CCL

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1.

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
Borító:

2.

001-es BibID:BIBFORM004939
Első szerző:Bene László (biofizikus)
Cím:Major histocompatibility complex class I protein conformation altered by transmembrane potential changes / Bene, L., Szollosi, J., Balazs, M., Matyus, L., Gaspar, R., Ameloot, M., Dale, R. E., Damjanovich, S.
Dátum:1997
ISSN:0196-4763
Megjegyzések:The nature of charge distributions in membrane-bound macromolecular structures renders them susceptible to interaction with transmembrane potential fields. As a result, conformational changes in such species may be expected to occur when this potential is altered. We have detected reversible conformational change in the major histocompatibility complex (MHC) class I antigen in the plasma membrane of human JY cells, as monitored by flow-cytometric resonance energy-transfer, upon reduction of the transmembrane potential (depolarization). This change increased the intramolecular energy-transfer efficiency between fluorescent donor- and acceptor-labeled monoclonal antibodies directed, respectively, to epitopes on the light (beta 2-microglobulin) and the heavy chains of the MHC class I antigen. Repolarization of the depolarized samples restored the energy-transfer efficiency to the original values measured before depolarization. Depolarization caused similar relative changes in fluorescence resonance energy-transfer efficiency when Fab fragments were used for labeling MHC class I complex, suggesting that the observed phenomenon is not restricted to whole monoclonal antibodies.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Antibodies, Monoclonal
Antigen Presentation
B-Lymphocytes
beta 2-Microglobulin
Cell Membrane
chemistry
cytology
Dyes
Energy Transfer
Enzyme Activation
Flow Cytometry
Fluorescein-5-isothiocyanate
Fluorescence
Fluorescent Dyes
Histocompatibility Antigens Class I
Human
Hungary
immunology
Light
Major Histocompatibility Complex
Membrane Potentials
metabolism
methods
Na(+)-K(+)-Exchanging ATPase
Patch-Clamp Techniques
physiology
Protein Conformation
Rhodamines
Surface Properties
Megjelenés:Cytometry. - 27 : 4 (1997), p. 353-357. -
További szerzők:Szöllősi János (1953-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Mátyus László (1956-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Ameloot, Marcel Dale, Robert E. Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:elektronikus változat
Borító:

3.

001-es BibID:BIBFORM004664
035-os BibID:(scopus)0033670124 (wos)000165543500002
Első szerző:Goda Katalin (biofizikus)
Cím:Conformational heterogeneity of P-glycoprotein / Goda, K., Nagy, H., Bene, L., Balazs, M., Arceci, R., Mechetner, E., Szabo, G.
Dátum:2000
Megjegyzések:P-glycoprotein (P-gp) acts as an active efflux mechanism for a large number of cytostatics and seems to be involved in the frequent failure of cancer chemotherapy. The molecular events of substrate recognition and transport still are not understood completely. We show here that the percentage of P-gp epitopes available for labeling with UIC2 monoclonal antibody is increased significantly after methanol permeabilization/fixation of cells. At the same time, binding of the MRK16 and 4E3 anti-P-gp antibodies is changed only moderately. Confocal microscopical images of UIC2-PE-labeled cells show that the epitopes becoming available after fixation are situated mainly in the plasma membrane. Thus, only a minority of P-gp molecules are accessible for UIC2 in the cell membrane of live cells, and methanol treatment can expose a large pool of previously plasma membrane-embedded, cryptic UIC2 epitopes. The UIC2-reactive P-gp molecules do not appear to be sequestered spatially, as suggested by the high fluorescence resonance energy transfer efficiency measured between the fluorescently labeled competing UIC2 and MRK16 antibodies, suggestive of P-gp dimerization and oligomerization on live cells
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
3T3 Cells
Animal
Antibodies
Antibodies,Monoclonal
Biophysics
Cell Membrane
Cell Membrane Permeability
Cells
chemistry
Dimerization
drug effects
Energy Transfer
Epitopes
Fixatives
Flow Cytometry
Fluorescence
Human
Hungary
immunology
KB Cells
metabolism
Methanol
Mice
Microscopy,Confocal
P-Glycoprotein
pharmacology
Protein Conformation
Support,Non-U.S.Gov't
Megjelenés:Cancer Detection and Prevention. - 24 : 5 (2000), p. 415-421. -
További szerzők:Nagy H. Bene László (1963-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Arceci, Robert Mechetner, Eugene Szabó Gábor (1953-) (biofizikus)
Borító:

4.

