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1.

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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2.

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
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3.

001-es BibID:BIBFORM001204
Első szerző:Bene László (biofizikus)
Cím:Colorectal carcinoma rearranges cell surface protein topology and density in CD4+ T cells / Bene L., Kanyári Z., Bodnár A., Kappelmayer J., Waldmann T. A., Vámosi G., Damjanovich L.
Dátum:2007
Megjegyzések:Previously, we described conserved protein clusters includingMHCI and II glycoproteins, ICAM-1 adhesion molecules, and interleukin- 2 and -15 receptors in lipid rafts of several human cell types. Differential protein interactions can modulate function, thus influence cell fate. Therefore, we analyzed supramolecular clusters of CD4+ T cells from draining lymph nodes and peripheral blood of colorectal carcinoma patients, and compared these to healthy controls. Superclusters of MHC I and II with IL-2/15 receptors were identified by confocal microscopy on all cell types. Flow-cytometricFRETrevealed molecular associations of these proteins with each other and withICAM-1 as well. In draining lymph nodes expression levels of all these proteins were lower, and interactions, particularly between IL-2/15 receptors and MHC molecules weakened or disappeared as compared to the control. Stimuli/local conditions can rearrange cell surface protein patterns on the same cell type in the same patient, having important implications on further function and cell fate.
Tárgyszavak:Orvostudományok Klinikai orvostudományok Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
CD4+ T cells
colorectal carcinoma
MHC I
MHC II
IL-2R
IL-15R
ICAM-1
receptor clustering
FRET
Flow cytometry
Confocal microscopy
Membrane protein association
Draining lymph node
Megjelenés:Biochemical and Biophysical Research Communications. - 361 : 1 (2007), p. 202-207. -
További szerzők:Kanyári Zsolt (1964-) (orvos) Dóczy-Bodnár Andrea (1970-) (biofizikus) Kappelmayer János (1960-) (laboratóriumi szakorvos) Waldmann, Thomas A. Vámosi György (1967-) (biofizikus) Damjanovich László (1960-) (általános sebész)
Internet cím:elektronikus változat
DOI
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4.

001-es BibID:BIBFORM046274
Első szerző:Gáspár Rezső (biofizikus)
Cím:[Béta]-scorpion toxin 2 from Centruroides noxius blocks voltage-gated K+ channels in human lymphocytes / Gaspar R., Bene L., Damjanovich S., Munoz-Garay C., Calderon-Aranda E. S., Possani L. D.
Dátum:1995
ISSN:0006-291X
Megjegyzések:Using the patch-clamp technique, we determined that beta-scorpion toxin 2 from Centruroides noxius Hoffmann decreased whole-cell n-type K+ currents in human peripheral blood lymphocytes, with a half blocking concentration of approx. 5 microM. Toxin-2-accelerated inactivation, however, did not influence the kinetics of activation of the K+ conductance. The percentage increase in K+ channel inactivation rate and the degree of drug-induced block was independent of membrane potential. K+ channel block by Toxin 2 was instantaneous, not removable by washing with drug free extracellular solution. However, 10 mg/ml BSA in the bath lifted the toxin-induced block almost instantaneously and completely. Flow cytometric membrane potential measurements with the oxonol dye showed that Toxin 2 depolarizes human lymphocytes in concert with its K+ channel blocking effect.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical And Biophysical Research Communications. - 213 : 2 (1995), p. 419-423. -
További szerzők:Bene László (1963-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Munoz-Garay, Carlos Calderon-Aranda, Emma S. Possani, Lourival Domingos
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DOI
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5.

