
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8.

001-es BibID:BIBFORM097487
Első szerző:Kenesei Ádám
Cím:IL-15 Trans-Presentation Is an Autonomous, Antigen-Independent Process / Kenesei Ádám, Volkó Julianna, Szalóki Nikoletta, Mocsár Gábor, Jambrovics Károly, Balajthy Zoltán, Bodnár Andrea, Tóth Katalin, Waldmann Thomas A., Vámosi György
Dátum:2021
ISSN:0022-1767 1550-6606
Megjegyzések:IL-15 plays a pivotal role in the long-term survival of T cells and immunological memory. Its receptor consists of three subunits (IL-15R?, IL-2/15R?, and ?c). IL-15 functions mainly via trans-presentation (TP), during which an APC expressing IL-15 bound to IL-15R? presents the ligand to the ??c receptor-heterodimer on a neighboring T/NK cell. To date, no direct biophysical evidence for the intercellular assembly of the IL-15R heterotrimer exists. Ag presentation (AP), the initial step of T cell activation, is also based on APC?T cell interaction. We were compelled to ask whether AP has any effect on IL-15 TP or whether they are independent processes. In our human Raji B cell?Jurkat T cell model system, we monitored inter-/intracellular protein interactions upon formation of IL-15 TP and AP receptor complexes by Förster resonance energy transfer measurements. We detected enrichment of IL-15R? and IL-2/15R? at the synapse and positive Förster resonance energy transfer efficiency if Raji cells were pretreated with IL-15, giving direct biophysical evidence for IL-15 TP. IL-15R? and MHC class II interacted and translocated jointly to the immunological synapse when either ligand was present, whereas IL-2/15R? and CD3 moved independently of each other. IL-15 TP initiated STAT5 phosphorylation in Jurkat cells, which was not further enhanced by AP. Conversely, IL-15 treatment slightly attenuated Ag-induced phosphorylation of the CD3? chain. Our studies prove that in our model system, IL-15 TP and AP can occur independently, and although AP enhances IL-15R assembly, it has no significant effect on IL-15 signaling during TP. Thus, IL-15 TP can be considered an autonomous, Ag-independent process.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
interleukin
trans-presentation
immunology
Megjelenés:Journal Of Immunology. - 207 : 10 (2021), p. 2489-2500. -
További szerzők:Volkó Julianna (1983-) (biotechnológus) Szalóki Nikoletta (1981-) (biológus) Mocsár Gábor (1981-) (biofizikus) Jambrovics Károly (1988-) (biológus, gyógyszer-biotechnológus) Balajthy Zoltán (1957-) (biokémikus, sejtbiológus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Tóth Katalin Ágnes (1977-) (biokémikus, molekuláris biológus) Waldmann, Thomas A. Vámosi György (1967-) (biofizikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00026
GINOP
EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
Tempus Public Foundation 273478
Egyéb
Deutscher Akademischer Austauschdienst 273478
Egyéb
HHS | NIH | National Cancer Institute intramural research program
Egyéb
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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9.

