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001-es BibID:	BIBFORM004699
Első szerző:	Bacsó Zsolt (biofizikus)
Cím:	INF-gamma rearranges membrane topography of MHC-I and ICAM-1 in colon carcinoma cells / Bacso, Z., Bene, L., Damjanovich, L., Damjanovich, S.
Dátum:	2002
Megjegyzések:	Flow-cytometric fluorescence energy transfer (FCET) measurements between fluorescently labeled cell surface MHC-I and ICAM-1 molecules indicated similar receptor patterns in the plasma membrane of interferon-gamma (INF-gamma)-treated colon carcinoma cells as those observed earlier at the surface of lymphoid cells. INF-gamma activation significantly increased the density of MHC-I and ICAM-1 proteins in the membrane. This increase in receptor density was accompanied by decreased proximity level of the homo-associated MHC-I receptors. Hetero-association of MHC-I and ICAM-1 molecules was increased by INF-gamma treatment. INF-gamma changed neither hetero- nor homo-association of transferrin receptors. By staining the sphingomyelin/cholesterol-enriched lipid microdomains with fluorescently labeled cholera toxin B subunit, we found an increase in the amount of lipid-raft associated G(M1)-gangliosides due to INF-gamma treatment. Confocal microscopic results and FCET measurements show that MHC-I and ICAM-1 are components of G(M1)-ganglioside containing lipid-rafts and also support an increase in the size of these lipid-rafts upon INF-gamma treatment.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Carcinoma Cell Membrane chemistry Cholera Toxin Colonic Neoplasms drug effects Energy Transfer Flow Cytometry Fluorescein-5-isothiocyanate Fluorescence G(M1) Ganglioside Histocompatibility Antigens Class I Human Hungary Intercellular Adhesion Molecule-1 Interferon Type II Membrane Microdomains metabolism Microscopy,Confocal pathology pharmacology Protein Binding Receptors,Cell Surface Receptors,Transferrin Support,Non-U.S.Gov't Tumor Cells,Cultured
Megjelenés:	Biochemical and Biophysical Research Communications. - 290 : 2 (2002), p. 635-640. -
További szerzők:	Bene László (1963-) (biofizikus) Damjanovich László (1960-) (általános sebész) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:	DOI elektronikus változat
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001-es BibID:	BIBFORM004830
035-os BibID:	WOS:000223675800046
Első szerző:	Bene László (biofizikus)
Cím:	Membrane topography of HLA I, HLA II, and ICAM-1 is affected by IFN-gamma in lipid rafts of uveal melanomas / László Bene, Andrea Bodnár, Sándor Damjanovich, György Vámosi, Zsolt Bacsó, János Aradi, András Berta, Judit Damjanovich
Dátum:	2004
Megjegyzések:	The lateral distribution and colocalization of HLA I, HLA-DR, and ICAM-1 proteins was studied for the first time in the plasma membrane of two human uveal melanoma cell lines, OCM-1 and OCM-3. Our fluorescence resonance energy transfer and confocal laser scanning microscopic experiments revealed that these molecules are mostly confined to the same membrane regions, where they form similar protein patterns (homo- and hetero-associates) to those found previously on other cell types of lymphoid as well as colorectal carcinoma origin. Confocal microscopic colocalization experiments with GM(1) gangliosides and the GPI-anchored CD59 molecules showed enrichment of HLA I, HLA-DR, and ICAM-1 molecules in specific membrane domains (lipid rafts) excluding the transferrin receptor. IFN-gamma remarkably increased the expression levels of these molecules and rearranged their association patterns, which can affect the adoptive immune response of effector cells
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Antigens Biophysics Carcinoma Cell Line Cells Energy Transfer Flow Cytometry Fluorescence Fluorescence Resonance Energy Transfer Histocompatibility Antigens Histocompatibility Antigens Class I Histocompatibility Antigens Class II Human Humans Hungary Intercellular Adhesion Molecule-1 Interferon Type II Melanoma Membrane Microdomains metabolism Microscopy,Confocal Proteins Research Support Uveal Neoplasms egyetemen (Magyarországon) készült közlemény
Megjelenés:	Biochemical and Biophysical Research Communications. - 322 : 2 (2004), p. 678-683. -
További szerzők:	Dóczy-Bodnár Andrea (1970-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Vámosi György (1967-) (biofizikus) Bacsó Zsolt (1963-) (biofizikus) Aradi János (1942-) (biokémikus, vegyész) Berta András (1955-) (szemész, gyermekszemész) Damjanovich Judit (1963-) (szemész)
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM004839
035-os BibID:	(WOS)000220105600025 (scopus)1342345242
Első szerző:	Nagy Henrietta
Cím:	Distinct groups of multidrug resistance modulating agents are distinguished by competition of P-glycoprotein-specific antibodies / Nagy, H., Goda, K., Fenyvesi, F., Bacso, Z., Szilasi, M., Kappelmayer, J., Lustyik, G., Cianfriglia, M., Szabo, G.
