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001-es BibID:	BIBFORM004687
Első szerző:	Nagy Péter (biofizikus)
Cím:	Cell fusion experiments reveal distinctly different association characteristics of cell-surface receptors / Péter Nagy, László Mátyus, Attila Jenei, György Panyi, Sándor Varga, János Matkó, János Szöllősi, Rezső Gáspár, Thomas M. Jovin, Sándor Damjanovich
Dátum:	2001
Megjegyzések:	The existence of small- and large-scale membrane protein clusters, containing dimers, oligomers and hundreds of proteins, respectively, has become widely accepted. However, it is largely unknown whether the internal structure of these formations is dynamic or static. Cell fusion was used to perturb the distribution of existing membrane protein clusters, and to investigate their mobility and associations. Scanning near-field optical microscopy, confocal and electron microscopy were applied to detect the exchange of proteins between large-scale protein clusters, whereas photobleaching fluorescence energy transfer was used to image the redistribution of existing small-scale membrane protein clusters. Large-scale clusters of major histocompatibility complex (MHC)-I exchanged proteins with each other and with MHC-II clusters. Similarly to MHC-I, large-scale MHC-II clusters were also dynamic. Exchange of components between small-scale protein clusters was not universal: intermixing did not take place in the case of MHC-II homoclusters; however, it was observed for homoclusters of MHC-I and for heteroclusters of MHC-I and MHC-II. These processes required a fluid state of the plasma membrane, and did not depend on endocytosis-mediated recycling of proteins. The redistribution of large-scale MHC-I clusters precedes the intermixing of small-scale clusters of MHC-I indicating a hierarchy in protein association. Investigation of a set of other proteins (alpha subunit of the interleukin 2 receptor, CD48 and transferrin receptor) suggested that a large-scale protein cluster usually exchanges components with the same type of clusters. These results offer new insight into processes requiring time-dependent changes in membrane protein interactions.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Biophysics Cell Fusion Cell Line Cell Membrane chemistry Dyes Energy Transfer Fluorescence Fluorescent Dyes Gold Colloid Histocompatibility Antigens Histocompatibility Antigens Class I Histocompatibility Antigens Class II Human Hungary Interleukin-2 Major Histocompatibility Complex Membrane Microdomains metabolism methods Microscopy Microscopy,Fluorescence physiology Proteins Receptor Aggregation Receptors,Cell Surface Receptors,Interleukin-2 Support,Non-U.S.Gov't
Megjelenés:	Journal of Cell Science 114 : Pt 22 (2001), p. 4063-4071. -
További szerzők:	Mátyus László (1956-) (biofizikus) Jenei Attila (1966-) (biofizikus) Panyi György (1966-) (biofizikus) Varga Sándor (1943-) (biofizikus) Matkó János (1952-) (biológus) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Jovin, Thomas M. Damjanovich Sándor (1936-2017) (biofizikus)
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001-es BibID:	BIBFORM004673
Első szerző:	Vereb György (biofizikus, orvos)
Cím:	Cholesterol-dependent clustering of IL-2Ralpha and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts / Vereb, G., Matko, J., Vamosi, G., Ibrahim, S. M., Magyar, E., Varga, S., Szollosi, J., Jenei, A., Gaspar, R., Waldmann, T. A., Damjanovich, S.
Dátum:	2000
Megjegyzések:	Immunogold staining and electron microscopy show that IL-2 receptor alpha-subunits exhibit nonrandom surface distribution on human T lymphoma cells. Analysis of interparticle distances reveals that this clustering on the scale of a few hundred nanometers is independent of the presence of IL-2 and of the expression of the IL-2R beta-subunit. Clustering of IL-2Ralpha is confirmed by confocal microscopy, yielding the same average cluster size, approximately 600-800 nm, as electron microscopy. HLA class I and II and CD48 molecules also form clusters of the same size. Disruption of cholesterol-rich lipid rafts with filipin or depletion of membrane cholesterol with methyl-beta-cyclodextrin results in the blurring of cluster boundaries and an apparent dispersion of clusters for all four proteins. Interestingly, the transferrin receptor, which is thought to be located outside lipid rafts, exhibits clusters that are only 300 nm in size and are less affected by modifying the membrane cholesterol content. Furthermore, transferrin receptor clusters hardly colocalize with IL-2Ralpha, HLA, and CD48 molecules (crosscorrelation coefficient is 0.05), whereas IL-2Ralpha colocalizes with both HLA and CD48 (crosscorrelation coefficient is between 0.37 and 0.46). This coclustering is confirmed by electron microscopy. The submicron clusters of IL-2Ralpha chains and their coclustering with HLA and CD48, presumably associated with lipid rafts, could underlie the efficiency of signaling in lymphoid cells.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk analysis Antigens,CD Biophysics Cells Cholesterol HLA Antigens Human Hungary Immunohistochemistry Interleukin-2 Lymphoma Lymphoma,T-Cell Membrane Fluidity Membrane Lipids metabolism Microscopy Microscopy,Confocal Microscopy,Immunoelectron Neoplasm Proteins pathology physiology Proteins Receptors,Interleukin-2 Support,Non-U.S.Gov't T-Lymphocytes Tumor Cells,Cultured
Megjelenés:	Proceedings of the National Academy of Sciences of the United States of America. - 97 : 11 (2000), p. 6013-6018. -
További szerzők:	Matkó János (1952-) (biológus) Vámosi György (1967-) (biofizikus) Ibrahim, Shehu M. Magyar Erika Varga Sándor (1943-) (biofizikus) Szöllősi János (1953-) (biofizikus) Jenei Attila (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
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