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1.

001-es BibID:BIBFORM005174
035-os BibID:(scopus)38349044364 (wos)000253278400023
Első szerző:Barok Márk (biofizikus)
Cím:Trastuzumab decreases the number of circulating and disseminated tumor cells despite trastuzumab resistance of the primary tumor / Márk Barok, Margit Balázs, Péter Nagy, Zsuzsa Rákosy, Andrea Treszl, Enikő Tóth, István Juhász, John W. Park, Jorma Isola, György Vereb, János Szöllősi
Dátum:2008
ISSN:304-3835 (Print)
Megjegyzések:We have recently shown that despite of the fact that the ErbB2-positive JIMT-1 human breast cancer cells intrinsically resistant to trastuzumab in vitro, trastuzumab inhibited the outgrowth of early phase JIMT-1 xenografts in SCID mice via antibody-dependent cellular cytotoxicity (ADCC). Here we show that trastuzumab significantly reduces the number of circulating and disseminated tumor cells (CTCs and DTCs) in this xenograft model system at a time when the primary tumor is already unresponsive to trastuzumab. This observation suggests that ErbB2 positive CTCs and DTCs might be sensitive to trastuzumab-mediated ADCC even if when the primary tumor is already non-responsive. Thus, trastuzumab treatment might also be beneficial in the case of patients with breast cancer that is already trastuzumab resistant.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
analysis
Animals
antagonists and inhibitors
Antibodies
Antibodies, Monoclonal
Antigens
Antigens, CD45
Antineoplastic Agents
article
Biophysics
blood
Bone Marrow
Breast Neoplasms
Cell Line, Tumor
Cells
Chromosomes, Human,X
drug effects
Drug Resistance, Neoplasm
drug therapy
EGFR
Epidermal Growth Factor
ErbB2
Female
genetics
Histocompatibility Antigens
Histocompatibility Antigens Class I
Human
Humans
Hungary
Immunohistochemistry
immunology
In Situ Hybridization,Fluorescence
In Vitro
metabolism
Mice
Mice, Scid
mouse
Neoplasm Circulating Cells
Neoplasm Metastasis
pathology
pharmacology
Receptor, Epidermal Growth Factor
Research
Research Support
Support
therapeutic use
Time Factors
Trastuzumab resistance
Xenograft Model Antitumor Assays
egyetemen (Magyarországon) készült közlemény
Megjelenés:Cancer Letters. - 260 : 1-2 (2008), p. 198-208. -
További szerzők:Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Nagy Péter (1971-) (biofizikus) Rákosy Zsuzsa (1978-) (sejtbiológus, molekuláris biológus, genetikus) Treszl Andrea (1974-) (molekuláris biológus) Tóth Enikő Juhász István (1956-) (bőrgyógyász, bőrsebész, kozmetológus, klinikai onkológus) Park, John W. Isola, Jorma Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus)
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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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DOI
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3.

001-es BibID:BIBFORM004878
035-os BibID:(scopus)26444586247 (wos)000232299300007
Első szerző:Nagy Péter (biofizikus)
Cím:Novel calibration method for flow cytometric fluorescence resonance energy transfer measurements between visible fluorescent proteins / Nagy, P., Bene, L., Hyun, W. C., Vereb, G., Braun, M., Antz, C., Paysan, J., Damjanovich, S., Park, J. W., Szollosi, J.
Dátum:2005
ISSN:1552-4922
Megjegyzések:The combination of fluorescence resonance energy transfer (FRET) and flow cytometry offers a statistically firm approach to study protein associations. Fusing green fluorescent protein (GFP) to a studied protein usually does not disturb the normal function of a protein, but quantitation of FRET efficiency calculated between GFP derivatives poses a problem in flow cytometry. METHODS: We generated chimeras in which cyan fluorescent protein (CFP) was separated by amino acid linkers of different sizes from yellow fluorescent protein (YFP) and used them to calibrate the cell-by-cell flow cytometric FRET measurements carried out on two different dual-laser flow cytometers. Then, CFP-Kip1 was coexpressed in yeast cells with YFP and cyclin-dependent kinase-2 (Cdk2) and served as a positive control for FRET measurements, and CFP-Kip1 coexpressed with a random peptide fused to YFP was the negative control. RESULTS: We measured donor, direct, and sensitized acceptor fluorescence intensities and developed a novel way to calculate a factor (alpha) that characterized the fluorescence intensity of acceptor molecules relative to the same number of excited donor molecules, which is essential for quantifying FRET efficiency. This was achieved by calculating FRET efficiency in two different ways and minimizing the squared difference between the two results by changing alpha. Our method reliably detected the association of Cdk2 with its inhibitor, Kip1, whereas the nonspecific FRET efficiency between Cdk2 and a random peptide was negligible. We identified and sorted subpopulations of yeast cells showing interaction between the studied proteins. CONCLUSIONS: We have described a straightforward novel calibration method to accurately quantitate FRET efficiency between GFP derivatives in flow cytometry
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
analysis
Biophysics
Calibration
Cells
chemistry
Cyclin-Dependent Kinase 2
Cyclin-Dependent Kinase Inhibitor p27
Energy Transfer
Flow Cytometry
Fluorescence
Fluorescence Resonance Energy Transfer
Hungary
metabolism
methods
Protein Binding
Proteins
Research
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Support
Megjelenés:Cytometry. Part A. - 67 : 2 (2005), p. 86-96. -
További szerzők:Bene László (1963-) (biofizikus) Hyun, William C. Vereb György (1965-) (biofizikus, orvos) Braun, Manuel Antz, Christof Paysan, Jacques Damjanovich Sándor (1936-2017) (biofizikus) Park, John W. Szöllősi János (1953-) (biofizikus)
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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)
Internet cím:elektronikus változat
elektronikus változat
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5.

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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6.

001-es BibID:BIBFORM039792
035-os BibID:(scopus)0036625779
Első szerző:Vereb György (biofizikus, orvos)
Cím:Signaling revealed by mapping molecular interactions : implications for ErbB-targeted cancer immunotherapies / György Vereb, Péter Nagy, John W. Park, János Szöllősi
Dátum:2002
ISSN:1529-1049
Megjegyzések:The ErbB2 (HER2) protein is a member of the EGF receptor (ErbB) family of transmembrane receptor tyrosine kinases. Although no direct ligand has yet been assigned to ErbB2, recent biochemical and biophysical evidence suggests that this protein operates as a shared receptor subunit with other ErbB proteins. Its medical importance stems form its frequent overexpression in breast and other cancers, resulting in various tumorigenic phenotypic changes, including higher transforming activity, metastatic potential, angiogenesis and drug resistance. The multitude of possible small-scale and large-scale interactions among the ErbB proteins makes them especially diverse and important in initiating and directing signal transduction. The mechanisms of homo- and hetero-associations among ErbB proteins in the cell membrane in relation to signal transduction events remain a critical focus of investigation. Recent studies to map the molecular interactions involved in the ErbB signaling network are elucidating these mechanisms, and promise to facilitate the development of new ErbB-targeted therapies, including approaches using antibodies, immunoliposomes, cancer vaccines, gene therapy and small molecule inhibitors.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
egyetemen (Magyarországon) készült közlemény
Megjelenés:Clinical and Applied Immunology Reviews. - 2 : 3 (2002), p. 169-186. -
További szerzők:Nagy Péter (1971-) (biofizikus) Park, John W. Szöllősi János (1953-) (biofizikus)
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DOI
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