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1.

001-es BibID:BIBFORM005185
035-os BibID:(scopus)46449085498 (wos)000257176000003
Első szerző:Kiss Endre (Budapest)
Cím:Cytometry of raft and caveola membrane microdomains : from flow and imaging techniques to high throughput screening assays / Kiss, E., Nagy, P., Balogh, A., Szollosi, J., Matko, J.
Dátum:2008
ISSN:552-4930 (Electronic)
Megjegyzések:The evolutionarily developed microdomain structure of biological membranes has gained more and more attention in the past decade. The caveolin-free "membrane rafts," the caveolin-expressing rafts (caveolae), as well as other membrane microdomains seem to play an essential role in controlling and coordinating cell-surface molecular recognition, internalization/endocytosis of the bound molecules or pathogenic organisms and in regulation of transmembrane signal transduction processes. Therefore, in many research fields (e.g. neurobiology and immunology), there is an ongoing need to understand the nature of these microdomains and to quantitatively characterize their lipid and protein composition under various physiological and pathological conditions. Flow and image cytometry offer many sophisticated and routine tools to study these questions. In this review, we give an overview of the past efforts to detect and characterize these membrane microdomains by the use of classical cytometric technologies, and finally we will discuss the results and perspectives of a new line of raft cytometry, the "high throughput screening assays of membrane microdomains," based on "lipidomic" and "proteomic" approaches.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Animals
article
Caveolae
Cell Membrane
chemistry
Detergents
Flow Cytometry
Fluorescence Resonance Energy Transfer
Humans
Hungary
Image Cytometry
immunology
Lipids
Membrane Lipids
Membrane Microdomains
metabolism
methods
pharmacology
Protein Structure, Tertiary
Proteomics
Research
Research Support
Signal Transduction
Support
Megjelenés:Cytometry. Part A. - 73A : 7 (2008), p. 599-614. -
További szerzők:Nagy Péter (1971-) (biofizikus) Balogh Andrea Szöllősi János (1953-) (biofizikus) Matkó János (1952-) (biológus)
Internet cím:DOI
elektronikus változat
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2.

001-es BibID:BIBFORM048673
Első szerző:Matkó János (biológus)
Cím:Fluorescent lipid probes 12-AS and TMA-DPH report on selective, purinergically induced fluidity changes in plasma membranes of lymphoid cells / János Matkó, Péter Nagy
Dátum:1997
ISSN:1011-1344
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal Of Photochemistry And Photobiology B-Biology. - 40 : 2 (1997), p. 120-125. -
További szerzők:Nagy Péter (1971-) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

3.