001-es BibID:BIBFORM046293
Első szerző:Gáspár Rezső (biofizikus)
Cím:Effect of acetylcholine on the electrophysiology and proliferative response of human lymphocytes / Gaspar R., Varga Z., Bene L., Marcheselli F., Pieri C., Damjanovich S.
Dátum:1996
ISSN:0006-291X
Megjegyzések:Using the patch-clamp technique, we determined that 1-15 mM extracellular acetylcholine reduced whole-cell n-type K+ currents in human peripheral blood lymphocytes and accelerated their inactivation. The percentage increase in K+ channel inactivation rate and the degree of drug induced block were independent of membrane potential. In flow cytometric membrane potential measurements with the oxonol dye similar doses of acetylcholine depolarized the lymphocyte population. Both acetylcholine induced K+ channel block and depolarization fully developed within 2 minutes. The depolarizing and K+ channel blocking effects of acetylcholine are in concert. [3H]thymidine incorporation experiments proved that the proliferative response of PHA stimulated peripheral blood lymphocytes was decreased by increasing concentrations of acetylcholine in the 1-50 mM range.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical And Biophysical Research Communications. - 226 : 2 (1996), p. 303-308. -
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Bene László (1963-) (biofizikus) Marcheselli, Fiorella Pieri, Carlo Damjanovich Sándor (1936-2017) (biofizikus)
Pályázati támogatás:T14655
OTKA
T13335
OTKA
6221
OTKA
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DOI
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6.

001-es BibID:BIBFORM006044
Első szerző:Matkó János (biológus)
Cím:Biphasic effect of extracellular ATP on the membrane potential of mouse thymocytes / Matko J., Nagy P., Panyi G., Vereb G. Jr., Bene L., Matyus L., Damjanovich S.
Dátum:1993
Megjegyzések:Extracellular ATP induced changes in the membrane potential of thymocytes from BALB/c mice were analyzed. At concentrations below 0.1 mM, ATP hyperpolarizes the cell membrane on the time scale of development of the Ca(2+)-signal. After a longer time hyperpolarization turns to depolarization. ATP concentrations higher than 0.5 mM caused rapid depolarization without previous hyperpolarization. Verapamil, quinine or the absence of extracellular Ca2+ blocked the hyperpolarization by ATP. In Na(+)-free medium the magnitude of depolarization decreased. Our data suggest a contribution of Ca(2+)-activated K+ channels to the hyperpolarizing effect of ATP at lower concentrations. The direction of membrane potential changes is determined presumably by a sensitive balance of ATP-receptor mediated Ca(2+)- and Na(+)-influx and the Ca(2+)-activated K(+)-channel activity.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Adenosine Triphosphate
Animal
Biophysics
Cell Membrane
cytology
drug effects
Hungary
Kinetics
Membrane Potentials
Mice
Mice,Inbred BALB C
pharmacology
physiology
Quinine
Support,Non-U.S.Gov't
Thymus Gland
Verapamil
Megjelenés:Biochemical and Biophysical Research Communications. - 191 : 2 (1993), p. 378-384. -
További szerzők:Nagy Péter (1971-) (biofizikus) Panyi György (1966-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Bene László (1963-) (biofizikus) Mátyus László (1956-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:elektronikus változat
DOI
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7.

001-es BibID:BIBFORM006046
Első szerző:Mátyus László (biofizikus)
Cím:Voltage gating of Ca2(+)-activated potassium channels in human lymphocytes / Matyus, L., Pieri, C., Recchioni, R., Moroni, F., Bene, L., Tron, L., Damjanovich, S.
Dátum:1990
Megjegyzések:The effect of membrane potential on Ca2+ activated K+ channels was studied on human peripheral lymphocytes. Membrane potential was monitored using bisoxonol and flow cytometry. 1 mM Ca2+ in the presence of 2 microM ionomycin depolarized the control cell population, while 100 microM Ca2+ caused hyperpolarization. However 1 mM Ca2+ had a hyperpolarizing effect on previously partially depolarized cells. Potassium channel blockers did not influence the depolarization, while they inhibited the hyperpolarization. Based on the experimental evidence a voltage gating of Ca2+ activated K+ channels is suggested.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Biophysics
Calcium
drug effects
Flow Cytometry
Human
Hungary
In Vitro
Ion Channel Gating
Ionomycin
Leukocytes,Mononuclear
Lymphocytes
Membrane Potentials
pharmacology
physiology
Potassium
Potassium Channel Blockers
Potassium Channels
Support,Non-U.S.Gov't
Megjelenés:Biochemical and Biophysical Research Communications. - 171 : 1 (1990), p. 325-329. -
További szerzők:Pieri, Carlo Recchioni, Rina Moroni, Fausto Bene László (1963-) (biofizikus) Trón Lajos (1941-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:elektronikus változat
DOI
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8.

