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001-es BibID:BIBFORM004628
035-os BibID:(scopus)0032190410 (wos)000076205700017
Első szerző:Damjanovich Sándor (biofizikus)
Cím:Supramolecular receptor structures in the plasma membrane of lymphocytes revealed by flow cytometric energy transfer, scanning force- and transmission electron-microscopic analyses / Damjanovich, S., Matko, J., Matyus, L., Szabo, G. jr., Szollosi, J., Pieri, J. C., Farkas, T., Gaspar, R.
Dátum:1998
ISSN:196-4763
Megjegyzések:Receptors in the plasma membrane of blood cells in general and in that of lymphocytes in particular are supposed to move around in a random walk fashion relatively freely driven by thermal diffusion, as described by the Singer-Nicolson fluid mosaic membrane model. In this article we summarized data and techniques that indicated nonrandom codistribution patterns of receptor superstructures under conditions, where the generation of such molecular colocalizations by the methods themselves were excluded. Application of fluorescence energy transfer in a flow cytometer helped to analyze such codistribution patterns in cell populations. After normalizing energy transfer values for possible differences between labeling ratios of the targeting monoclonal antibodies and using the mean values of energy transfer distribution curves, two-dimensional receptor maps were generated from data obtained in a pair-wise fashion between receptors. Major histocompatibility complex (MHC) class I and II, intercellular adhesion molecule-1 (ICAM-1), TcR-CD3-CD4, tetraspan molecules (CD81, CD82, CD53), and the subunits of the multisubunit IL-2 receptor displayed nonrandom codistribution patterns sometimes with, but very frequently without induction by their ligand. Immunogold-bead "sandwich" labeling analyzed by atomic force microscopy has shown that such receptor "islands" existed also in "receptor-island-groups". This indicated the existence of nonrandom receptor distribution of MHC class I and II molecules also at an elevated hierarchical level. An analysis is given herein concerning a standardized approach. The apparent incompatibility of these supramolecular patterns with the Singer-Nicolson type "free-protein and lipid-mobility paradigm" was resolved by recommending an additional emphasis on the mosaicism of the membrane besides receptor mobility.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
analysis
Antibodies
Antigens
Antigen
blood
Monoclonal
chemistry
Diffusion
Dyes
Energy Transfer
Flow Cytometry
Fluorescence
Fluorescent Dyes
HLA Antigens
Human
Hungary
Immunoglobulins
Fab
Immunohistochemistry
immunology
Intercellular Adhesion Molecule-1
Interleukin-2
Lymphocytes
Macromolecular Systems
Major Histocompatibility Complex
Membrane Fluidity
methods
Microscopy
Atomic Force
Microspheres
Modelsl
Motion
Receptor-CD3 Complex
T-Cell
Receptors
Cell Surface
Support
Non-U.S.Gov't
Tumor Cells
Cultured
Megjelenés:Cytometry. - 33 : 2 (1998), p. 225-233. -
További szerzők:Matkó János (1952-) (biológus) Mátyus László (1956-) (biofizikus) Szabó Gábor (1953-) (biofizikus) Szöllősi János (1953-) (biofizikus) Pieri, J. C. Farkas Tamás (1971-) (biológus) Gáspár Rezső (1944-) (biofizikus)
Internet cím:DOI
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2.

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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