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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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