CCL

Összesen 17 találat.
#/oldal:
Részletezés:
Rendezés:

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
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

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
Borító:

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: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:

5.

001-es BibID:BIBFORM004940
Első szerző:Damjanovich Sándor (biofizikus)
Cím:Preassembly of interleukin 2 (IL-2) receptor subunits on resting Kit 225 K6 T cells and their modulation by IL-2, IL-7, and IL-15 : a fluorescence resonance energy transfer study / Damjanovich, S., Bene, L., Matko, J., Alileche, A., Goldman, C. K., Sharrow, S., Waldmann, T. A.
Dátum:1997
ISSN:0027-8424
Megjegyzések:Assembly and mutual proximities of alpha, beta, and gamma(c) subunits of the interleukin 2 receptors (IL-2R) in plasma membranes of Kit 225 K6 T lymphoma cells were investigated by fluorescence resonance energy transfer (FRET) using fluorescein isothiocyanate- and Cy3-conjugated monoclonal antibodies (mAbs) that were directed against the IL-2R alpha, IL-2R beta, and gamma(c) subunits of IL-2R. The cell-surface distribution of subunits was analyzed at the nanometer scale (2-10 nm) by FRET on a cell-by-cell basis. The cells were probed in resting phase and after coculture with saturating concentrations of IL-2, IL-7, and IL-15. FRET data from donor- and acceptor-labeled IL-2R beta-alpha, gamma-alpha, and gamma-beta pairs demonstrated close proximity of all subunits to each other in the plasma membrane of resting T cells. These mutual proximities do not appear to represent mAb-induced microaggregation, because FRET measurements with Fab fragments of the mAbs gave similar results. The relative proximities were meaningfully modulated by binding of IL-2, IL-7, and IL-15. Based on FRET analysis the topology of the three subunits at the surface of resting cells can be best described by a "triangular model" in the absence of added interleukins. IL-2 strengthens the bridges between the subunits, making the triangle more compact. IL-7 and IL-15 act in the opposite direction by opening the triangle possibly because they associate their private specific alpha receptors with the beta and/or gamma(c) subunits of the IL-2R complex. These data suggest that IL-2R subunits are already colocalized in resting T cells and do not require cytokine-induced redistribution. This colocalization is significantly modulated by binding of relevant interleukins in a cytokine-specific manner.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Adult
analysis
Cell Membrane
chemistry
Energy Transfer
Fluorescence
Human
Interleukin-15
Interleukin-2
Interleukin-7
metabolism
pharmacology
Protein Conformation
Receptors,Interleukin-2
T-Lymphocytes
Tumor Cells,Cultured
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 94 : 24 (1997), p. 13134-13139. -
További szerzők:Bene László (1963-) (biofizikus) Matkó János (1952-) (biológus) Alileche, Abdelkrim Goldman, Caroline K. Sharrow, Susan Waldmann, Thomas A.
Internet cím:elektronikus változat
elektronikus változat
Borító:

6.

001-es BibID:BIBFORM004703
035-os BibID:(scopus)0037013728 (wos)000176059200014
Első szerző:Damjanovich Sándor (biofizikus)
Cím:Does mosaicism of the plasma membrane at molecular and higher hierarchical levels in human lymphocytes carry information on the immediate history of cells? / Damjanovich, S., Matyus, L., Damjanovich, L., Bene, L., Jenei, A., Matko, J., Gaspar, R., Szollosi, J.
Dátum:2002
Megjegyzések:A theoretical analysis of experimental data is presented in this mini-review on non-random homo- and hetero-associations of cell surface receptors, which can be recruited in the plasma membrane or at the surface of the rough endoplasmic reticulum during the protein synthesis. In the latter case, the likely genetic origin of these supramolecular formations is analyzed, contrasting this concept to the mobility of the cell surface proteins. A model is offered which, on the one hand, allows the mobility in a restricted way even among microdomain-confined receptor proteins through 'swapping partners'. On the other hand, the lack of mixing molecular components of protein clusters will be analyzed, when homo-and hetero-associations are studied through cell fusion experiments. The most frequently studied cell surface patterns have included lipid raft organized HLA class I and II, ICAM-1, tetraspan molecules, IL2 and IL15 and other receptors, as well. On the contrary coated pit-associated transferrin receptors would not mix with the above lipid raft associated receptor patterns, although transferrin receptor would readily oligomerize into homo-associates. The functional consequences of these superstructures are also analyzed. On the 30th anniversary of the Singer-Nicolson fluid mosaic membrane model one has to pay tribute to the authors, because of their deep insight emphasizing also the mosaicism of the membranes in general and that of the plasma membrane, in particular.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
analysis
Biophysics
Cell Fusion
Cells
Human
Hungary
Lymphocytes
Proteins
egyetemen (Magyarországon) készült közlemény
Megjelenés:Immunology Letters. - 82 : 1-2 (2002), p. 93-99. -
További szerzők:Mátyus László (1956-) (biofizikus) Damjanovich László (1960-) (általános sebész) Bene László (1963-) (biofizikus) Jenei Attila (1966-) (biofizikus) Matkó János (1952-) (biológus) Gáspár Rezső (1944-) (biofizikus) Szöllősi János (1953-) (biofizikus)
Internet cím:DOI
elektronikus változat
Borító:

