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1.

001-es BibID:	BIBFORM004705
035-os BibID:	(scopus)18544371851 (wos)000173421300040
Első szerző:	Dornan, Saffron
Cím:	Differential association of CD45 isoforms with CD4 and CD8 regulates the actions of specific pools of p56lck tyrosine kinase in T cell antigen receptor signal transduction / Dornan, S., Sebestyen, Z., Gamble, J., Nagy, P., Bodnar, A., Alldridge, L., Doe, S., Holmes, N., Goff, L. K., Beverley, P., Szollosi, J., Alexander, D. R.
Dátum:	2002
Megjegyzések:	An investigation into the role of CD45 isoforms in T cell antigen receptor signal transduction was carried out by transfecting CD45-negative CD4(+)CD8(+) HPB-ALL T cells with the CD45R0, CD45RBC, and CD45RABC isoforms. Fluorescence resonance energy transfer analysis showed that the CD45R0 isoform, but not the CD45RBC or CD45RABC isoforms, was found as homodimers and also preferentially associated with CD4 and CD8 at the cell-surface. A comparison was therefore made of T cell antigen receptor signaling between sub-clones expressing either CD45R0 or CD45RBC. Under basal conditions CD4-associated p56(lck) tyrosine kinase activity and cellular protein tyrosine phosphorylation levels were higher in the CD45R0(+) than in the CD45RBC(+) sub-clones. Upon CD3-CD4 ligation, TCR-zeta phosphorylation, ZAP-70 recruitment to the p21/p23 TCR-zeta phosphoisomers, ZAP-70 phosphorylation, as well as p56(lck), c-Cbl and Slp-76 phosphorylation, were all markedly increased in CD45R0(+) compared with CD45RBC(+) cells. T cell antigen receptor (TCR) stimulation alone also promoted c-Cbl phosphorylation in CD45R0(+) but not in CD45RBC(+) cells. Our results are consistent with a model in which association of CD45R0 with CD4 generates a more active pool of CD4-associated p56(lck) kinase molecules. Upon CD3-CD4 co-ligation, the active p56(lck) increases the intensity of T cell antigen receptor signal transduction coupling by promoting TCR-zeta chain phosphorylation and ZAP-70 recruitment.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk analysis Antigens,CD4 Antigens,CD45 Antigens,CD8 Energy Transfer Fluorescence Human immunology Lymphocyte Specific Protein Tyrosine Kinase p56(lck) metabolism Phosphorylation Receptors,Antigen,T-Cell Signal Transduction Support,Non-U.S.Gov't
Megjelenés:	The Journal of Biological Chemistry. - 277 : 3 (2002), p. 1912-1918. -
További szerzők:	Sebestyén Zsolt Gamble, John Nagy Péter (1971-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Alldridge, Lou Doe, Senam Holmes, Nick Goff, Lindsey K. Beverley, Peter Szöllősi János (1953-) (biofizikus) Alexander, Denis R.
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2.

001-es BibID:	BIBFORM042484
035-os BibID:	(scopus)23844475901 (wos)000231845600013
Első szerző:	Mocanu, Maria-Magdalena
Cím:	Associations of ErbB2, beta1-integrin and lipid rafts on Herceptin (Trastuzumab) resistant and sensitive tumor cell lines / Maria-Magdalena Mocanu, Zsolt Fazekas, Miklós Petrás, Péter Nagy, Zsolt Sebestyén, Jorma Isola, József Tímár, John W. Park, György Vereb, János Szöllősi
Dátum:	2005
ISSN:	0304-3835
Megjegyzések:	ErbB2-mediated transmembrane signaling is a key target of novel anticancer agents such as Herceptin. Our comparison of Herceptin resistant (JIMT-1, MKN-7) and sensitive (SKBR-3, N-87) cell lines demonstrates the importance of ErbB2 association patterns involving integrins and lipid rafts. Flow cytometric FRET and confocal microscopic measurements revealed colocalization and molecular proximity between b1-integrins and ErbB2, as well as their association with lipid rafts. A weak functional interaction between ErbB2 and b1-integrin and the fact that ErbB2 did not co-patch with b1-integrins uponcrosslinking imply that ErbB2 and b1-integrin define two distinct molecular association clusters from a functional point of view. Although Herceptin-sensitive cell lines expressed more ErbB2 and fewer b1-integrin molecules on their surface than their resistant counterparts, this finding probably does not explain the Herceptin resistant phenotype due to the weak interaction between b1-integrins and ErbB2. Our results imply that the true significance of the expression profile of proteins involved inoncogenesis can only be understood after characterizing their molecular interactions.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Antibodies Antibodies,Monoclonal Antigens,CD29 Biophysics Breast Neoplasms Cell Line Cell Membrane Drug Resistance,Neoplasm Humans Hungary Membrane Microdomains metabolism pathology pharmacology Phenotype physiology Proteins Receptor,erbB-2 Research Support Tumor Cells,Cultured egyetemen (Magyarországon) készült közlemény
Megjelenés:	Cancer Letters. - 227 : 2 (2005), p. 201-212. -
További szerzők:	Fazekas Zsolt (1971-) (biofizikus) Petrás Miklós (1977-) (orvos) Nagy Péter (1971-) (biofizikus) Sebestyén Zsolt Isola, Jorma Timár József Park, John W. Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus)
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3.