001-es BibID:BIBFORM020764
Első szerző:Kis-Tóth Katalin (immunológus)
Cím:Voltage-Gated Sodium Channel Nav1.7 Maintains the Membrane Potential and Regulates the Activation and Chemokine-Induced Migration of a Monocyte-Derived Dendritic Cell Subset / Katalin Kis-Toth, Peter Hajdu, Ildiko Bacskai, Orsolya Szilagyi, Ferenc Papp, Attila Szanto, Edit Posta, Peter Gogolak, Gyorgy Panyi, Eva Rajnavolgyi
Dátum:2011
Megjegyzések:Expression of CD1a protein defines a human dendritic cell (DC) subset with unique functional activities. We aimed to study the expression of the Nav1.7 sodium channel and the functional consequences of its activity in CD1a(-) and CD1a(+) DC. Single-cell electrophysiology (patch-clamp) and quantitative PCR experiments performed on sorted CD1a(-) and CD1a(+) immature DC (IDC) showed that the frequency of cells expressing Na(+) current, current density, and the relative expression of the SCN9A gene encoding Nav1.7 were significantly higher in CD1a(+) cells than in their CD1a(-) counterparts. The activity of Nav1.7 results in a depolarized resting membrane potential (-8.7 +/- 1.5 mV) in CD1a(+) IDC as compared with CD1a(-) cells lacking Nav1.7 (-47 +/- 6.2 mV). Stimulation of DC by inflammatory signals or by increased intracellular Ca(2+) levels resulted in reduced Nav1.7 expression. Silencing of the SCN9A gene shifted the membrane potential to a hyperpolarizing direction in CD1a(+) IDC, resulting in decreased cell migration, whereas pharmacological inhibition of Nav1.7 by tetrodotoxin sensitized the cells for activation signals. Fine-tuning of IDC functions by a voltage-gated sodium channel emerges as a new regulatory mechanism modulating the migration and cytokine responses of these DC subsets
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
ACTIVATION
article
Cells
Electrophysiology
Human
Hungary
immunology
Sodium
Tetrodotoxin
Megjelenés:The Journal of Immunology. - 187 : 3 (2011), p. 1273-1280. -
További szerzők:Hajdu Péter (1975-) (biofizikus) Bacskai Ildikó (1985-) (immunológus) Szilágyi Orsolya (1985-) (molekuláris biológus, biokémikus) Papp Ferenc (1979-) (biofizikus) Szántó Attila (1976-) (orvos, biokémikus) Feketéné Posta Edit (1986-) (reumatológus) Gogolák Péter (1968-) (biológus, immunológus) Panyi György (1966-) (biofizikus) Rajnavölgyi Éva (1950-) (immunológus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Molekuláris immunológia
TÁMOP-4.2.2-08/1-2008-0015
TÁMOP
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
Szerző által megadott URL
Borító:

10.

001-es BibID:BIBFORM062127
Első szerző:Pallai Anna (biokémikus, molekuláris biológus)
Cím:Transmembrane TNF-[alfa] Reverse Signaling Inhibits Lipopolysaccharide-Induced Proinflammatory Cytokine Formation in Macrophages by Inducing TGF-[béta] : therapeutic Implications / Anna Pallai, Beáta Kiss, György Vereb, Marietta Armaka, George Kollias, Zoltán Szekanecz, Zsuzsa Szondy
Dátum:2016
ISSN:0022-1767 1550-6606
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal Of Immunology 196 : 3 (2016), p. 1146-1157. -
További szerzők:Kiss Beáta (1984-) (biokémikus, molekuláris biológus) Vereb György (1965-) (biofizikus, orvos) Armaka Marietta Kollias, George Szekanecz Zoltán (1964-) (reumatológus, belgyógyász, immunológus) Szondy Zsuzsanna (1959-) (molekuláris sejtbiológus, biokémikus)
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11.

001-es BibID:BIBFORM004690
035-os BibID:(scopus)0035191769 (wos)000172278000004
Első szerző:Pfeiffer, Alexandra
Cím:Lipopolysaccharide and ceramide docking to CD14 provokes ligand-specific receptor clustering in rafts / Pfeiffer, A., Bottcher, A., Orso, E., Kapinsky, M., Nagy, P., Bodnar, A., Spreitzer, I., Liebisch, G., Drobnik, W., Gempel, K., Horn, M., Holmer, S., Hartung, T., Multhoff, G., Schutz, G., Schindler, H., Ulmer, A. J., Heine, H., Stelter, F., Schutt, C., Rothe, G., Szollosi, J., Damjanovich, S., Schmitz, G.
Dátum:2001
Megjegyzések:The glycosylphosphatidylinositol-anchored receptor CD14 plays a major role in the inflammatory response of monocytes to lipopolysaccharide. Here, we describe that ceramide, a constituent of atherogenic lipoproteins, binds to CD14 and induces clustering of CD14 to co-receptors in rafts. In resting cells, CD14 was associated with CD55, the Fcgamma-receptors CD32 and CD64 and the pentaspan CD47. Ceramide further recruited the complement receptor 3 (CD11b/CD18) and CD36 into proximity of CD14. Lipopolysaccharide, in addition, induced co-clustering with Toll-like receptor 4, Fcgamma-RIIIa (CD16a) and the tetraspanin CD81 while CD47 was dissociated. The different receptor complexes may be linked to ligand-specific cellular responses initiated by CD14.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Antigens,CD
Antigens,CD14
Carrier Proteins
Ceramides
chemistry
Glycoproteins
Human
Inflammation
Ligands
Lipopolysaccharides
Macrophage-1 Antigen
Membrane Glycoproteins
Membrane Microdomains
metabolism
Monocytes
pharmacology
Receptors,Cell Surface
Support,Non-U.S.Gov't
Megjelenés:European Journal of Immunology. - 31 : 11 (2001), p. 3153-3164. -
További szerzők:Böttcher, Alfred Orsó Evelyn Kapinsky, Michael Nagy Péter (1971-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Spreitzer, Ingo Liebisch, Gerhard Drobnik, Wolfgang Gempel, Klaus Horn, Markus Holmer, Stefan Hartung, Thomas Multhoff, Gabriele Schütz, Gerhard Schindler, Hansgeorg Ulmer, Artur J. Heine, Holger Stelter, Felix Schütt, Christine Rothe, Gregor Szöllősi János (1953-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Schmitz, Gerd
Internet cím:DOI
Borító:

