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1.

001-es BibID:BIBFORM048680
Első szerző:Brázda Péter (biológus, angol-magyar szakfordító)
Cím:Live-cell fluorescence correlation spectroscopy dissects the role of coregulator exchange and chromatin binding in retinoic acid receptor mobility / Peter Brazda, Tibor Szekeres, Balázs Bravics, Katalin Tóth, György Vámosi, László Nagy
Dátum:2011
ISSN:0021-9533
Megjegyzések:The retinoic acid receptor (RAR) is a member of the nuclear receptor superfamily. This ligand-inducible transcription factor binds to DNA as a heterodimer with the retinoid X receptor (RXR) in the nucleus. The nucleus is a dynamic compartment and live-cell imaging techniques make it possible to investigate transcription factor action in real-time. We studied the diffusion of EGFP-RAR by fluorescence correlation spectroscopy (FCS) to uncover the molecular interactions determining receptor mobility. In the absence of ligand, we identified two distinct species with different mobilities. The fast component has a diffusion coefficient of D(1)=1.8-6.0 ?m(2)/second corresponding to small oligomeric forms, whereas the slow component with D(2)=0.05-0.10 ?m(2)/second corresponds to interactions of RAR with the chromatin or other large structures. The RAR ligand-binding-domain fragment also has a slow component, probably as a result of indirect DNA-binding through RXR, with lower affinity than the intact RAR-RXR complex. Importantly, RAR-agonist treatment shifts the equilibrium towards the slow population of the wild-type receptor, but without significantly changing the mobility of either the fast or the slow population. By using a series of mutant forms of the receptor with altered DNA- or coregulator-binding capacity we found that the slow component is probably related to chromatin binding, and that coregulator exchange, specifically the binding of the coactivator complex, is the main determinant contributing to the redistribution of RAR during ligand activation.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
transcription regulation
nuclear receptor
RAR
fluorescence correlation spectroscopy
Megjelenés:Journal of Cell Science. - 124 : 21 (2011), p. 3631-3642. -
További szerzők:Szekeres Tibor (1984-) (molekuláris biológus) Bravics Balázs Tóth Katalin Ágnes (1977-) (biokémikus, molekuláris biológus) Vámosi György (1967-) (biofizikus) Nagy László (1966-) (molekuláris sejtbiológus, biokémikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Magreceptorok
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Fehérje-fehérje kölcsönhatások limfociták membránjában és a sejtmagban
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM005177
Első szerző:de Bakker, Bärbel I.
Cím:Nanometer-scale organization of the alpha subunits of the receptors for IL2 and IL15 in human T lymphoma cells / de Bakker, B. I., Bodnar, A., van Dijk, E. M. H. P., Vamosi, G., Damjanovich, S., Waldmann, T. A., van Hulst, N. F., Jenei, A., Garcia-Parajo, M. F.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Cells
Human
Lymphoma
Biophysics
Hungary
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal of Cell Science. - 121 : 5 (2008), p. 627-633. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Dijk, Erik M. H. P., van Vámosi György (1967-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A. Hulst, Niek F., van Jenei Attila (1966-) (biofizikus) Garcia-Parajo, Maria F.
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Intézményi repozitóriumban (DEA) tárolt változat
DOI
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3.

001-es BibID:BIBFORM044572
Első szerző:Nagy Péter (biofizikus)
Cím:Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy / Péter Nagy, Attila Jenei, Achim K. Kirsch, János Szöllősi, Sándor Damjanovich, Thomas M. Jovin
Dátum:1999
Megjegyzések:ErbB2 (HER2, Neu), a member of the epidermal growth factor (EGF) receptor tyrosine kinase family, is often overexpressed in breast cancer and other malignancies. ErbB2 homodimerizes but also presents as a common auxiliary subunit of the EGF and heregulin receptors (erbB1 or EGFR; and erbB3-4, respectively), with which it heteroassociates. ErbB2 is generally regarded as an orphan (ligand-less) receptor with a very potent kinase domain activated either via its associated partners or constitutively as a consequence of discrete mutations. It follows that the extent and regulation of its cell surface interactions are of central importance. We have studied the large-scale association pattern of erbB2 in quiescent and activated cells labeled with fluorescent anti-erbB2 monoclonal antibodies using scanning near-field optical microscopy (SNOM). ErbB2 was found to be concentrated in irregular membrane patches with a mean diameter of approx. 0.5 microm in nonactivated SKBR3 and MDA453 human breast tumor cells. The average number of erbB2 proteins in a single cluster on nonactivated SKBR3 cells was about 10(3). Activation of SKBR3 cells with EGF, heregulin as well as a partially agonistic anti-erbB2 monoclonal antibody led to an increase in the mean cluster diameter to 0.6-0.9 microm, irrespective of the ligand. The EGF-induced increase in the erbB2 cluster size was inhibited by the EGFR-specific tyrosine kinase inhibitor PD153035. The average size of erbB2 clusters on the erbB2-transfected line of CHO cells (CB2) was similar to that of activated SKBR3 cells, a finding correlated with the increased base-line tyrosine phosphorylation of erbB2 in cells expressing only erbB2. We conclude that an increase in cluster size may constitute a general phenomenon in the activation of erbB2.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animal
antagonists and inhibitors
chemistry
Cho Cells
Enzyme Activation
Enzyme Inhibitors
Hamsters
Human
metabolism
methods
Microscopy
Microscopy, Atomic Force
Microscopy, Confocal
pharmacology
Quinazolines
Receptor Protein-Tyrosine Kinases
Receptor, Epidermal Growth Factor
Receptor, erbB-2
Support, Non-U.S.Gov't
Tumor Cells, Cultured
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal of Cell Science 112 : Pt 11 (1999), p. 1733-1741. -
További szerzők:Jenei Attila (1966-) (biofizikus) Kirsch, Achim K. Szöllősi János (1953-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Jovin, Thomas M.
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Szerző által megadott URL
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4.

