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001-es BibID:	BIBFORM079931
035-os BibID:	(cikkazonosító)3370 (scopus)85071327332 (wos)000477041100254
Első szerző:	Vámosi György (biofizikus)
Cím:	EGF Receptor Stalls upon Activation as Evidenced by Complementary Fluorescence Correlation Spectroscopy and Fluorescence Recovery after Photobleaching Measurements / Vámosi György, Friedländer-Brock Elza, Ibrahim Shehu M., Brock Roland, Szöllősi János, Vereb György
Dátum:	2019
ISSN:	1661-6596 1422-0067
Megjegyzések:	To elucidate the molecular details of the activation-associated clustering of epidermal growth factor receptors (EGFRs), the time course of the mobility and aggregation states of eGFP tagged EGFR in the membranes of Chinese hamster ovary (CHO) cells was assessed by in situ mobility assays. Fluorescence correlation spectroscopy (FCS) was used to probe molecular movements of small ensembles of molecules over short distances and time scales, and to report on the state of aggregation. The diffusion of larger ensembles of molecules over longer distances (and time scales) was investigated by fluorescence recovery after photobleaching (FRAP). Autocorrelation functions could be best fitted by a two-component diffusion model corrected for triplet formation and blinking. The slow, 100?1000 ms component was attributed to membrane localized receptors moving with free Brownian diffusion, whereas the fast, ms component was assigned to cytosolic receptors or their fragments. Upon stimulation with 50 nM EGF, a significant decrease from 0.11 to 0.07 ?m2/s in the diffusion coefficient of membrane-localized receptors was observed, followed by recovery to the original value in ~20 min. In contrast, the apparent brightness of diffusing species remained the same. Stripe FRAP experiments yielded a decrease in long-range molecular mobility directly after stimulation, evidenced by an increase in the recovery time of the slow component from 13 to 21.9 s. Our observations are best explained by the transient attachment of ligand-bound EGFRs to immobile or slowly moving structures such as the cytoskeleton or large, previously photobleached receptor aggregates.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Fluorescence correlation spectroscopy FCS fluorescence recovery after photobleaching FRAP epidermal growth factor receptor translational diffusion EGFR?eGFP fusion protein
Megjelenés:	International Journal Of Molecular Sciences. - 20 : 13 (2019), p. 1-22. -
További szerzők:	Friedländer Elza (1980-) (biofizikus) Ibrahim, Shehu M. Brock Roland Szöllősi János (1953-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
Pályázati támogatás:	K119690 OTKA NN129371 OTKA GINOP-2.3.2-15-2016-00050 GINOP GINOP-2.3.3-15-2016-00003 GINOP
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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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)
Internet cím:	elektronikus változat elektronikus változat
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