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001-es BibID:	BIBFORM065104
035-os BibID:	(WoS)000380371400013 (Scopus)84993661764
Első szerző:	Mocsár Gábor (biofizikus)
Cím:	MHC I expression regulates co-clustering and mobility of interleukin-2 and -15 receptors in T cells / G. Mocsár, J. Volkó, D. Rönnlund, J. Widengren, P. Nagy, J. Szöllősi, K. Tóth, C. K. Goldman, S. Damjanovich, T. A. Waldmann, A. Bodnár, G. Vámosi
Dátum:	2016
ISSN:	0006-3495
Megjegyzések:	MHC glycoproteins form supramolecular clusters with interleukin-2 and -15 receptors in lipid rafts of T cells.The role of highly expressed MHC I in maintaining these clusters is unknown. We knocked down MHC I inFT7.10 human T cells, and studied protein clustering at two hierarchic levels: molecular aggregations andmobility by FRET and fluorescence correlation spectroscopy, and segregation into larger domains orsuperclusters by superresolution STED microscopy. FCS based molecular brightness analysis revealed thatthe studied molecules diffused as tight aggregates of several proteins of a kind. Knockdown reduced thenumber of MHC I containing molecular aggregates and their average MHC I content, and decreased theheteroassociation of MHC I with IL-2R?/IL-15R?. The mobility of not only MHC I but also that of IL-2R?/IL-15R? increased, corroborating the general size decrease of tight aggregates. A multifaceted analysis of STEDimages revealed that the diameter of MHC I superclusters diminished from 400-600 to 200-300 nm, whereasthose of IL-2R?/IL-15R? hardly changed. MHC I and IL-2R?/IL-15R? colocalized with GM1 gangliosiderichlipid rafts, but MHC I clusters retracted to smaller subsets of GM1- and IL-2R?/IL-15R?-rich areas uponknockdown. Our results prove that changes in expression level may significantly alter the organization andmobility of interacting membrane proteins.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Biophysical Journal. - 111 : 1 (2016), p. 100-112. -
További szerzők:	Volkó Julianna (1983-) (biotechnológus) Rönnlund, Daniel Widengren, Jerker Nagy Péter (1971-) (biofizikus) Szöllősi János (1953-) (biofizikus) Tóth Katalin (Heidelberg) Goldman, Caroline K. Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A. Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM006011
Első szerző:	Szöllősi János (biofizikus)
Cím:	Flow cytometric resonance energy transfer measurements support the association of a 95-kDa peptide termed T27 with the 55-kDa Tac peptide / J. Szöllösi, S. Damjanovich, C. K. Goldman, M. J. Fulwyler, A. A. Aszalos, G. Goldstein, P. Rao, M. A. Talle, T. A. Waldmann
Dátum:	1987
Megjegyzések:	Two monoclonal antibodies (OKT27 and OKT27b) have been produced that react with distinct epitopes of a 95-kDa peptide. The T27 antigen is widely distributed, being expressed on B lymphocytes, monocytes, and adult T-leukemic cells but not on polymorphonuclear leukocytes or platelets. There was a low level of T27 expression on resting T cells that increased on T-cell activation. In preliminary studies, the OKT27b antibody coprecipitated a 55-kDa peptide, as well as the 95-kDa peptide, from the radiolabeled cells of the HuT 102B2 cell line. Preclearance with anti-Tac, a monoclonal antibody to the 55-kDa peptide of the multichain interleukin 2 receptor, removed the 55-kDa but not the 95-kDa peptide from subsequent OKT27b immunoprecipitates of HuT 102B2 extracts, suggesting the possibility that the T27 peptide was associated with the Tac peptide. However, the precipitation of the p55 Tac peptide by OKT27b was quite inconsistent. Thus, additional information was sought using a flow cytometric energy transfer technique to provide a physical estimation of the proximity between the Tac and the T27 peptides. The flow cytometric version of the fluorescence resonance energy transfer technique permits the determination of inter- and intramolecular distances at 2- to 10-nm levels on a cell-by-cell basis. Using this approach, there was a mean energy transfer of 7.3% with HuT 102B2 cells when fluorescein isothiocyanate anti-Tac served as the donor and tetramethylrhodamine isothiocyanate OKT27 served as the acceptor. In contrast, there was no energy transfer in comparable studies observed when fluorescein anti-Tac and rhodamine anti-transferrin receptor antibodies were used. These observations support the conclusion that there is a close nonrandom proximity in HuT 102B2 cells between the 95-kDa peptide identified by the OKT27 monoclonal antibody and the p55 Tac peptide of the multichain interleukin 2 receptor.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Adult analysis Antibodies,Monoclonal Antigens,CD27 Antigens,Neoplasm Antigens,Surface B-Lymphocytes Biophysics Cell Line Energy Transfer Epitopes Flow Cytometry Fluorescence Human Hungary immunology Interleukin-2 Lymphocytes Monocytes Peptides Receptors,Immunologic Receptors,Interleukin-2 Support,Non-U.S.Gov't Support,U.S.Gov't,Non-P.H.S. T-Lymphocytes Tumor Cells,Cultured
Megjelenés:	Proceedings of the National Academy of Sciences of the United States of America. - 84 : 20 (1987), p. 7246-7250. -
További szerzők:	Damjanovich Sándor (1936-2017) (biofizikus) Goldman, Caroline K. Fulwyler, Mack J. Aszalos Adorján Goldstein, G. Rao, P. Talle, M. A. Waldmann, Thomas A.
Internet cím:	elektronikus változat
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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 Intézményi repozitóriumban (DEA) tárolt változat
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