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1.

001-es BibID:BIBFORM046289
Első szerző:Bacsó Zsolt (biofizikus)
Cím:A photobleaching energy transfer analysis of CD8MHC-I and LFA-1ICAM-1 interactions in CTL-target cell conjugates / Bacsó Zsolt, Bene László, Bodnár Andrea, Matkó János, Damjanovich Sándor
Dátum:1996
ISSN:0165-2478
Megjegyzések:The photobleaching energy transfer (pbFRET) technique is a fluorescence method to measure proximity relationships between molecules, especially cell surface proteins, labeled with fluorophore-conjugated monoclonal antibodies, on a pixel-by-pixel base using digital imaging microscopy. This technique enables analysis of inter- and intramolecular proximities at cell surfaces at physiological conditions. We have developed a pbFRET approach to measure intercellular proximities in order to access spatial organization of interacting proteins in the contact region of two 'communicating' cells. Two examples, as possible application areas of this approach, are presented here: interaction between CD8 and MHC-I molecules in point contacts and interaction between LFA-1 and ICAM-1 molecules in focal contacts of CTL-target conjugates. The geometry of these protein contacts based on our resonance energy transfer (RET) data is consistent with the observed blocking effects of monoclonal antibodies (directed against the interacting proteins) on the cytolytic activity of CTLs and suggest a critical role for CD8beta-subunit in signal transmission in peripheral T-lymphocytes
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Immunology Letters. - 54 : 2-3 (1996), p. 151-156. -
További szerzők:Bene László (1963-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Matkó János (1952-) (biológus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
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2.

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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3.

001-es BibID:BIBFORM035548
Első szerző:Bacsó Zsolt (biofizikus)
Cím:Intercellular photobleaching energy transfer measurement monitoring recognition processes / Bacso, Z., Bene, L., Matko, J., Damjanovich, S.
Dátum:1996
ISSN:0079-6107
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
egyetemen (Magyarországon) készült közlemény
Megjelenés:Progress In Biophysics & Molecular Biology. - 65 : 1 (1996), p. PC122. -
További szerzők:Bene László (1963-) (biofizikus) Matkó János (1952-) (biológus) Damjanovich Sándor (1936-2017) (biofizikus)
Borító:

4.

001-es BibID:BIBFORM006064
035-os BibID:WOS:A1996UY72200007
Első szerző:Bacsó Zsolt (biofizikus)
Cím:Changes in membrane potential of target cells promotes cytotoxic activity of effector T lymphocytes / Zsolt Bacsó, János Matkó, János Szöllősi, Rezső Gáspár, Sándor Damjanovich
Dátum:1996
Megjegyzések:The effector function of CD8+ lymphocytes depends on recognition by the TcR-CD3 complex of an oligopeptide presented by an MHC class I molecule on target cells. Recently it has been shown that MHC class I molecules change their conformation upon depolarization of human B lymphoblastoid JY cells. We studied here the effects of changes in membrane potential of target cells on the function of cytotoxic T lymphocytes (CTL). Selective alterations of plasma membrane potential of JY target cells were achieved by treatments with specific ionophore molecules as well as with Na(+)-K(+)-ATPase inhibitor, while the cytotoxic lymphocytes were not influenced. The plasma membrane was depolarized by gramicidin D and ouabain, while hyperpolarization was induced by valinomycin treatment. Alterations of the resting membrane potential of target cells in both direction resulted in an enhanced cytotoxic activity. The observed changes in cytolytic activities of cytotoxic T effectors may have a more general biological significance, namely apoptotic cells become depolarized after a given time, moreover neoplastic and virus infected cells also frequently show decreased membrane potential. A more efficient recognition of these cells by CTL is supposed to enhance the efficiency of their elimination, as well.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Cytotoxicity,Immunologic
Human
Hungary
immunology
Lymphocytes
Membrane Potentials
Support,Non-U.S.Gov't
T-Lymphocytes
T-Lymphocytes,Cytotoxic
Tumor Cells,Cultured
Valinomycin
egyetemen (Magyarországon) készült közlemény
Megjelenés:Immunology Letters. - 51 : 3 (1996), p. 175-180. -
További szerzők:Matkó János (1952-) (biológus) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:elektronikus változat
DOI
Borító:

5.

