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001-es BibID:BIBFORM004659
Első szerző:Dzoljic, M.
Cím:Ethanol and halothane differently modulate HLA class I and class II oligomerization : a new look at the mode of action of anesthetic agents through fluorescence spectroscopy / Dzoljic, M., Bene, L., Krasznai, Z., Damjanovich, S., Van Duijn, B.
Dátum:2000
Megjegyzések:The field of research considering the working mechanism of anesthetic agents is a complex one and the site or sites of action of general anesthetics are yet to be elucidated. Through the years, on the molecular level, the discussion has shifted from the lipid theories to the more specific interaction with the proteins responsible for the signal transduction. While this approach led to several models, they offer, at best, partial explanations for the observed phenomena. Anesthetic agents interact with many systems, of which the neuronal is best studied, leaving interaction with the immune defense system relatively unexplored. In this study we focus on the interaction of ethanol and halothane with the co-localization on the membrane of HLA I and II molecules. We show that ethanol tends to randomize the distribution of HLA I and II molecules, while halothane increases the clustering of HLA I proteins. The notion that anesthetics modulate cell function by disrupting clustering and thereby promoting a random distribution is a novel approach that may explain the general involvement of many systems during exposition to anesthetic drugs. In this study we show the disturbance of co-localization of molecules that may form a functional network. The relevance of this finding depends on the importance of these networks for extracellular and intracellular processes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Anesthetics, Inhalation
Antibodies, Monoclonal
B-Lymphocytes
Cell Line
chemistry
Comparative Study
drug effects
Energy Transfer
Ethanol
Fluorescence
Halothane
Histocompatibility Antigens Class I
Histocompatibility Antigens Class II
Human
Macromolecular Systems
methods
pharmacology
Research
Signal Transduction
Spectrometry, Fluorescence
Support, Non-U.S.Gov't
Megjelenés:Journal of Photochemistry and Photobiology. B, Biology. - 56 : 1 (2000), p. 48-52. -
További szerzők:Bene László (1963-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Duijn, B., Van
Internet cím:DOI
elektronikus változat
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2.

001-es BibID:BIBFORM004685
Első szerző:Mátyus László (biofizikus)
Cím:Organization of the glycoprotein (GP) IIb/IIIa heterodimer on resting human platelets studied by flow cytometric energy transfer / Matyus, L., Bene, L., Harsfalvi, J., Alvarez, M. V., Gonzalez-Rodriguez, J., Jenei, A., Muszbek, L., Damjanovich, S.
Dátum:2001
Megjegyzések:Glycoprotein IIb/IIIa is a heterodimer of glycoproteins IIb and IIIa which serves as the inducible receptor for fibrinogen and other adhesive proteins at the surface of platelets. Although a model of the quaternary structure of the GPIIb/IIIa molecule has been constructed in solution by Calvete et al. [Biochem. J. 282 (1992) 523], a corresponding model at the surface of intact platelets is still missing. In the present work conformation and lateral distribution of the GPIIb/IIIa heterodimer were studied at a nanometer resolution on the surface of resting human platelets under physiological conditions. The experiments were based on dual wavelength flow cytometric detection of fluorescence resonance energy transfer and application of a panel of monoclonal antibodies raised against well described binding sites. Monodisperse distribution of the GPIIb/IIIa heterodimer has been observed and a detailed three-dimensional proximity map of antibody binding sites was constructed on the platelet membrane, under physiological conditions, for the first time. Our data support the view that the GPIIb subunit is in a bent conformation. A detailed analysis of the K(d)-values and the number of binding sites for a set of monoclonal antibodies was also carried out giving supplementary data for the topology of the binding sites. Our results provide a refinement of the membrane-topology of the GPIIb/IIIa heterodimer.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animal
Antibodies,Monoclonal
Binding Sites
Blood Platelets
Dimerization
Energy Transfer
Flow Cytometry
Fluorescence
Glycoproteins
Human
Hungary
metabolism
Mice
Platelet Glycoprotein GPIIb-IIIa Complex
Support, Non-U.S.Gov't
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal of Photochemistry and Photobiology. B, Biology. - 65 : 1 (2001), p. 47-58. -
További szerzők:Bene László (1963-) (biofizikus) Hársfalvi Jolán (1949-) (klinikai biokémikus) Alvarez, M. V. Gonzalez-Rodriguez, J. Jenei Attila (1966-) (biofizikus) Muszbek László (1942-) (haematológus, kutató orvos) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:DOI
elektronikus változat
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