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1.

001-es BibID:	BIBFORM004864
035-os BibID:	(scopus)26444452209 (wos)000232299300016
Első szerző:	Friedländer Elza (biofizikus)
Cím:	Signal transduction of erbB receptors in trastuzumab (Herceptin) sensitive and resistant cell lines : local stimulation using magnetic microspheres as assessed by quantitative digital microscopy / Friedlander, E., Arndt-Jovin, D. J., Nagy, P., Jovin, T. M., Szollosi, J., Vereb, G.
Dátum:	2005
ISSN:	1552-4922
Megjegyzések:	ErbB2 (HER-2), a member of the epidermal growth factor (EGF) receptor family, is a class I transmembrane receptor tyrosine kinase. Although erbB2 has no known physiologic ligand, it can form complexes with other members of the family and undergo transactivation of its very potent kinase activity, thereby initiating downstream signaling and cell proliferation. ErbB2 is a frequent pathologic marker in ductal invasive breast carcinomas and is targeted by using a specific humanized monoclonal antibody, trastuzumab (Herceptin). The antibody is effective in only 20% to 50% of erbB2-positive tumors, and this resistance, as yet poorly understood, constitutes a major therapeutic challenge. METHODS: Magnetic microspheres coated with ligands or antibodies are widely used for separation of proteins and cells and allow localized, high intensity, and precisely timed stimulation of cells. We used EGF- and trastuzumab-covered paramagnetic microspheres, quantitative confocal laser scanning microscopy, and digital image processing to investigate the (trans)activation of and local signal propagation from erbB1 and erbB2 on trastuzumab sensitive and resistant carcinoma cell lines expressing these receptors at high levels. RESULTS: On A431 cells expressing high levels of endogenous erbB1 and transfected erbB2-mYFP (A4-erbB2-mYFP F4 cell line), EGF-coupled-microspheres activated erbB1 and transactivated erbB2-mYFP. In two other cell lines with comparable erbB2 expression but lower levels of erbB1, EGF microspheres transactivated erbB2 less efficiently. Trastuzumab in solution activated erbB2 on A4-erbB2-mYFP and the trastuzumab sensitive SKBR-3 cells, but only negligibly on the resistant JIMT-1 cells that showed a 10 times higher K(d) for the antibody. Nevertheless, pronounced erbB2 activation and tyrosine phosphorylation could be detected after stimulation with trastuzumab-coupled microspheres in all cell lines, although transactivation of erbB1 was negligible. Receptor phosphorylation was restricted to the immediate proximity of the microspheres, i.e., receptor clusters external to these locations remained inactive. CONCLUSION: ErbB1 ligand and erbB2 specific antibody attached to magnetic microspheres are efficient tools in assessing erbB activation, localized signal propagation, and erbB heterodimer formation. Trastuzumab coupled to microspheres is more efficient at accessing erbB2 and activating it than trastuzumab in solution
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Animals Antibodies Antibodies,Monoclonal Biophysics Carcinoma Cell Line Cell Line,Tumor Cell Proliferation Cells chemistry drug effects Drug Resistance,Neoplasm Epidermal Growth Factor genetics Humans Hungary Ligands Magnetics metabolism methods Microscopy Microspheres pharmacology Phosphorylation Proteins Receptor,erbB-2 Research Signal Transduction Solubility Support Trans-Activation (Genetics)
Megjelenés:	Cytometry. Part A. - 67 : 2 (2005), p. 161-171. -
További szerzők:	Arndt-Jovin, Donna J. Nagy Péter (1971-) (biofizikus) Jovin, Thomas M. Szöllősi János (1953-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
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2.

001-es BibID:	BIBFORM004838
Első szerző:	Lidke, Diane S.
Cím:	Quantum dot ligands provide new insights into erbB/HER receptor-mediated signal transduction / Lidke, D. S., Nagy, P., Heintzmann, R., Arndt-Jovin, D., Post, J. N., Grecco, H. E., Jares-Erijman, E. A., Jovin, T. M.
Dátum:	2004
Megjegyzések:	The erbB/HER family of transmembrane receptor tyrosine kinases (RTKs) mediate cellular responses to epidermal growth factor (EGF) and related ligands. We have imaged the early stages of RTK-dependent signaling in living cells using: (i) stable expression of erbB1/2/3 fused with visible fluorescent proteins (VFPs), (ii) fluorescent quantum dots (QDs) bearing epidermal growth factor (EGF-QD) and (iii) continuous confocal laser scanning microscopy and flow cytometry. Here we demonstrate that EGF-QDs are highly specific and potent in the binding and activation of the EGF receptor (erbB1), being rapidly internalized into endosomes that exhibit active trafficking and extensive fusion. EGF-QDs bound to erbB1 expressed on filopodia revealed a previously unreported mechanism of retrograde transport to the cell body. When erbB2-monomeric yellow fluorescent protein (mYFP) or erbB3-monomeric Citrine (mCitrine) were coexpressed with erbB1, the rates and extent of endocytosis of EGF-QD and the RTK-VFP demonstrated that erbB2 but not erbB3 heterodimerizes with erbB1 after EGF stimulation, thereby modulating EGF-induced signaling. QD-ligands will find widespread use in basic research and biotechnological developments
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Animals Cell Membrane Cells chemistry Cricetinae Endocytosis Endosomes Epidermal Growth Factor Flow Cytometry Humans Ligands metabolism methods Microscopy Motion Oncogene Proteins v-erbB physiology Protein Binding Protein Interaction Mapping Protein Transport Proteins Quantum Dots Receptors, Cell Surface Research Signal Transduction Spectrometry, Fluorescence Support Tyrosine ultrastructure
Megjelenés:	Nature Biotechnology 22 : 2 (2004), p. 198-203. -
További szerzők:	Nagy Péter (1971-) (biofizikus) Heintzmann, Rainer Arndt-Jovin, Donna J. Post, Janine N. Grecco, Hernan E. Jares-Erijman, Elizabeth A. Jovin, Thomas M.
Internet cím:	elektronikus változat DOI
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3.