001-es BibID:BIBFORM023492
Első szerző:Matkó János (biológus)
Cím:Analysis of cell surface molecular distributions and cellular signaling by flow cytometry / J. Matkó, L. Mátyus, J. Szöllősi, L. Bene, A. Jenei, P. Nagy, A. Bodnár, S. Damjanovich
Dátum:1994
ISSN:1053-0509
Megjegyzések:Flow cytometry is a fast analysis and separation method for large cell populations, based on collection and processing of optical signals gained on a cell-by-cell basis. These optical signals are scattered light and fluorescence. Owing to its unique potential ofStatistical data analysis and sensitive monitoring of (micro)heterogeneities in large cell populations, flow cytometry?in combination with microscopic imaging techniques?is a powerful tool to study molecular details of cellular signal transduction processes as well. The method also has a widespread clinical application, mostly in analysis of lymphocyte subpopulations for diagnostic (or research) purposes in diseases related to the immune system. A special application of flow cytometry is the mapping of molecular interactions (proximity relationships between membrane proteins) at the cell surface, on a cell-by-cell basis. We developed two approaches to study such questions; both are based ondistance-dependent quenching of excited state fluorophores (donors) by fluorescent or dark (nitroxide radical) acceptors via Förstertype dipole-dipole resonance energy transfer (FRET) and long-range electron transfer (LRET) mechanisms, respectively. A critical evaluation of these methods using donor- or acceptor-conjugated monoclonal antibodies (or their Fab fragments) to select the appropriate cell surface receptor or antigen will be presented in comparison with other approaches for similar purposes. The applicability of FRET and LRET for two-dimensional antigen mapping as well as for detection of conformational changes in extracellular domains of membrane-bound proteins is discussed and illustrated by examples of several lymphoma cell lines. Another special application area of flow cytometry is the analysis of different aspects of cellular signal transduction, e.g., changes of intracellular ion (Ca2+, H+, Na+) concentrations, regulation of ion channel activities, or more complex physiological responses of cell to external stimuli via correlated fluorescence and scatter signal analysis, on a cell-by-cell basis. This way different signaling events such as changes in membrane permeability, membrane potential, cell size and shape, ion distribution, cell density, chromatin structure, etc., can be easily and quickly monitored over large cell populations with the advantage of revealing microheterogeneities in the cellular responses. Flow cytometry also offers the possibility to follow the kinetics of slow (minute- and hour-scale) biological processes in cell populations. These applications are illustrated by the example of complex flow cytometric analysis of signaling in extracellular ATP-triggered apoptosis (programmed cell death) of murine thymic lymphocytes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
fluorescence
flow cytometry
energy transfer
electron transfer
protein-protein interaction
signal transduction
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal Of Fluorescence 4 : 4 (1994), p. 303-314. -
További szerzők:Mátyus László (1956-) (biofizikus) Szöllősi János (1953-) (biofizikus) Bene László (1963-) (biofizikus) Jenei Attila (1966-) (biofizikus) Nagy Péter (1971-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változa
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4.

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
Intézményi repozitóriumban (DEA) tárolt változa
Borító:

5.

001-es BibID:BIBFORM046282
Első szerző:Nagy Péter (biofizikus)
Cím:Ion-channel activities regulate transmembrane signaling in thymocyte apoptosis and T-cell activation / Nagy Péter, Panyi György, Jenei Attila, Bene László, Gáspár Rezső, Matkó János, Damjanovich Sándor
Dátum:1995
ISSN:0165-2478
Megjegyzések:Several examples have shown that plasma membrane ion channels (e.g., Ca2+ and K+ channels) make an important contribution to lymphocyte activation or thymocyte apoptosis. Here we report on the importance of these ion channels in the sensitivity or resistance of lymphoid cells to extracellular ATP-induced apoptosis. Thymocytes of Balb/c mice responded to extracellular ATP (ATPex) sensitively, with an immediate increase in the intracellular calcium level and later with an increased membrane permeability to low MW markers. Mature (medullary) thymocytes showed a higher sensitivity than did cortical thymocytes. Three human lymphoma cell lines, including SUPT13, a cell line reported to be sensitive to TcR/CD3 activation-induced apoptosis, showed a high resistance to ATPex action. These observations suggest that maturation/differentiation state-dependent activity or disappearance of early ATP-receptor operated signaling systems (including ion channels) are critical for the cells in developing towards apoptosis. Using the patch-clamp technique we demonstrated that bretylium tosylate (a particular K(+)-channel blocker) known as inhibitor of T-lymphocyte proliferation also influences the single-channel properties of voltage-gated K+ channels through depressing whole-cell K+ currents. This finding is yet another example underlying the importance of K+ channel activity in T-lymphocyte proliferation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Immunology Letters. - 44 : 2-3 (1995), p. 91-95. -
További szerzők:Panyi György (1966-) (biofizikus) Jenei Attila (1966-) (biofizikus) Bene László (1963-) (biofizikus) Gáspár Rezső (1921-2001) (fizikus) Matkó János (1952-) (biológus) Damjanovich Sándor (1936-2017) (biofizikus)
Pályázati támogatás:T14655
OTKA
F13335
OTKA
T6163
OTKA
T6221
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

6.