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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4.

001-es BibID:	BIBFORM020768
Első szerző:	Roszik János (biofizikus)
Cím:	T-cell synapse formation depends on antigen recognition but not CD3 interaction : studies with TCR : zeta, a candidate transgene for TCR gene therapy / Roszik J., Sebestyén Z., Govers C., Guri Y., Szöor A., Pályi-Krekk Z., Vereb G., Nagy P., Szöllosi J., Debets R.
Dátum:	2011
Megjegyzések:	T-cell receptors (TCRs) can be genetically modified to improve gene-engineered T-cell responses, a strategy considered critical for the success of clinical TCR gene therapy to treat cancers. TCR:zeta, which is a heterodimer of TCRalpha and beta chains each coupled to complete human CD3zeta, overcomes issues of mis-pairing with endogenous TCR chains, shows high surface expression and mediates antigen-specific T-cell functions in vitro. In the current study, we further characterized TCR:zeta in gene-engineered T cells and assessed whether this receptor is able to interact with surface molecules and drive correct synapse formation in Jurkat T cells. The results showed that TCR:zeta mediates the formation of synaptic areas with antigen-positive target cells, interacts closely with CD8alpha and MHC class I (MHCI), and co-localizes with CD28, CD45 and lipid rafts, similar to WT TCR. TCR:zeta did not closely associate with endogenous CD3epsilon, despite its co-presence in immune synapses, and TCR:zeta showed enhanced synaptic accumulation in T cells negative for surface-expressed TCR molecules. Notably, synaptic TCR:zeta demonstrated lowered densities when compared with TCR in dual TCR T cells, a phenomenon that was related to both extracellular and intracellular CD3zeta domains present in the TCR:zeta molecule and responsible for enlarged synapse areas
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Adoptive Transfer Antigens Antigens,CD28 Antigens,CD3 Antigens,CD45 Antigens,CD8 article Biophysics Cells Flow Cytometry Gene Therapy genetics Histocompatibility Antigens Histocompatibility Antigens Class I Human Humans Hungary Immunity,Cellular Immunological Synapses immunology In Vitro Jurkat Cells lipid raft LIPID RAFTS Membrane Microdomains metabolism physiology Receptor-CD3 Complex,Antigen,T-Cell Receptors,Antigen,T-Cell,alpha-beta Research Research Support Support Synapses T-Lymphocytes therapy Transgenes
Megjelenés:	European Journal of Immunology. - 41 : 5 (2011), p. 1288-1297. -
További szerzők:	Sebestyén Zsolt Govers, Coen Guri, Yakir Szöőr Árpád (1984-) (orvos) Pályiné Krekk Zsuzsanna (1974-) (molekuláris biológus) Vereb György (1965-) (biofizikus, orvos) Nagy Péter (1971-) (biofizikus) Szöllősi János (1953-) (biofizikus) Debets, Reno
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5.

