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001-es BibID:	BIBFORM046090
Első szerző:	Bacsó Zsolt (biofizikus)
Cím:	Raft and cytoskeleton associations of an ABC transporter : P-glycoprotein / Zsolt Bacso, Henrietta Nagy, Katalin Goda, László Bene, Ferenc Fenyvesi, János Matkó, Gábor Szabó
Dátum:	2004
ISSN:	0196-4763
Megjegyzések:	A novel flow cytometric assay has been described in an accompanying report (Gombos et al., METHODS: The kinetics of the decrease in immunofluorescence intensity was analyzed after the addition of the raft-preserving Triton X-100 or Nonidet P-40, both of which disrupt the entire membrane. Mild treatments by both detergents leave cells attached to only those proteins that are anchored to the cytoskeleton by rafts or independent of rafts. Agents that affect microfilaments and modulate membrane levels of cholesterol by cyclodextrin were used to distinguish between the raft-mediated and non-raft-related associations of the Pgp. Confocal microscopy and flow cytometric fluorescence energy transfer measurements were used to confirm colocalization of Pgp with raft constituents. RESULTS: The assay was proved to be sensitive enough to resolve differences between the resistance of UIC2-labeled cell-surface Pgps to Triton X-100 versus Nonidet P-40. Approximately 34% of the UIC2 Fab-labeled Pgp molecules were associated with the cytoskeleton through detergent-resistant, cholesterol-sensitive microdomains or directly, whereas approximately 15% were found to be directly linked to the cytoskeleton. Accordingly, confocal microscopy showed that Pgps colocalize with raft markers, mainly in microvilli. Fluorescence resonance energy transfer efficiency data indicating molecular proximity between Pgp and the raft markers CD44, CD59, and G(M1)-gangliosides also suggested that a significant fraction of Pgps resides in raft microdomains. Raft association of Pgp appears to be of functional significance because its modulation markedly affected drug pumping. CONCLUSIONS: By using the flow cytometric detergent resistance assay in kinetic mode, we were able to assess the extent of raft association and actin cytoskeleton anchorage of Pgp expressed at physiologically relevant levels. We demonstrated that a significant fraction of Pgp is raft associated on LS-174-T human colon carcinoma cells and that this localization may influence its transporter function. The kinetic flow cytometric detergent resistance assay presented in this report is considered to be generally applicable for the analysis of molecular interactions of membrane proteins expressed at low levelsújratöltve - BIBFORM004828
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Cytometry. - 61 : 2 (2004), p. 105-116. -
További szerzők:	Nagy Henrietta Goda Katalin (1969-) (biofizikus) Bene László (1963-) (biofizikus) Fenyvesi Ferenc (1977-) (gyógyszerész, gyógyszertechnológus) Matkó János (1952-) (biológus) Szabó Gábor (1953-) (biofizikus)
Pályázati támogatás:	T032563 OTKA 034393 OTKA T046945 OTKA
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM004645
035-os BibID:	(scopus)0033552675 (wos)000084290400003
Első szerző:	Damjanovich Sándor (biofizikus)
Cím:	Two-dimensional receptor patterns in the plasma membrane of cells : a critical evaluation of their identification, origin and information content / Damjanovich, S., Bene, L., Matko, J., Matyus, L., Krasznai, Z., Szabo, G., Pieri, C., Gaspar, R., Szollosi, J.
Dátum:	1999
Megjegyzések:	A concise review is presented on the nature, possible origin and functional significance of cell surface receptor patterns in the plasma membrane of lymphoid cells. A special emphasize has been laid on the available methodological approaches, their individual virtues and sources of errors. Fluorescence energy transfer is one of the oldest available means for studying non-randomized co-distribution patterns of cell surface receptors. A detailed and critical description is given on the generation of two-dimensional cell surface receptor patterns based on pair-wise energy transfer measurements. A second hierarchical-level of receptor clusters have been described by electron and scanning force microscopies after immuno-gold-labeling of distinct receptor kinds. The origin of these receptor islands at a nanometer scale and island groups at a higher hierarchical (mum) level, has been explained mostly by detergent insoluble glycolipid-enriched complexes known as rafts, or detergent insoluble glycolipids (DIGs). These rafts are the most-likely organizational forces behind at least some kind of receptor clustering [K. Simons et al., Nature 387 (1997) 569]. These models, which have great significance in trans-membrane signaling and intra-membrane and intracellular trafficking, are accentuating the necessity to revisit the Singer-Nicolson fluid mosaic membrane model and substitute the free protein diffusion with a restricted diffusion concept.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Biophysics Cells Diffusion Energy Transfer Fluorescence Hungary Microscopy
Megjelenés:	Biophysical Chemistry. - 82 : 2-3 (1999), p. 99-108. -
További szerzők:	Bene László (1963-) (biofizikus) Matkó János (1952-) (biológus) Mátyus László (1956-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Szabó Gábor (1953-) (biofizikus) Pieri, Carlo Gáspár Rezső (1944-) (biofizikus) Szöllősi János (1953-) (biofizikus)
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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)
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001-es BibID:	BIBFORM035608
Első szerző:	Szabó Gábor (biofizikus)
Cím:	Lack of Correlation Between c-myc and Transferrin receptor Expression in Proliferating HL60 Cells / Szabó Gábor, Bacsó Zsolt, Bene László, Pohubi László, Damjanovich Sándor
Dátum:	1990
Tárgyszavak:	Orvostudományok Elméleti orvostudományok könyvfejezet könyvrészlet
Megjelenés:	Oncogenesis: Oncogenes in Signal Transduction and Cell Proliferation / szerk. Papas T. - p. 183-187.
További szerzők:	Bacsó Zsolt (1963-) (biofizikus) Bene László (1963-) (biofizikus) Pohubi László (1959-) (fizikus) Damjanovich Sándor (1936-2017) (biofizikus)
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