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1.

001-es BibID:BIBFORM076128
035-os BibID:(Wos)000450299400006 (Scopus)85055751019
Első szerző:Nizsalóczki Enikő
Cím:Minimum degree of overlap between IL-9R and IL-2R on human T lymphoma cells : a quantitative CLSM and FRET analysis / Nizsalóczki Enikő, Nagy Péter, Mocsár Gábor, Szabó Ágnes, Csomós István, Waldmann Thomas A., Vámosi György, Mátyus László, Bodnár Andrea
Dátum:2018
ISSN:1552-4922 1552-4930
Megjegyzések:The heterodimeric receptor complex of IL-9 consists of the cytokine-speci?c ?-subunit and the common ? -chain shared with other cytokines, including IL-2, a central regulator of T cell function. We have shown previously the bipartite spatial relationship of IL-9 and IL-2 receptors at the surface of human T lymphoma cells: in addition to common clusters, expression of the two receptor kinds could also be observed in segregated membrane areas. Here we analyzed further the mutual cell surface organization of IL-9 and IL-2 receptors. Complementing Pearson correlation data with co-occurrence analysis of confocal microscopic images revealed that a minimum degree of IL-9R/IL-2R co-localization exists at the cell surface regardless of the overall spatial correlation of the two receptor kinds. Moreover, our FRET experiments demonstrated molecular scale assemblies of the elements of the IL-9/IL-2R system. Binding of IL-9 altered the structure and/or composition of these clusters. It is hypothesized, that by sequestering receptor subunits in common membrane areas, the overlapping domains of IL-9R and IL-2R provide a platform enabling both the formation of the appropriate receptor complex as well as subunit sharing between related cytokines.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
IL-9 and -2 receptors
uorescence resonance energy transfer
Manders coef-cient
co-occurrence analysis
Pearson correlation analysis
confocal microscopy
human T lymphoma cells
co-localization of membrane proteins
Megjelenés:Cytometry Part A. - 93 : 11 (2018), p. 1106-1117. -
További szerzők:Nagy Péter (1971-) (biofizikus) Mocsár Gábor (1981-) (biofizikus) Nagyné Szabó Ágnes Timea (1982-) (vegyész) Csomós István (1983-) (molekuláris biológus) Waldmann, Thomas A. Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
GINOP-2.3.2-15-2016-00026
GINOP
GINOP-2.3.3-15-2016-00003
GINOP
K120302
OTKA
Intramural research program of the National Cancer Institute, NIH
Egyéb
Internet cím:Szerző által megadott URL
DOI
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2.

001-es BibID:BIBFORM057902
Első szerző:Nizsalóczki Enikő
Cím:Distinct spatial relationship of the interleukin-9 receptor with interleukin-2 receptor and major histocompatibility complex glycoproteins in human T lymphoma cells / Enikő Nizsalóczki, István Csomós, Péter Nagy, Zsolt Fazekas, Carolyn K. Goldman, Thomas A. Waldmann, Sándor Damjanovich, György Vámosi, László Mátyus, Andrea Bodnár
Dátum:2014
ISSN:1439-4235
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
confocal microscopy
membrane proteins
FRET
protein protein interactions
receptors
Molekuláris Medicina
Doktori iskola
Megjelenés:Chemphyschem. - 15 : 18 (2014), p. 3969-3978. -
További szerzők:Csomós István (1983-) (molekuláris biológus) Nagy Péter (1971-) (biofizikus) Fazekas Zsolt (1971-) (biofizikus) Goldman, Caroline K. Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Sejtfelszíni fehérjék szerveződése: az MHC I. szerepe
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Molekuláris Orvostudomány Doktori Iskola
TÁMOP-4.2.2.A-11/1/KONV-2012-0023
TÁMOP
TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
TÁMOP-4.2.4.A/2-11/1-2012-0001
TÁMOP
CK 78179
OTKA
K 103965
OTKA
K 103906
OTKA
NK 101337
OTKA
Baross Gábor Program REG-EA-09-1-2009-0010
Egyéb
Internal Research Program of the University of Debrecen RH/885/2013
Egyéb
Intramural Research Program of the National Cancer Institute, National Institutes of Health
Egyéb
Internet cím:Szerző által megadott URL
DOI
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3.

001-es BibID:BIBFORM004736
Első szerző:Panyi György (biofizikus)
Cím:Colocalization and nonrandom distribution of Kv1.3 potassium channels and CD3 molecules in the plasma membrane of human T lymphocytes / Panyi, G., Bagdany, M., Bodnar, A., Vamosi, G., Szentesi, G., Jenei, A., Matyus, L., Varga, S., Waldmann, T. A., Gaspar, R., Damjanovich, S.
Dátum:2003
ISSN:027-8424 (Print)
Megjegyzések:Distribution and lateral organization of Kv1.3 potassium channels and CD3 molecules were studied by using electron microscopy, confocal laser scanning microscopy, and fluorescence resonance energy transfer. Immunogold labeling and electron microscopy showed that the distribution of FLAG epitope-tagged Kv1.3 channels (Kv1.3/FLAG) significantly differs from the stochastic Poisson distribution in the plasma membrane of human T lymphoma cells. Confocal laser scanning microscopy images showed that Kv1.3/FLAG channels and CD3 molecules accumulated in largely overlapping membrane areas. The numerical analysis of crosscorrelation of the spatial intensity distributions yielded a high correlation coefficient (C = 0.64). A different hierarchical level of molecular proximity between Kv1.3/FLAG and CD3 proteins was reported by a high fluorescence resonance energy transfer efficiency (E = 51%). These findings implicate that reciprocal regulation of ion-channel activity, membrane potential, and the function of receptor complexes may contribute to the proper functioning of the immunological synapse.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
Antigens, CD3
Biophysics
biosynthesis
Cell Membrane
Cells
chemistry
Electrophysiology
Energy Transfer
Epitopes
Fluorescence
Fluorescence Resonance Energy Transfer
Human
Humans
Hungary
Immunohistochemistry
immunology
Jurkat Cells
Kv1.3 Potassium Channel
Lymphocytes
Lymphoma
metabolism
Mice
Microscopy
Microscopy, Confocal
Microscopy, Electron
Models, Statistical
Potassium
Potassium Channels
Potassium Channels, Voltage-Gated
Proteins
Research
Support
T-Lymphocytes
Transfection
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 100 : 5 (2003), p. 2592-2597. -
További szerzők:Bagdány Miklós Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus) Szentesi Gergely (1976-) (kémia-fizika tanár) Jenei Attila (1966-) (biofizikus) Mátyus László (1956-) (biofizikus) Varga Sándor (1943-) (biofizikus) Waldmann, Thomas A. Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:DOI
elektronikus változat
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4.