Dátum:	2004
Megjegyzések:	P-glycoprotein (Pgp) is one of the ABC transporters responsible for the multidrug resistance of cancer cells. The conformational changes of Pgp that occur in the presence of substrates/modulators or ATP depletion are accompanied by the up-shift of UIC2 monoclonal antibody (mAb) binding. In the case of cyclosporin A, vinblastine or valinomycin, this up-shift was found to be concomitant with the near-complete suppression of labeling with other mAbs specific for Pgp epitopes overlapping with UIC2, while pre-treatment with verapamil or Tween 80 brings about a modest suppression. Here we have extended these observations to 44 Pgp interacting agents, and found that only 8 fall into the cyclosporin-like category, inducing a conformational state characterized by the complete UIC2 dominance. The rest of the drugs either did not affect antibody competition or had a modest effect. Thus, Pgp substrates/modulators can be classified into distinct modalities based on the conformational change they elicit.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Adenosine Adenosine Triphosphatases Animals Anti-Bacterial Agents Antibodies Antibodies,Monoclonal Antineoplastic Agents Binding,Competitive Biophysics Calcium Calcium Channel Blockers Cells Cyclosporine Detergents Drug Resistance,Multiple Drug Resistance,Neoplasm Epitopes Flow Cytometry Fluorescein Fluoresceins genetics Humans Hungary immunology Ivermectin metabolism Mice Nih 3T3 Cells P-Glycoprotein pharmacology physiology Research Substrate Specificity Support Valinomycin Verapamil Vinblastine egyetemen (Magyarországon) készült közlemény
Megjelenés:	Biochemical and Biophysical Research Communications. - 315 : 4 (2004), p. 942-949. -
További szerzők:	Goda Katalin (1969-) (biofizikus) Fenyvesi Ferenc (1977-) (gyógyszerész, gyógyszertechnológus) Bacsó Zsolt (1963-) (biofizikus) Szilasi Mária (1953-) (tüdőgyógyász, klinikai immunológus, allergológus, belgyógyász) Kappelmayer János (1960-) (laboratóriumi szakorvos) Lustyik György Cianfriglia, Maurizio Szabó Gábor (1953-) (biofizikus)
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001-es BibID:	BIBFORM043991
Első szerző:	Pieri, Carlo
Cím:	Bretylium differentiates between distinct signal transducing pathways in human lymphocytes / Pieri, C., Bacso, Z., Recchioni, R., Moroni, F., Balazs, M., Gaspar, R., Damjanovich, S.
Dátum:	1993
ISSN:	0006-291X
Megjegyzések:	The selection of signal transducing pathways of T cells depends on the type of triggers. Antigens, antibodies or lectins induce the T cell receptor-CD3 operated pathway, and IL-2 transmits its activation signal via the IL-2 receptor. It has been demonstrated that bretylium, a quaternary ammonium ion, can significantly inhibit the first pathway at the same dose range that stimulates cell activation through the IL-2 receptor system. In the light of the different complexity of the two pathways at the plasma membrane level, and the non-toxic and reversible behavior of the drug, it is suggested that the bretylium induced sustained membrane hyperpolarization is responsible for the observation. This finding may open new possibilities in studying the mechanism of different signal transducing pathways.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Biochemical And Biophysical Research Communications. - 190 : 2 (1993), p. 654-659. -
További szerzők:	Bacsó Zsolt (1963-) (biofizikus) Recchioni, Rina Moroni, Fausto Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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