001-es BibID:BIBFORM006042
035-os BibID:PMID:8419464
Első szerző:Márián Teréz (radiobiológus)
Cím:Hypo-osmotic shock induces an osmolality-dependent permeabilization and structural changes in the membrane of carp sperm / Teréz Márián, Zoltán Krasznai, László Balkay, Margit Balázs, Miklós Emri, László Bene, Lajos Trón
Dátum:1993
Megjegyzések:We carried out spectrofluorimetric and flow cytometric measurements to investigate the effect of hypo-osmotic shock on cell membranes of common carp sperm. The time course of the permeability of the sperm cell membrane, as monitored by DNA-related propidium iodide (PI) fluorescence, was followed for 30 min after dilution of semen in hypo-osmotic environments of different ionic strengths. Spectrofluorimetric measurements indicated a continuous increase in the total PI emission intensity of a sperm suspension. Cell-by-cell flow cytometric measurements suggested that the permeability changes were of the all-or-none type. The permeabilized fraction of cells in the individual samples was time and osmolality dependent. The number and percentage of cells in which DNA was stained by PI increased gradually over time and reached a steady-state plateau value after 5-15 min. This equilibrium fraction of cells with a PI-permeable cytoplasmic membrane displayed an inverse relationship with the osmolality of the diluent, having a near 100% value for fresh water and distilled water. Dilution of sperm in hypo-osmotic medium brought about a fast decrease in the forward light-scattering signal on a short time scale compared to the pre-steady-state time of the permeabilization. With the addition of extracellular Ca2+ (1.8 mM), restoration of the light scattering signal was observed. Permeabilization of the membrane and restoration of light scattering were not coincident in time. We propose a two-dimensional reorganization of the lipid structure as the underlying mechanism of the latter process.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animal
Calcium
Calcium Chloride
Carps
Cell Membrane
Cell Membrane Permeability
Cells
Dna
drug effects
Flow Cytometry
Fluorescence
Hungary
Light
Male
Osmolar Concentration
Osmotic Pressure
pharmacology
physiology
Propidium
Semen
Spectrometry,Fluorescence
Spermatozoa
Support,Non-U.S.Gov't
ultrastructure
Water
egyetemen (Magyarországon) készült közlemény
Megjelenés:The Journal of Histochemistry and Cytochemistry. - 41 : 2 (1993), p. 291-297. -
További szerzők:Krasznai Zoltán (1950-) (biofizikus) Balkay László (1963-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Emri Miklós (1962-) (fizikus) Bene László (1963-) (biofizikus) Trón Lajos (1941-) (biofizikus)
Internet cím:elektronikus változat
Szerző által megadott URL
DOI
Borító:

5.