001-es BibID:BIBFORM046086
Első szerző:Dóczy-Bodnár Andrea (biofizikus)
Cím:Class I HLA oligomerization at the surface of B cells is controlled by exogenous [béta]2-microglobulin : implications in activation of cytotoxic T lymphocytes / Bodnar A., Bacso Z., Jenei A., Jovin T. M., Edidin M., Damjanovich S., Matko J.
Dátum:2003
ISSN:1460-2377
Megjegyzések:Submicroscopic molecular clusters (oligomers) of class I HLA have been detected by physical techniques [e.g. fluorescence resonance energy transfer (FRET) and single particle tracking of molecular diffusion] at the surface of various activated and transformed human cells, including B lymphocytes. Here, the sensitivity of this homotypic association to exogenous beta(2)-microglobulin (beta(2)m) and the role of free heavy chains (FHC) in class I HLA oligomerization were investigated on a B lymphoblastoid cell line, JY. Scanning near-field optical microscopy and FRET data both demonstrated that FHC and class I HLA heterodimers are co-clustered at the cell surface. Culturing the cells with excess beta(2)m resulted in a reduced co-clustering and decreased molecular homotypic association, as assessed by FRET. The decreased HLA clustering on JY target cells (antigen-presenting cells) was accompanied with their reduced susceptibility to specific lysis by allospecific CD8(+) cytotoxic T lymphocytes (CTL). JY B cells with reduced HLA clustering also provoked significantly weaker T cell activation signals, such as lower expression of CD69 activation marker and lower magnitude of TCR down-regulation, than did the untreated B cells. These results together suggest that the actual level of beta(2)m available at the cell surface can control CTL activation and the subsequent cytotoxic effector function through regulation of the homotypic HLA-I association. This might be especially important in some inflammatory and autoimmune diseases where elevated serum beta(2)m levels are reported.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:International Immunology. - 15 : 3 (2003), p. 331-339. -
További szerzők:Bacsó Zsolt (1963-) (biofizikus) Jenei Attila (1966-) (biofizikus) Jovin, Thomas M. Edidin, Michael Damjanovich Sándor (1936-2017) (biofizikus) Matkó János (1952-) (biológus)
Pályázati támogatás:T034393
OTKA
T030411
OTKA
F034487
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:BIBFORM046091
Első szerző:Gombos Imre
Cím:Cholesterol sensitivity of detergent resistance : a rapid flow cytometric test for detecting constitutive or induced raft association of membrane proteins / Imre Gombos, Zsolt Bacsó, Cynthia Detre, Henrietta Nagy, Katalin Goda, Márton Andrásfalvy, Gábor Szabó, János Matkó
Dátum:2004
ISSN:0196-4763
Megjegyzések:Lipid rafts are cholesterol- and glycosphingolipid-rich microdomains in the cellular plasma membranes that play critical roles in compartmentalization (concentration, coupling, and isolation) of receptors and signal molecules. Therefore, detecting constitutive or induced raft associations of such proteins is of central interest in cell biology. This has mostly been done with time- and cell-consuming immunobiochemical techniques affected by several sources of artifacts. A flow cytometric analysis of immunocytochemical staining under differential circumstances of detergent treatment offers a new alternative to this method. METHODS: Membrane microdomains are resistant to nonionic detergents due to extensive, strong interactions between their molecular constituents. We used this feature to develop a rapid flow cytometric assay of differential detergent resistance based on immunocytochemical labeling of extracellular domain epitopes in membrane proteins. Data evaluation is based on comparative detection of their detergent solubility without and with cholesterol depletion of cell membranes, resolved by moderate concentrations of nonionic detergents. RESULTS: Nonionic detergents Triton X-100 and Nonidet-40 (0.05-0.1%) in cold or Brij-98 (0.1-0.5%) at 37 degrees C efficiently resolved detergent solubility or resistance of many lymphocyte cell surface proteins. Kinetic data revealed that a short (5-10 min) detergent treatment is sufficient for this assay. Comparison of detergent solubility in untreated and cholesterol-depleted cells differentiated membrane proteins associated with or excluded from raft microdomains, respectively. Confocal microscopy showed that this mild detergent treatment leaves the cytoskeleton of the cells intact, with a detectable expression of raft marker detergent-resistant proteins attached to it. An induced association with rafts of immunoglobulin E receptors upon antigen cross-linking was also easily detectable in rat mast cells by this approach. CONCLUSIONS: A protocol is proposed for a rapid (5-10 min) test of detergent resistance of membrane proteins in cells. The approach requires only a small amount of cells (10(4)/sample) and offers a good resolution of detergent solubility or resistance of membrane proteins, also in terms of the underlying mechanisms, with an advantage of applicability for all conventional bench-top flow cytometers.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cytometry. Part A. - 61A : 2 (2004), p. 117-126. -
További szerzők:Bacsó Zsolt (1963-) (biofizikus) Detre, Cynthia Nagy Henrietta Goda Katalin (1969-) (biofizikus) Andrásfalvy Márton Szabó Gábor (1953-) (biofizikus) Matkó János (1952-) (biológus)
Pályázati támogatás:T034393
OTKA
TS044711
OTKA
T032563
OTKA
T046945
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

7.

001-es BibID:BIBFORM035567
035-os BibID:WOS:000221319900021
Első szerző:Gombos Imre
Cím:Flow cytofluorimetric analysis of differential detergent resistance (FCDRA) : a rapid test of raft-association of membrane proteins / Gombos, I., Bacso, Zs., Detre, C., Szabo, G., Andrasfalvy, M., Prechl, J., Matko, J.
Dátum:2004
ISSN:1552-4922
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
egyetemen (Magyarországon) készült közlemény
Megjelenés:Cytometry Part A. - 59A :1 (2004), p. 30. -
További szerzők:Bacsó Zsolt (1963-) (biofizikus) Detre, Cynthia Szabó Gábor (1953-) (biofizikus) Andrásfalvy Márton Prechl József Matkó János (1952-) (biológus)
Borító:

8.

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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