001-es BibID:BIBFORM004635
Első szerző:Péter Mózes (orvos, neuroradiológus) ifj.
Cím:Pandinus imperator scorpion venom blocks voltage-gated K+ channels in human lymphocytes / Peter, M. Jr., Varga, Z., Panyi, G., Bene, L., Damjanovich, S., Pieri, C., Possani, L. D., Gaspar, R.
Dátum:1998
ISSN:006-291X
Megjegyzések:Using the patch-clamp technique, we determined that Pandinus imperator scorpion venom blocked whole-cell n-type K+ currents in human peripheral blood lymphocytes in a dose-dependent manner with Kd = 0.02 microgram/ml. K+ channel block was instantaneous and removable by washing with venom-free extracellular solution. The venom-induced block was independent of membrane potential. The venom did not influence activation and inactivation kinetics of the K+ channels, however, accelerated recovery from inactivation. Purified peptides Pi1, Pi2, and Pi3 from the P. imperator venom powerfully blocked Kv1.3 channels in human lymphocytes with Kd values of 9.7 nM, 50 pM, and 0.5 nM, respectively. Flow cytometric membrane potential measurements with the oxonol dye showed that Pi2, the most effective peptide toxin of the P. imperator venom, depolarizes human lymphocytes in accordance with its K+ channel blocking effect.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Barbiturates
blood
drug effects
Electrophysiology
Flow Cytometry
Fluorescent Dyes
Human
isolation and purification
Isoxazoles
Kinetics
Lymphocytes
Membrane Potentials
metabolism
Patch-Clamp Techniques
pharmacology
physiology
Potassium
Potassium Channel Blockers
Potassium Channels
Protein Binding
Scorpion Venoms
Support, Non-U.S.Gov't
Support, U.S.Gov't, P.H.S.
Toxins
Megjelenés:Biochemical and Biophysical Research Communications. - 242 : 3 (1998), p. 621-625. -
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Panyi György (1966-) (biofizikus) Bene László (1963-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Pieri, Carlo Possani, Lourival Domingos Gáspár Rezső (1944-) (biofizikus)
Internet cím:DOI
elektronikus változat
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9.

001-es BibID:BIBFORM046306
Első szerző:Varga Zoltán (biofizikus, szakfordító)
Cím:The Effect of Juglone on the Membrane Potential and Whole-Cell K+Currents of Human Lymphocytes / Varga Z., Bene L., Pieri C., Damjanovich S., Gaspar R.
Dátum:1996
ISSN:0006-291X
Megjegyzések:Using flow cytometric membrane potential measurements with the oxonol dye, we determined that 5.7-57 microM juglone depolarizes human lymphocytes in a dose dependent manner. The depolarizing effect of juglone was verified by patch-clamp. Juglone decreased whole-cell n-type K+ currents in human peripheral blood lymphocytes and accelerated inactivation; however, it did not influence the kinetics of activation of the K+ conductance. The percentage increase in K+ channel inactivation rate and the degree of drug induced block was independent of membrane potential, K+ channel block by juglone fully developed within 4 minutes and was not removable by washing with drug free extracellular solution. Blocking of n-type K+ channels by juglone is in concert with its depolarizing effect on human lymphocytes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical And Biophysical Research Communications. - 218 : 3 (1996), p. 828-832. -
További szerzők:Bene László (1963-) (biofizikus) Pieri, Carlo Damjanovich Sándor (1936-2017) (biofizikus) Gáspár Rezső (1944-) (biofizikus)
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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