7.

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)
Internet cím:DOI
elektronikus változat
Borító:

8.

001-es BibID:BIBFORM046291
Első szerző:Dóczy-Bodnár Andrea (biofizikus)
Cím:Modification of membrane cholesterol level affects expression and clustering of class I HLA molecules at the surface of JY human lymphoblasts / Bodnár Andrea, Jenei Attila, Bene László, Damjanovich Sándor, Matkó János
Dátum:1996
ISSN:0165-2478
Megjegyzések:Recently we have found that class I HLA molecules, key elements of the antigen presentation system for CD8 + effector cells, show a clustered lateral distribution (homoassociation) at the surface of activated human T- and B-lymphocytes as well as virus-transformed T- and B-lymphoblasts, in contrast to a disperse distribution on resting human PBLs (Matk6 et al. (1994) J. Immunol. 152, 3353; Bene et al. (1994) Eur. J. Immunol. 24, 2115). Expression of beta2m-free HLA heavy chains and exogenous beta2m have been shown as potential regulation factors of HLA-I clustering, which in turn may affect cytotoxic activity of CD8+ effector cells. Here we report a study on the effect of plasma membrane-modification (by exogenous cholesterol and phosphatidylcholine) on the expression of free HLA heavy chains and beta2m-bound HLA-I molecules on JY human B-lymphoblasts. The modulating effect of these two treatments on the lipid fluidity of cells was demonstrated by fluorescence anisotropy of DPH lipid probe. The lateral clustering (association) of HLA-I molecules was detected by flow cytometric fluorescence resonance energy transfer (FCET) and digital imaging microscopic photobleaching energy transfer (pbFRET) methods, using flourescein-isothiocyanate (FITC) (donor)- and tetramethyl-rhodamine-isothiocyanate (TRITC) (acceptor)-labeled W6/32 or KE2 antibodies directed against intact HLA-I molecules. Cholesterol enrichment of the plasma membrane increased membrane fluidity and reduced the expression of heavy- and light-chain determinants of HLA-I molecules and free heavy chains (FHCs). This was accompanied with a higher degree of HLA-I clustering as shown by the enhanced intermolecular energy transfer efficiency. In contrast, cholesterol depletion resulted in membrane fluidization and increased expression of HLA-I epitopes. Our results suggest that both cholesterol level and lipid structure/fluidity of the plasma membrane in lymphoblastoid cells may also potentially regulate lateral organization and consequently the presentation efficiency of HLA-I molecules.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Immunology Letters. - 54 : 2-3 (1996), p. 221-226. -
További szerzők:Jenei Attila (1966-) (biofizikus) Bene László (1963-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Matkó János (1952-) (biológus)
Pályázati támogatás:T6163
OTKA
6221
OTKA
17592
OTKA
F020102
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

9.