12.

001-es BibID:BIBFORM020768
Első szerző:Roszik János (biofizikus)
Cím:T-cell synapse formation depends on antigen recognition but not CD3 interaction : studies with TCR : zeta, a candidate transgene for TCR gene therapy / Roszik J., Sebestyén Z., Govers C., Guri Y., Szöor A., Pályi-Krekk Z., Vereb G., Nagy P., Szöllosi J., Debets R.
Dátum:2011
Megjegyzések:T-cell receptors (TCRs) can be genetically modified to improve gene-engineered T-cell responses, a strategy considered critical for the success of clinical TCR gene therapy to treat cancers. TCR:zeta, which is a heterodimer of TCRalpha and beta chains each coupled to complete human CD3zeta, overcomes issues of mis-pairing with endogenous TCR chains, shows high surface expression and mediates antigen-specific T-cell functions in vitro. In the current study, we further characterized TCR:zeta in gene-engineered T cells and assessed whether this receptor is able to interact with surface molecules and drive correct synapse formation in Jurkat T cells. The results showed that TCR:zeta mediates the formation of synaptic areas with antigen-positive target cells, interacts closely with CD8alpha and MHC class I (MHCI), and co-localizes with CD28, CD45 and lipid rafts, similar to WT TCR. TCR:zeta did not closely associate with endogenous CD3epsilon, despite its co-presence in immune synapses, and TCR:zeta showed enhanced synaptic accumulation in T cells negative for surface-expressed TCR molecules. Notably, synaptic TCR:zeta demonstrated lowered densities when compared with TCR in dual TCR T cells, a phenomenon that was related to both extracellular and intracellular CD3zeta domains present in the TCR:zeta molecule and responsible for enlarged synapse areas
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Adoptive Transfer
Antigens
Antigens,CD28
Antigens,CD3
Antigens,CD45
Antigens,CD8
article
Biophysics
Cells
Flow Cytometry
Gene Therapy
genetics
Histocompatibility Antigens
Histocompatibility Antigens Class I
Human
Humans
Hungary
Immunity,Cellular
Immunological Synapses
immunology
In Vitro
Jurkat Cells
lipid raft
LIPID RAFTS
Membrane Microdomains
metabolism
physiology
Receptor-CD3 Complex,Antigen,T-Cell
Receptors,Antigen,T-Cell,alpha-beta
Research
Research Support
Support
Synapses
T-Lymphocytes
therapy
Transgenes
Megjelenés:European Journal of Immunology. - 41 : 5 (2011), p. 1288-1297. -
További szerzők:Sebestyén Zsolt Govers, Coen Guri, Yakir Szöőr Árpád (1984-) (orvos) Pályiné Krekk Zsuzsanna (1974-) (molekuláris biológus) Vereb György (1965-) (biofizikus, orvos) Nagy Péter (1971-) (biofizikus) Szöllősi János (1953-) (biofizikus) Debets, Reno
Internet cím:DOI
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