001-es BibID:	BIBFORM004732
Első szerző:	Lidke, Diane S.
Cím:	Imaging molecular interactions in cells by dynamic and static fluorescence anisotropy (rFLIM and emFRET) / D. S. Lidke, P. Nagy, B. G. Barisas, R. Heintzmann, J. N. Post, K. A. Lidke, A. H. A. Clayton, D. J. Arndt-Jovin, T. M. Jovin
Dátum:	2003
ISSN:	300-5127 (Print)
Megjegyzések:	We report the implementation and exploitation of fluorescence polarization measurements, in the form of anisotropy fluorescence lifetime imaging microscopy (rFLIM) and energy migration Forster resonance energy transfer (emFRET) modalities, for wide-field, confocal laser-scanning microscopy and flow cytometry of cells. These methods permit the assessment of rotational motion, association and proximity of cellular proteins in vivo. They are particularly applicable to probes generated by fusions of visible fluorescence proteins, as exemplified by studies of the erbB receptor tyrosine kinases involved in growth-factor-mediated signal transduction.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Animals Anisotropy Cell Line Cells chemistry Cho Cells Cricetinae Dose-Response Relationship, Drug Energy Transfer Epidermal Growth Factor Flow Cytometry Fluorescence Fluorescence Polarization Green Fluorescent Proteins Humans instrumentation Luminescent Proteins metabolism methods Microscopy Microscopy,Confocal Microscopy,Fluorescence Models,Statistical Motion Mutation Proteins Receptor,Epidermal Growth Factor Research Signal Transduction Support Tyrosine
Megjelenés:	Biochemical Society Transactions 31 : Pt 5 (2003), p. 1020-1027. -
További szerzők:	Nagy Péter (1971-) (biofizikus) Barisas, B. G. Heintzmann, Rainer Post, Janine N. Lidke, K. A. Clayton, A. H. A. Arndt-Jovin, Donna J. Jovin, Thomas M.
Internet cím:	elektronikus változat
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4.

001-es BibID:	BIBFORM002760
Első szerző:	Lidke, Diane S.
Cím:	Biotin-ligand complexes with sreptavidin quantum dots for in vivo cell labeling of membrane receptors / Lidke, D. S., Nagy P., Jovin, T. M., Arndt-Jovin, D.
Dátum:	2007
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Quantum Dots quantum dot methods
Megjelenés:	Methods in Molecular Biology. - 374 (2007), p. 69-79. -
További szerzők:	Nagy Péter (1971-) (biofizikus) Jovin, Thomas M. Arndt-Jovin, Donna J.
Internet cím:	elektronikus változat
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5.