001-es BibID:	BIBFORM039658
035-os BibID:	(scopus)0036628631 (wos)000176656500002
Első szerző:	Sebestyén Zsolt
Cím:	Long wavelength fluorophores and cell-by-cell correction for autofluorescence significantly improves the accuracy of flow cytometric energy transfer measurements on a dual-laser benchtop flow cytometer / Zsolt Sebestyén, Péter Nagy, Gábor Horváth, György Vámosi, Reno Debets, Jan W. Gratama, Denis R. Alexander, János Szöllősi
Dátum:	2002
ISSN:	0196-4763
Megjegyzések:	Flow cytometric fluorescence resonance energy transfer (FCET) is an efficient method to map associations between biomolecules because of its high sensitivity to changes in molecular distances in the range of 1-10 nm. However, the requirement for a dual-laser instrument and the need for a relatively high signal-to-noise system (i.e., high expression level of the molecules) pose limitations to a wide application of the method.METHODS:Antibodies conjugated to cyanines 3 and 5 (Cy3 and Cy5) were used to label membrane proteins on the cell surface. FCET measurements were made on a widely used benchtop dual-laser flow cytometer, the FACSCalibur, by using cell-by-cell analysis of energy transfer efficiency.ResultsTo increase the accuracy of FCET measurements, we applied a long wavelength donor-acceptor pair, Cy3 and Cy5, which beneficially affected the signal-to-noise ratio in comparison with the classic pair of fluorescein and rhodamine. A new algorithm for cell-by-cell correction of autofluorescence further improved the sensitivity of the technique; cell subpopulations with only slightly different FCET efficiencies could be identified. The new FCET technique was tested on various direct and indirect immunofluorescent labeling strategies. The highest FCET values could be measured when applying direct labeling on both (donor and acceptor) sides. Upon increasing the complexity of the labeling scheme by introducing secondary antibodies, we detected a decrease in the energy transfer efficiency.CONCLUSIONS:We developed a new FCET protocol by applying long wavelength excitation and detection of fluorescence and by refining autofluorescence correction. The increased accuracy of the new method makes cells with low receptor expression amenable to FCET investigation, and the new approach can be implemented easily on a commercially available dual-laser flow cytometer, such as a FACSCalibur.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Algorithms analysis Antibodies Biophysics Calibration Cell Line, Transformed Cells Comparative Study Dyes Energy Transfer Flow Cytometry Fluorescein Fluorescence Fluorescence Resonance Energy Transfer Fluorescent Dyes Humans Hungary instrumentation Lasers Membrane Proteins methods Proteins Reproducibility of Results Research Spectrometry, Fluorescence Subtraction Technique Support Tumor Cells, Cultured egyetemen (Magyarországon) készült közlemény
Megjelenés:	Cytometry. - 48 : 3 (2002), p. 124-135. -
További szerzők:	Nagy Péter (1971-) (biofizikus) Horváth Gábor (1974-) (biofizikus) Vámosi György (1967-) (biofizikus) Debets, Reno Gratama, Jan Willem Alexander, Denis R. Szöllősi János (1953-) (biofizikus)
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6.

001-es BibID:	BIBFORM059568
Első szerző:	Szöllősi János (biofizikus)
Cím:	Applications of fluorescence resonance energy transfer for mapping biological membranes / János Szöllősi, Péter Nagy, Zsolt Sebestyén, Sándor Damjanovich, John W. Park, László Mátyus
Dátum:	2002
ISSN:	1389-0352
Megjegyzések:	The interaction of the cell surface proteins plays a key role in the process of transmembrane signaling. Receptor clustering and changes in their conformation are often essential factors in the final outcome of ligand receptor interactions. Fluorescence resonance energy transfer (FRET) is an excellent tool for determining distance relationships and supramolecular organization of cell surface molecules. This paper reviews the theoretical background of fluorescence resonance energy transfer, its flow cytometric and microscopic applications (including the intensity based and photobleaching versions), and provides a critical evaluation of the methods as well. In order to illustrate the applicability of the method, we summarize a few biological results: clustering of lectin receptors, cell surface distribution of hematopoietic cluster of differentiation (CD) molecules, and that of the receptor tyrosine kinases, conformational changes of Major Histocompatibility Complex (MHC) I molecules upon membrane potential change and ligand binding.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Biophysics Energy Transfer Fluorescence Hungary Major Histocompatibility Complex methods Proteins
Megjelenés:	Reviews in Molecular Biotechnology. - 82 : 3 (2002), p. 251-266. -
További szerzők:	Nagy Péter (1971-) (biofizikus) Sebestyén Zsolt Damjanovich Sándor (1936-2017) (biofizikus) Park, John W. Mátyus László (1956-) (biofizikus)
Pályázati támogatás:	OTKA-T30399 OTKA OTKA-T023835 OTKA
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