001-es BibID:BIBFORM004713
035-os BibID:(scopus)0037112996 (wos)000179662300005
Első szerző:Nagy Péter (biofizikus)
Cím:Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2 / Nagy, P., Vereb, G., Sebestyen, Z., Horvath, G., Lockett, S. J., Damjanovich, S., Park, J. W., Jovin, T. M., Szollosi, J.
Dátum:2002
Megjegyzések:The ErbB family of transmembrane receptor tyrosine kinases plays an important role in the pathogenesis of many cancers. The four members of the family, ErbB1-4, form various homo- and heterodimers during the course of signal transduction. A second hierarchical level of molecular associations involving 10(2)-10(3) molecules, termed large-scale clustering, has also been identified, but the regulatory factors and biological consequences of such structures have not been systematically evaluated. In this report, we describe the states of association of ErbB2 and their relationship to local ErbB3 density and lipid rafts based on quantitative fluorescence microscopy of SKBR-3 breast cancer cells. Clusters of ErbB2 colocalized with lipid rafts identified by the GM1-binding B subunit of cholera toxin. Pixel-by-pixel analysis of fluorescence resonance energy transfer between labeled antibodies indicated that the homoassociation (homodimerization) of ErbB2 was proportional to the local density of ErbB2 and inversely proportional to that of ErbB3 and of the raft-specific lipid GM1. Crosslinking lipid rafts with the B subunit of cholera toxin caused dissociation of the rafts and ErbB2 clusters, an effect that was independent of the cytoskeletal anchoring of ErbB2. Crosslinking also decreased ErbB2-ErbB3 heteroassociation and the EGF- and heregulin-induced tyrosine phosphorylation of Shc. When cells were treated with the anti-ErbB2 monoclonal antibody 4D5 (parent murine version of Trastuzumab used in the immunotherapy of breast cancer), internalization of the antibody was inhibited by crosslinking of lipid rafts, but the antiproliferative activity of 4D5 was retained and even enhanced. We conclude that local densities of ErbB2 and ErbB3, as well as the lipid environment profoundly influence the association properties and biological function of ErbB2.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Adaptor Proteins,Signal Transducing
Adaptor Proteins,Vesicular Transport
analysis
Antibodies
Antibodies,Monoclonal
Antineoplastic Agents
Biophysics
Breast Neoplasms
Carcinoma
Cell Division
Cell Membrane
Cell Transformation,Neoplastic
Cells
Cholera Toxin
Cytoskeletal Proteins
Dimerization
drug effects
Energy Transfer
Eukaryotic Cells
Female
Fluorescence
Fluorescence Resonance Energy Transfer
genetics
Humans
Hungary
Macromolecular Substances
Membrane Microdomains
metabolism
Microscopy
Oncogene Proteins v-erbB
pharmacology
Phosphorylation
physiology
Protein Binding
Protein-Tyrosine Kinases
Proteins
Receptor Protein-Tyrosine Kinases
Receptor,erbB-2
Receptor,erbB-3
Receptors,Cell Surface
Research
Signal Transduction
Support
Tumor Cells,Cultured
ultrastructure
Megjelenés:Journal of Cell Science. - 115 : Pt 22 (2002), p. 4251-4262. -
További szerzők:Vereb György (1965-) (biofizikus, orvos) Sebestyén Zsolt Horváth Gábor (1974-) (biofizikus) Lockett, Steven J. Damjanovich Sándor (1936-2017) (biofizikus) Park, John W. Jovin, Thomas M. Szöllősi János (1953-) (biofizikus)
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5.

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)
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