001-es BibID:BIBFORM004646
Első szerző:Erdei Anna
Cím:Inhibition of IgE-mediated triggering of mast cells by complement-derived peptides interacting with the Fc epsilon RI / Erdei, A., Toth, G. K., Andrasfalvy, M., Matko, J., Bene, L., Bajtay, Z., Ischenko, A., Rong, X., Pecht, I.
Dátum:1999
Megjegyzések:Mucosal type mast cells, in contrast to the serosal type ones, do not respond to cationic agents, or to the complement-derived peptides C3a and C5a. Earlier we have found that while C3a does not activate the rat mucosal type mast cells (line RBL-2H3), it strongly inhibits the IgE-mediated triggering of these cells, by interfering with the Fc epsilon RI-initiated signaling pathway. In the present study we further investigated the mechanism of this process. It is shown, that C3a interacts with the beta-chain of the Fc epsilon RI complex. Binding of the complement peptide to the cells apparently causes a decrease in the proximity of the IgE-binding Fc epsilon RI. Investigating certain sequences of C3a we found that the inhibition is caused by the C-terminal sequences of the complement-peptide, ranging from positions 56 to 77 and also by a shorter sequence, ranging from positions 56 to 64. The inhibitory effect of these peptides was observed both in the case of RBL-2H3 cells and mouse bone marrow derived mast cells
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Amino Acid Sequence
Animal
Bone Marrow Cells
Cells
Cells,Cultured
chemistry
Complement
Complement 3a
Hungary
Immunoglobulin E
immunology
Immunosuppressive Agents
Mast Cells
metabolism
Mice
Molecular Sequence Data
Peptides
pharmacology
physiology
Protein Conformation
Rats
Receptors, IgE
Support, Non-U.S.Gov't
Megjelenés:Immunology Letters. - 68 : 1 (1999), p. 79-82. -
További szerzők:Tóth Gábor K. Andrásfalvy Márton Matkó János (1952-) (biológus) Bene László (1963-) (biofizikus) Bajtay Zsuzsa Ischenko, Alexander Rong, Xu Pecht, Israel
Internet cím:DOI
elektronikus változat
elektronikus változat
Borító:

10.

001-es BibID:BIBFORM060604
035-os BibID:(scopus)0035871630 (wos)000170948300037
Első szerző:Gáspár Rezső (biofizikus)
Cím:Clustering of class I HLA oligomers with CD8 and TCR: three-dimensional models based on fluorescence resonance energy transfer and crystallographic data / Rezső Gáspár Jr., Péter Bagossi, László Bene, János Matkó, János Szöllősi, József Tőzsér, László Fésüs, Thomas A. Waldmann, Sándor Damjanovich
Dátum:2001
Megjegyzések:Fluorescence resonance energy transfer (FRET) data, in accordance with lateral mobility measurements, suggested the existence of class I HLA dimers and oligomers at the surface of live human cells, including the B lymphoblast cell line (JY) used in the present study. Intra- and intermolecular class I HLA epitope distances were measured on JY B cells by FRET using fluorophoreconjugated Ag-binding fragments of mAbs W6/32 and L368 directed against structurally well-characterized heavy and light chain epitopes, respectively. Out-of-plane location of these epitopes relative to the membrane-bound BODIPY-PC (2-(4,4-difluoro-5-(4- phenyl-1,3-butadienyl)-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycero-3-phosphocholine) was also determined by FRET. Computer-simulated docking of crystallographic structures of class I HLA and epitope-specific Ag-binding fragments, with experimentally determined interepitope and epitope to cell surface distances as constraints, revealed several sterically allowed and FRET-compatible class I HLA dimeric and tetrameric arrangements. Extension of the tetrameric class I HLA model with interacting TCR and CD8 resulted in a model of a supramolecular cluster that may exist physiologically and serve as a functionally significant unit for a network of CD8-HLA-I complexes providing enhanced signaling efficiency even at low MHC-peptide concentrations at the interface of effector and APCs.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal of immunology. - 166 : 8 (2001), p. 5078-5086. -
További szerzők:Bagossi Péter (1966-2011) (biokémikus, vegyész) Bene László (1963-) (biofizikus) Matkó János (1952-) (biológus) Szöllősi János (1953-) (biofizikus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Fésüs László (1947-) (orvos biokémikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
Pályázati támogatás:T029947
OTKA
F020590
OTKA
T019372
OTKA
T030399
OTKA
T023873
OTKA
T030411
OTKA
FKFP 327/2000
Egyéb
ETT T05/102/2000
Egyéb
FKFP 0518/99
Egyéb
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

11.