001-es BibID:BIBFORM004634
035-os BibID:(scopus)0032101894 (wos)000073937700007
Első szerző:Nagy Péter (biofizikus)
Cím:EGF-induced redistribution of erbB2 on breast tumor cells : flow and image cytometric energy transfer measurements / Nagy, P., Bene, L., Balazs, M., Hyun, W. C., Lockett, S. J., Chiang, N. Y., Waldman, F., Feuerstein, B. G., Damjanovich, S., Szollosi, J.
Dátum:1998
Megjegyzések:erbB2, a member of the epidermal growth factor (EGF) receptor-type tyrosine kinase receptor family, is overexpressed in breast carcinomas with poor prognosis. We examined the cell surface association of this receptor with itself and with other cell surface proteins by the Forster-type fluorescence resonance energy transfer using whole antibodies and Fab fragments. We found that erbB2 molecules homoassociate in unstimulated SK-BR-3, BT474 and BT474-M (a metastatic version of the parent BT474 line) breast tumor cells, and that the interaction was enhanced by EGF treatment in suspensions of SK-BR-3 and BT474-M cells. BT474 cells (with low EGF receptor expression) and attached SK-BR-3 cells do not respond to EGF. Image microscopic energy transfer measurements found considerable pixel-by-pixel heterogeneity in the homoassociation state of erbB2. In accordance with the EGF-induced redistribution of erbB2, EGF receptor was found to be in close proximity to erbB2 in FRET measurements. By labeling different epitopes on erbB2 and the lipid bilayer, we were able to prepare an epitope map of erbB2 molecule. Our data suggest the existence of dynamic cell surface patterns of erbB2 and point to functions fulfilled by these molecular complexes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
analysis
biosynthesis
Breast Neoplasms
Carcinoma
Cell Membrane
chemistry
drug effects
Energy Transfer
Epidermal Growth Factor
Female
Flow Cytometry
Fluorescence
Human
Hungary
metabolism
methods
Models
Molecular
pharmacology
Receptor
erbB-2
Receptors
Transferrin
Support
Non-U.S.Gov't
Tumor Cells,Cultured
Squamous Cell
ultrastructure
Megjelenés:Cytometry. - 32 : 2 (1998), p. 120-131. -
További szerzők:Bene László (1963-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Hyun, William C. Lockett, Steven J. Chiang, Nancy Y. Waldman, Frederick Feuerstein, Burt G. Damjanovich Sándor (1936-2017) (biofizikus) Szöllősi János (1953-) (biofizikus)
Internet cím:elektronikus változat
DOI
Borító:

6.

001-es BibID:BIBFORM033278
035-os BibID:PMID:8588941 WOS:A1995TF18900001
Első szerző:Vereb György (biofizikus, orvos)
Cím:Plasma-membrane-bound macromolecules are dynamically aggregated to form non-random codistribution patterns of selected functional elements. Do pattern recognition processes govern antigen presentation and intercellular interactions? / György Vereb, László Matyus, László Bene, György Panyi, Zsolt Bacsó, Margit Balázs, János Matkó, János Szöllősi, Rezső Gáspár, Sándor Damjanovich, Robert E. Dale, Carlo Pieri, Marcel Ameloot
Dátum:1995
Megjegyzések:Molecular recognition processes between cell surface elements are discussed with special reference to cell surface pattern formation of membrane-bound integral proteins. The existence, as detected by flow cytometric resonance energy transfer (Appendix), and significance of cell surface patterns involving the interleukin-2 receptor, the T-cell receptor-CD3 system, the intercellular adhesion molecule ICAM-1, and the major histocompatibility complex class I and class II molecules in the plasma membrane of lymphocytes are described. The modulation of antigen presentation by transmembrane potential changes is discussed, and a general role of transmembrane potential changes, and therefore of ion channel activities, adduced as one of the major regulatory mechanisms of cell-cell communication. A general role in the mediation and regulation of intercellular interactions is suggested for cell-surface macromolecular patterns. The dynamic pattern of protein and lipid molecules in the plasma membrane is generated by the genetic code, but has a remarkable flexibility and may be one of the major instruments of accommodation and recognition processes at the cellular level.
Tárgyszavak:Orvostudományok Egészségtudományok idegen nyelvű folyóiratközlemény külföldi lapban
cell surface
molecular pattern
energy transfer
fluorescence
flow cytometry
transmembrane potential
MHC
antigen presentation
intercellular communication
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal of Molecular Recognition. - 8 : 4 (1995), p. 237-246. -
További szerzők:Mátyus László (1956-) (biofizikus) Bene László (1963-) (biofizikus) Panyi György (1966-) (biofizikus) Bacsó Zsolt (1963-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Matkó János (1952-) (biológus) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Dale, Robert E. Pieri, Carlo Ameloot, Marcel
Internet cím:DOI
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