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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.
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001-es BibID:	BIBFORM006011
Első szerző:	Szöllősi János (biofizikus)
Cím:	Flow cytometric resonance energy transfer measurements support the association of a 95-kDa peptide termed T27 with the 55-kDa Tac peptide / J. Szöllösi, S. Damjanovich, C. K. Goldman, M. J. Fulwyler, A. A. Aszalos, G. Goldstein, P. Rao, M. A. Talle, T. A. Waldmann
Dátum:	1987
Megjegyzések:	Two monoclonal antibodies (OKT27 and OKT27b) have been produced that react with distinct epitopes of a 95-kDa peptide. The T27 antigen is widely distributed, being expressed on B lymphocytes, monocytes, and adult T-leukemic cells but not on polymorphonuclear leukocytes or platelets. There was a low level of T27 expression on resting T cells that increased on T-cell activation. In preliminary studies, the OKT27b antibody coprecipitated a 55-kDa peptide, as well as the 95-kDa peptide, from the radiolabeled cells of the HuT 102B2 cell line. Preclearance with anti-Tac, a monoclonal antibody to the 55-kDa peptide of the multichain interleukin 2 receptor, removed the 55-kDa but not the 95-kDa peptide from subsequent OKT27b immunoprecipitates of HuT 102B2 extracts, suggesting the possibility that the T27 peptide was associated with the Tac peptide. However, the precipitation of the p55 Tac peptide by OKT27b was quite inconsistent. Thus, additional information was sought using a flow cytometric energy transfer technique to provide a physical estimation of the proximity between the Tac and the T27 peptides. The flow cytometric version of the fluorescence resonance energy transfer technique permits the determination of inter- and intramolecular distances at 2- to 10-nm levels on a cell-by-cell basis. Using this approach, there was a mean energy transfer of 7.3% with HuT 102B2 cells when fluorescein isothiocyanate anti-Tac served as the donor and tetramethylrhodamine isothiocyanate OKT27 served as the acceptor. In contrast, there was no energy transfer in comparable studies observed when fluorescein anti-Tac and rhodamine anti-transferrin receptor antibodies were used. These observations support the conclusion that there is a close nonrandom proximity in HuT 102B2 cells between the 95-kDa peptide identified by the OKT27 monoclonal antibody and the p55 Tac peptide of the multichain interleukin 2 receptor.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Adult analysis Antibodies,Monoclonal Antigens,CD27 Antigens,Neoplasm Antigens,Surface B-Lymphocytes Biophysics Cell Line Energy Transfer Epitopes Flow Cytometry Fluorescence Human Hungary immunology Interleukin-2 Lymphocytes Monocytes Peptides Receptors,Immunologic Receptors,Interleukin-2 Support,Non-U.S.Gov't Support,U.S.Gov't,Non-P.H.S. T-Lymphocytes Tumor Cells,Cultured
Megjelenés:	Proceedings of the National Academy of Sciences of the United States of America. - 84 : 20 (1987), p. 7246-7250. -
További szerzők:	Damjanovich Sándor (1936-2017) (biofizikus) Goldman, Caroline K. Fulwyler, Mack J. Aszalos Adorján Goldstein, G. Rao, P. Talle, M. A. Waldmann, Thomas A.
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001-es BibID:	BIBFORM045740
035-os BibID:	(dekdb)9630543567
Első szerző:	Trón Lajos (biofizikus)
Cím:	On the role of cell surface dynamics and transmembrane information transfer: cyclosporin A changes physical properties of cell membranes / L. Trón, S. Damjanovich, A. Aszalós, J. Szöllősi, Sally A. Mulhern, M. J. Fulwyler
Dátum:	1986
ISBN:	9630543567
Tárgyszavak:	Orvostudományok Elméleti orvostudományok könyvfejezet Enzimek Biofizika Membránok (biológia) Anyagcsere Fehérjék Nukleinsavak
Megjelenés:	Dynamics of biochemical systems: lectures presented at the FEBS advanced course and round table discussion of the IUB interest group on kinetics and mechanisms of enzymes and metabolic networks: Debrecen, Hungary, 18-24 August 1985 / ed. by S. Damjanovich, T. Keleti, L. Trón. - p. 417-441. -
További szerzők:	Damjanovich Sándor (1936-2017) (biofizikus) Aszalos Adorján Szöllősi János (1953-) (biofizikus) Mulhern, Sally Fulwyler, Mack J.
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM006018
Első szerző:	Trón Lajos (biofizikus)
Cím:	On the biophysics of transmembrane signalling / L. Trón, A. Aszalos, M. Balázs, Sally A. Mulhern, J. Szöllösi, S. Damjanovich
Dátum:	1988
Megjegyzések:	Transmembrane signalling involves a number of physical translocations, changes in proximity of membrane elements like receptor subunits, or sequestration of proteins from the membrane. The monitoring of such changes with flow cytometric energy transfer revealed a new putative subunit of the IL-2 receptor and a possible intermolecular interaction between HLA class I and class II antigens. Lateral diffusion of the components of the multi-subunit IL-2 receptor was also followed. Changes in the intracellular pH were considered as a measure of efficient signal transfer in a number of cases. An overview and critical comparison of data is presented in the paper.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Biophysics Cell Membrane Diffusion Energy Transfer HLA Antigens Human Hungary immunology Interleukin-2 physiology Receptors,Interleukin-2 Signal Transduction Support,Non-U.S.Gov't
Megjelenés:	Molecular Immunology. - 25 : 11 (1988), p. 1075-1080. -
További szerzők:	Aszalos Adorján Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Mulhern, Sally Szöllősi János (1953-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
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