001-es BibID:BIBFORM004687
Első szerző:Nagy Péter (biofizikus)
Cím:Cell fusion experiments reveal distinctly different association characteristics of cell-surface receptors / Péter Nagy, László Mátyus, Attila Jenei, György Panyi, Sándor Varga, János Matkó, János Szöllősi, Rezső Gáspár, Thomas M. Jovin, Sándor Damjanovich
Dátum:2001
Megjegyzések:The existence of small- and large-scale membrane protein clusters, containing dimers, oligomers and hundreds of proteins, respectively, has become widely accepted. However, it is largely unknown whether the internal structure of these formations is dynamic or static. Cell fusion was used to perturb the distribution of existing membrane protein clusters, and to investigate their mobility and associations. Scanning near-field optical microscopy, confocal and electron microscopy were applied to detect the exchange of proteins between large-scale protein clusters, whereas photobleaching fluorescence energy transfer was used to image the redistribution of existing small-scale membrane protein clusters. Large-scale clusters of major histocompatibility complex (MHC)-I exchanged proteins with each other and with MHC-II clusters. Similarly to MHC-I, large-scale MHC-II clusters were also dynamic. Exchange of components between small-scale protein clusters was not universal: intermixing did not take place in the case of MHC-II homoclusters; however, it was observed for homoclusters of MHC-I and for heteroclusters of MHC-I and MHC-II. These processes required a fluid state of the plasma membrane, and did not depend on endocytosis-mediated recycling of proteins. The redistribution of large-scale MHC-I clusters precedes the intermixing of small-scale clusters of MHC-I indicating a hierarchy in protein association. Investigation of a set of other proteins (alpha subunit of the interleukin 2 receptor, CD48 and transferrin receptor) suggested that a large-scale protein cluster usually exchanges components with the same type of clusters. These results offer new insight into processes requiring time-dependent changes in membrane protein interactions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Biophysics
Cell Fusion
Cell Line
Cell Membrane
chemistry
Dyes
Energy Transfer
Fluorescence
Fluorescent Dyes
Gold Colloid
Histocompatibility Antigens
Histocompatibility Antigens Class I
Histocompatibility Antigens Class II
Human
Hungary
Interleukin-2
Major Histocompatibility Complex
Membrane Microdomains
metabolism
methods
Microscopy
Microscopy,Fluorescence
physiology
Proteins
Receptor Aggregation
Receptors,Cell Surface
Receptors,Interleukin-2
Support,Non-U.S.Gov't
Megjelenés:Journal of Cell Science 114 : Pt 22 (2001), p. 4063-4071. -
További szerzők:Mátyus László (1956-) (biofizikus) Jenei Attila (1966-) (biofizikus) Panyi György (1966-) (biofizikus) Varga Sándor (1943-) (biofizikus) Matkó János (1952-) (biológus) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Jovin, Thomas M. Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:elektronikus változat
Szerző által megadott URL
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7.