001-es BibID:BIBFORM046092
Első szerző:Vámosi György (biofizikus)
Cím:IL-2 and IL-15 receptor [alfa]-subunits are coexpressed in a supramolecular receptor cluster in lipid rafts of T cells / Vamosi G., Bodnar A., Vereb G., Jenei A., Goldman C. K., Langowski J., Toth K., Matyus L., Szollosi J., Waldmann T. A., Damjanovich S.
Dátum:2004
ISSN:0027-8424
Megjegyzések:The private alpha-chains of IL-2 and IL-15 receptors (IL-2R and IL-15R) share the signaling beta- and gamma(c)-subunits, resulting in both common and contrasting roles of IL-2 and IL-15 in T cell function. Knowledge of the cytokine-dependent subunit assembly is indispensable for understanding the paradox of distinct signaling capacities. By using fluorescence resonance energy transfer and confocal microscopy, we have shown that IL-2R alpha, IL-15R alpha, IL-2/15R beta and gamma(c)-subunits, as well as MHC class I and II glycoproteins formed supramolecular receptor clusters in lipid rafts of the T lymphoma line Kit 225 FT7.10. Fluorescence crosscorrelation microscopy demonstrated the comobility of IL-15R alpha with IL-2R alpha and MHC class I. A model was generated for subunit switching between IL-2R alpha and IL-15R alpha upon the binding of the appropriate cytokine resulting in the formation of high-affinity heterotrimeric receptors. This model suggests a direct role for the alpha-subunits, to which no definite function has been assigned so far, in tuning cellular responses to IL-2 or IL-15. In addition, both alpha-chains were at least partially homodimerized/oligomerized, which could be the basis of distinct signaling pathways by the two cytokines.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Proceedings Of The National Academy Of Sciences Of The United States Of America. - 101 : 30 (2004), p. 11082-11087. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Jenei Attila (1966-) (biofizikus) Goldman, Caroline K. Langowski, Jörg Tóth Katalin (biofizikus) Mátyus László (1956-) (biofizikus) Szöllősi János (1953-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
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5.

001-es BibID:BIBFORM004743
035-os BibID:(scopus)0038492661 (wos)000184222500005
Első szerző:Vereb György (biofizikus, orvos)
Cím:Dynamic, yet structured : the cell membrane three decades after the Singer-Nicolson model / Vereb, G., Szollosi, J., Matko, J., Nagy, P., Farkas, T., Vigh, L., Matyus, L., Waldmann, T. A., Damjanovich, S.
Dátum:2003
ISSN:027-8424 (Print)
Megjegyzések:The fluid mosaic membrane model proved to be a very useful hypothesis in explaining many, but certainly not all, phenomena taking place in biological membranes. New experimental data show that the compartmentalization of membrane components can be as important for effective signal transduction as is the fluidity of the membrane. In this work, we pay tribute to the Singer-Nicolson model, which is near its 30th anniversary, honoring its basic features, "mosaicism" and "diffusion," which predict the interspersion of proteins and lipids and their ability to undergo dynamic rearrangement via Brownian motion. At the same time, modifications based on quantitative data are proposed, highlighting the often genetically predestined, yet flexible, multilevel structure implementing a vast complexity of cellular functions. This new "dynamically structured mosaic model" bears the following characteristics: emphasis is shifted from fluidity to mosaicism, which, in our interpretation, means nonrandom codistribution patterns of specific kinds of membrane proteins forming small-scale clusters at the molecular level and large-scale clusters (groups of clusters, islands) at the submicrometer level. The cohesive forces, which maintain these assemblies as principal elements of the membranes, originate from within a microdomain structure, where lipid-lipid, protein-protein, and protein-lipid interactions, as well as sub- and supramembrane (cytoskeletal, extracellular matrix, other cell) effectors, many of them genetically predestined, play equally important roles. The concept of fluidity in the original model now is interpreted as permissiveness of the architecture to continuous, dynamic restructuring of the molecular- and higher-level clusters according to the needs of the cell and as evoked by the environment.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Animals
Biophysics
Cell Membrane
chemistry
Chemistry,Physical
Diffusion
Extracellular Matrix
Fluorescence Resonance Energy Transfer
Hungary
Lipid Bilayers
Membrane Fluidity
Membrane Lipids
Membrane Microdomains
Membrane Proteins
Microscopy,Electron
Models,Biological
Motion
physiology
Proteins
Research
Signal Transduction
Support
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 100 : 14 (2003), p. 8053-8058. -
További szerzők:Szöllősi János (1953-) (biofizikus) Matkó János (1952-) (biológus) Nagy Péter (1971-) (biofizikus) Farkas Tamás (1971-) (biológus) Vígh L. Mátyus László (1956-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:DOI
elektronikus változat
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