001-es BibID:	BIBFORM002759
Első szerző:	Lidke, Diane S.
Cím:	In vivo imaging using quantum-dot-conjugated probes / Lidke, D. S., Nagy P., Arndt-Jovin, D. J.
Dátum:	2007
Megjegyzések:	This unit describes the use of quantum dots (QDs) for live-cell imaging and the use of QDs in flow cytometry for quantitative analysis of ligand binding constants and receptor density. Conventional fluorophores and visible fluorescent protein (VFP) constructs have allowed visualization of many cellular processes. However, organic and biomolecular fluorophores have limitations in their applications, due to their small Stokes' shift and tendency to photobleach during prolonged imaging. QDs have many advantages over conventional fluorophores, including high brightness and photostability, which make them an exceptional tool for live-cell imaging. There are a large variety of commercially available QDs with different surface reactivities and characteristics. The authors have limited the laboratory protocols presented here to the use of streptavidin-coupled QDs because this gives almost universal applicability to any cell surface receptor by coupling the ligand or antibody that recognizes the receptor to biotin and visualizing the complex by use of QDs
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban analysis Animal Animals Antibodies antibody combining site antigen antibody reaction Antigen-Antibody Reactions article Binding Sites Binding Sites,Antibody Biotinylation Cell Culture cell surface receptor Cells,Cultured Dyes dyes,reagents,indicators,markers and buffers Flow Cytometry fluorescence microscopy fluorescent dye Fluorescent Dyes Human Humans Indicators and Reagents instrumentation ligand Ligands metabolism methodology Mexico Mice Microscopy,Fluorescence microsphere Microspheres mouse quantum dot Quantum Dots Receptors,Cell Surface Streptavidin ultrastructure
Megjelenés:	Current Protocols in Cell Biology. - Supplement 36. (2007), unit 25.1.1-25.1.18. -
További szerzők:	Nagy Péter (1971-) (biofizikus) Arndt-Jovin, Donna J.
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:	BIBFORM015624
Első szerző:	Nagy Péter (biofizikus)
Cím:	Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis / Nagy, P., Claus, J., Jovin, T. M., Arndt-Jovin, D. J.
Dátum:	2010
Megjegyzések:	Ligand-driven dimerizations of ErbB receptor subunits fulfill a fundamental role in their activation. We have used the number and brightness analysis technique to investigate the existence of preformed ligand-independent dimers and clusters and to characterize the initial steps in the activation of ErbB1 and ErbB2. In cells expressing 50,000-200,000 receptors, ErbB1 was monomeric in the absence of ligand stimulation, whereas in CHO cells with receptor levels >500,000 as much as 30% of ErbB1 was present as preformed dimers. EGF induced the formation of ErbB1 dimers as well as larger clusters (up to pentamers) that colocalized with clathrin-coated pits. The distribution of unstimulated ErbB2 in cells expressing 3.10(5)-10(6) receptors was fundamentally different, in that this receptor was present in preformed homoassociated aggregates containing 5-10 molecules. These constitutive ErbB2 homoclusters colocalized with caveolae, increased in size at subphysiological temperatures, but decreased in size upon EGF stimulation. We conclude that these ErbB2 clusters are promoted primarily by membrane-mediated interactions and are dispersed upon ligand stimulation.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban A431 CELLS ACTIVATION analysis article Caveolae Cells Cho Cells CORRELATION SPECTROSCOPY CRYSTAL-STRUCTURE Dimerization EGFR ENERGY-TRANSFER Epidermal Growth Factor EPIDERMAL-GROWTH-FACTOR ErbB proteins ErbB1 ErbB2 FLUORESCENCE ANISOTROPY HIGHER-ORDER OLIGOMERS ligand LIPID RAFTS LIVING CELLS MOLECULAR-INTERACTIONS receptor clusters Receptor tyrosine kinase Signal Transduction Temperature Tyrosine OTKA::1 MAB::3.1
Megjelenés:	Proceedings of the National Academy of Sciences of the United States of America. - 107 : 38 (2010), p. 16524-16529. -
További szerzők:	Claus, J. Jovin, Thomas M. Arndt-Jovin, Donna J.
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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7.

001-es BibID:	BIBFORM004735
Első szerző:	Nagy Péter (biofizikus)
Cím:	Small interfering RNAs suppress the expression of endogenous and GFP-fused epidermal growth factor receptor (erbB1) and induce apoptosis in erbB1-overexpressing cells / Nagy, P., Arndt-Jovin, D. J., Jovin, T. M.
Dátum:	2003
ISSN:	014-4827 (Print)
Megjegyzések:	Deregulated and excessive expression of epidermal growth factor receptor (EGFR or erbB1), a transmembrane receptor tyrosine kinase specific for the epidermal growth factor (EGF), is a feature and/or cause of a wide range of human cancers, and thus inhibition of its expression is potentially therapeutic. In RNA interference (RNAi), duplexes of 21-nucleotide RNAs (small interfering RNA, siRNA) corresponding to mRNA sequences of particular genes are used to efficiently inhibit the expression of the target proteins in mammalian cells. Here we show that by using RNAi the expression of endogenous erbB1 can be specifically and extensively (90%) suppressed in A431 human epidermoid carcinoma cells. As a consequence, EGF-induced tyrosine phosphorylation was inhibited and cell proliferation was reduced due to induction of apoptosis. We established an inverse correlation between the level of expressed erbB1 and EGF sensitivity on a cell-by-cell basis using flow cytometry. A431 cells expressing endogenous erbB1 were transfected with erbB1 fused C-terminally to enhanced green fluorescent protein (EGFP). Selective inhibition of the expression of the fusion protein was achieved with an siRNA specific for the EGFP mRNA, whereas the erbB1-specific siRNAs inhibited the expression of both molecules. siRNA-mediated inhibition of erbB1 and other erbB tyrosine kinases may constitute a useful therapeutic approach in the treatment of human cancer.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Animals Apoptosis Carcinoma Cell Cycle Cell Line Cell Proliferation Cells chemistry Epidermal Growth Factor Flow Cytometry genetics Green Fluorescent Proteins Human Humans Indicators and Reagents Luminescent Proteins metabolism Microscopy,Fluorescence Phosphorylation physiology Proteins Receptor, Epidermal Growth Factor Recombinant Fusion Proteins Research RNA,Small Interfering Support Tyrosine
Megjelenés:	Experimental Cell Research. - 285 : 1 (2003), p. 39-49. -
További szerzők:	Arndt-Jovin, Donna J. Jovin, Thomas M.
Internet cím:	DOI elektronikus változat
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