001-es BibID:BIBFORM004947
Első szerző:Kiss Erzsébet
Cím:Effect of TSH and anti-TSH receptor antibodies on the plasma membrane potential of polymorphonuclear granulocytes / Kiss, E., Balazs, C., Bene, L., Damjanovich, S., Matko, J.
Dátum:1997
ISSN:0165-2478
Megjegyzések:Effects of thyrotropin hormone (TSH) and anti-TSH receptor antibodies on the plasma membrane potential of polymorphonuclear granulocytes (PMN) were analyzed by means of flow cytometry. Both TSH and the autoantibody caused a rapid, dose-dependent hyperpolarization of the plasma membrane of PMNs. TSH was also able to mask (revert) the depolarizing effect of a chemotactic peptide, fMLP, on PMNs. No detectable rise in the cytosolic free calcium level accompanied the observed hyperpolarization. Quinine, a blocker of Ca(2+)-activated and voltage-gated K+ channels did not affect the hyperpolarization by TSH and antibodies. Decreasing the [K+] gradient across the plasma membrane by valinomycin, however, blocked the hyperpolarizing effect. Peptide362-376 (derived from the extracellular domain of TSH receptor) also blocked the hyperpolarization induced by both TSH and anti-TSHR antibodies. These data suggest that the observed hyperpolarization is a specific, receptor-mediated early signal during interaction of PMNs with TSH or anti-TSHR antibodies.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Amino Acid Sequence
Antibodies,Monoclonal
Autoantibodies
Calcium
Cell Membrane
chemistry
Dose-Response Relationship,Drug
drug effects
Flow Cytometry
Fluorescence Polarization
Human
Hungary
immunology
Membrane Potentials
metabolism
Molecular Sequence Data
N-Formylmethionine Leucyl-Phenylalanine
Neutrophils
Oligopeptides
pharmacology
physiology
Potassium
Potassium Channels
Quinine
Receptors,Thyrotropin
Support,Non-U.S.Gov't
Thyrotropin
ultrastructure
Valinomycin
Megjelenés:Immunology Letters. - 55 : 3 (1997), p. 173-177. -
További szerzők:Balázs Csaba Bene László (1963-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Matkó János (1952-) (biológus)
Internet cím:elektronikus változat
DOI
Borító:

12.

001-es BibID:BIBFORM039514
Első szerző:Matkó János (biológus)
Cím:GPI-microdomains (membrane rafts) and signaling of the multi-chain interleukin-2 receptor in human lymphoma/leukemia T cell lines / Matko, J., Bodnar, A., Vereb, G., Bene, L., Vamosi, G., Szentesi, G., Szollosi, J., Gaspar, R., Horejsi, V., Waldmann, T. A., Damjanovich, S.
Dátum:2002
ISSN:0014-2956
Megjegyzések:Subunits (alpha, beta and gamma) of the interleukin-2 receptor complex (IL-2R) are involved in both proliferative and activation-induced cell death (AICD) signaling of T cells. In addition, the signaling beta and gamma chains are shared by other cytokines (e.g. IL-7, IL-9, IL-15). However, the molecular mechanisms responsible for recruiting/sorting the alpha chains to the signaling chains at the cell surface are not clear. Here we show, in four cell lines of human adult T cell lymphoma/leukemia origin, that the three IL-2R subunits are compartmented together with HLA glycoproteins and CD48 molecules in the plasma membrane, by means of fluorescence resonance energy transfer (FRET), confocal microscopy and immuno-biochemical techniques. In addition to the beta and gamma(c) chains constitutively expressed in detergent-resistant membrane fractions (DRMs) of T cells, IL-2Ralpha (CD25) was also found in DRMs, independently of its ligand-occupation. Association of CD25 with rafts was also confirmed by its colocalization with GM-1 ganglioside. Depletion of membrane cholesterol using methyl-beta-cyclodextrin substantially reduced co-clustering of CD25 with CD48 and HLA-DR, as well as the IL-2 stimulated tyrosine-phosphorylation of STATs (signal transducer and activator of transcription). These data indicate a GPI-microdomain (raft)-assisted recruitment of CD25 to the vicinity of the signaling beta and gamma(c) chains. Rafts may promote rapid formation of a high affinity IL-2R complex, even at low levels of IL-2 stimulus, and may also form a platform for the regulation of IL-2 induced signals by GPI-proteins (e.g. CD48). Based on these data, the integrity of these GPI-microdomains seems critical in signal transduction through the IL-2R complex.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:European Journal Of Biochemistry. - 269 : 4 (2002), p. 1199-1208. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Bene László (1963-) (biofizikus) Vámosi György (1967-) (biofizikus) Szentesi Gergely (1976-) (kémia-fizika tanár) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Horejsi, Václav Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Rekordok letöltése1 2 
Corvina könyvtári katalógus v8.2.27 © 2023 Monguz kft. Minden jog fenntartva.