001-es BibID:BIBFORM004669
Első szerző:Nagy Péter (biofizikus)
Cím:Apoptosis of murine thymocytes induced by extracellular ATP is dose- and cytosolic pH-dependent / Nagy, P. V., Feher, T., Morga, S., Matko, J.
Dátum:2000
Megjegyzések:Thymocytes from young Balb/C mice responded to low extracellular ATP (ATPec) doses (0.3 mM) with a rapid intracellular acidification (mean pH: ca. 0.3 pH unit) that was inhibited by the Ca2+ channel blocker verapamil, or by suramin (50 gammaM) and TNP-ATP (40 gammaM), potent P2x (and P2y) purinoreceptor antagonists. ATPec also triggered a remarkable DNA fragmentation and cell shrinkage detectable only at these low doses. DNA fragmentation gradually disappears with increasing [ATPec] above 0.5 mM, with a concomitant dominance of cytosolic alkalinization of the cells. Suramin and TNP-ATP also blocked the ATPec-triggered DNA fragmentation efficiently. oATP, inhibitor of P2z nonspecific ATP-gated membrane pores, and 2 mM extracellular Mg2+ did not influence either the cytosolic acidification or the DNA fragmentation, but almost completely abolished the intracellular alkalinization characteristic of P2z receptor activation at high ATPec doses. Antagonist-sensitivity of the ATPec-induced membrane potential responses indicates that hyperpolarization is associated with intracellular acidification, while rapid depolarization is linked to alkalinization. These data together indicate that the Ca2+-dependent hyperpolarization and cytosolic acidification triggered by low ATPec doses are essential early signals in apoptosis of murine thymocytes and are likely mediated by P2x1 type ATP-gated ion channels. Subset specificity of the early purinergic signals suggests that the double positive thymocytes are most sensitive to ATPec showing both P2z and P2x receptor activation characteristics, the double negative thymocytes preferentially show P2z-type, while single positive (CD4-CD8+ or CD4+CD8-) thymocytes respond mostly by weaker P2x-type changes, indicating that ATPec, similarly to adenosine may serve as a potential regulator of cell death and differentiation in the thymus.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Apoptosis
Megjelenés:Immunology Letters. - 72 : 1 (2000), p. 23-30. -
További szerzők:Fehér Tamás Morga, Sabina Matkó János (1952-) (biológus)
Internet cím:elektronikus változat
DOI
Borító:

8.

001-es BibID:BIBFORM004743
035-os BibID:(scopus)0038492661 (wos)000184222500005
Első szerző:Vereb György (biofizikus, orvos)
Cím:Dynamic, yet structured : the cell membrane three decades after the Singer-Nicolson model / Vereb, G., Szollosi, J., Matko, J., Nagy, P., Farkas, T., Vigh, L., Matyus, L., Waldmann, T. A., Damjanovich, S.
Dátum:2003
ISSN:027-8424 (Print)
Megjegyzések:The fluid mosaic membrane model proved to be a very useful hypothesis in explaining many, but certainly not all, phenomena taking place in biological membranes. New experimental data show that the compartmentalization of membrane components can be as important for effective signal transduction as is the fluidity of the membrane. In this work, we pay tribute to the Singer-Nicolson model, which is near its 30th anniversary, honoring its basic features, "mosaicism" and "diffusion," which predict the interspersion of proteins and lipids and their ability to undergo dynamic rearrangement via Brownian motion. At the same time, modifications based on quantitative data are proposed, highlighting the often genetically predestined, yet flexible, multilevel structure implementing a vast complexity of cellular functions. This new "dynamically structured mosaic model" bears the following characteristics: emphasis is shifted from fluidity to mosaicism, which, in our interpretation, means nonrandom codistribution patterns of specific kinds of membrane proteins forming small-scale clusters at the molecular level and large-scale clusters (groups of clusters, islands) at the submicrometer level. The cohesive forces, which maintain these assemblies as principal elements of the membranes, originate from within a microdomain structure, where lipid-lipid, protein-protein, and protein-lipid interactions, as well as sub- and supramembrane (cytoskeletal, extracellular matrix, other cell) effectors, many of them genetically predestined, play equally important roles. The concept of fluidity in the original model now is interpreted as permissiveness of the architecture to continuous, dynamic restructuring of the molecular- and higher-level clusters according to the needs of the cell and as evoked by the environment.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Animals
Biophysics
Cell Membrane
chemistry
Chemistry,Physical
Diffusion
Extracellular Matrix
Fluorescence Resonance Energy Transfer
Hungary
Lipid Bilayers
Membrane Fluidity
Membrane Lipids
Membrane Microdomains
Membrane Proteins
Microscopy,Electron
Models,Biological
Motion
physiology
Proteins
Research
Signal Transduction
Support
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 100 : 14 (2003), p. 8053-8058. -
További szerzők:Szöllősi János (1953-) (biofizikus) Matkó János (1952-) (biológus) Nagy Péter (1971-) (biofizikus) Farkas Tamás (1971-) (biológus) Vígh L. Mátyus László (1956-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:DOI
elektronikus változat
Borító:
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