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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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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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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
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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 Intézményi repozitóriumban (DEA) tárolt változat
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