Találati lista | Tudóstér

001-es BibID:	BIBFORM004658
Első szerző:	Burgess, Janette K.
Cím:	Physical proximity and functional association of glycoprotein 1balpha and protein-disulfide isomerase on the platelet plasma membrane / Burgess, J. K., Hotchkiss, K. A., Suter, C., Dudman, N. P., Szollosi, J., Chesterman, C. N., Chong, B. H., Hogg, P. J.
Dátum:	2000
Megjegyzések:	Platelet function is influenced by the platelet thiol-disulfide balance. Platelet activation resulted in 440% increase in surface protein thiol groups. Two proteins that presented free thiol(s) on the activated platelet surface were protein-disulfide isomerase (PDI) and glycoprotein 1balpha (GP1balpha). PDI contains two active site dithiols/disulfides. The active sites of 26% of the PDI on resting platelets was in the dithiol form, compared with 81% in the dithiol form on activated platelets. Similarly, GP1balpha presented one or more free thiols on the activated platelet surface but not on resting platelets. Anti-PDI antibodies increased the dissociation constant for binding of vWF to platelets by approximately 50% and PDI and GP1balpha were sufficiently close on the platelet surface to allow fluorescence resonance energy transfer between chromophores attached to PDI and GP1balpha. Incubation of resting platelets with anti-PDI antibodies followed by activation with thrombin enhanced labeling and binding of monoclonal antibodies to the N-terminal region of GP1balpha on the activated platelet surface. These observations indicated that platelet activation triggered reduction of the active site disulfides of PDI and a conformational change in GP1balpha that resulted in exposure of a free thiol(s).
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Antibodies blood Blood Platelets Cell Membrane chemistry Disulfides Energy Transfer enzymology Fluorescence Glycoproteins Human immunology Membrane Glycoproteins metabolism Molecular Weight pathology Platelet Activation Platelet Aggregation Platelet Membrane Glycoproteins Protein Disulfide-Isomerase Proteins Research Sulfhydryl Compounds Support, Non-U.S.Gov't Thrombin von Willebrand Factor
Megjelenés:	The Journal of Biological Chemistry. - 275 : 13 (2000), p. 9758-9766. -
További szerzők:	Hotchkiss, Kylie A. Suter, Catherine Dudman, Nicholas P. B. Szöllősi János (1953-) (biofizikus) Chesterman, Colin N. Chong, Beng H. Hogg, Philip J.
Internet cím:	elektronikus változat DOI
Borító:
Saját polcon:

001-es BibID:	BIBFORM004705
035-os BibID:	(scopus)18544371851 (wos)000173421300040
Első szerző:	Dornan, Saffron
Cím:	Differential association of CD45 isoforms with CD4 and CD8 regulates the actions of specific pools of p56lck tyrosine kinase in T cell antigen receptor signal transduction / Dornan, S., Sebestyen, Z., Gamble, J., Nagy, P., Bodnar, A., Alldridge, L., Doe, S., Holmes, N., Goff, L. K., Beverley, P., Szollosi, J., Alexander, D. R.
Dátum:	2002
Megjegyzések:	An investigation into the role of CD45 isoforms in T cell antigen receptor signal transduction was carried out by transfecting CD45-negative CD4(+)CD8(+) HPB-ALL T cells with the CD45R0, CD45RBC, and CD45RABC isoforms. Fluorescence resonance energy transfer analysis showed that the CD45R0 isoform, but not the CD45RBC or CD45RABC isoforms, was found as homodimers and also preferentially associated with CD4 and CD8 at the cell-surface. A comparison was therefore made of T cell antigen receptor signaling between sub-clones expressing either CD45R0 or CD45RBC. Under basal conditions CD4-associated p56(lck) tyrosine kinase activity and cellular protein tyrosine phosphorylation levels were higher in the CD45R0(+) than in the CD45RBC(+) sub-clones. Upon CD3-CD4 ligation, TCR-zeta phosphorylation, ZAP-70 recruitment to the p21/p23 TCR-zeta phosphoisomers, ZAP-70 phosphorylation, as well as p56(lck), c-Cbl and Slp-76 phosphorylation, were all markedly increased in CD45R0(+) compared with CD45RBC(+) cells. T cell antigen receptor (TCR) stimulation alone also promoted c-Cbl phosphorylation in CD45R0(+) but not in CD45RBC(+) cells. Our results are consistent with a model in which association of CD45R0 with CD4 generates a more active pool of CD4-associated p56(lck) kinase molecules. Upon CD3-CD4 co-ligation, the active p56(lck) increases the intensity of T cell antigen receptor signal transduction coupling by promoting TCR-zeta chain phosphorylation and ZAP-70 recruitment.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk analysis Antigens,CD4 Antigens,CD45 Antigens,CD8 Energy Transfer Fluorescence Human immunology Lymphocyte Specific Protein Tyrosine Kinase p56(lck) metabolism Phosphorylation Receptors,Antigen,T-Cell Signal Transduction Support,Non-U.S.Gov't
Megjelenés:	The Journal of Biological Chemistry. - 277 : 3 (2002), p. 1912-1918. -
További szerzők:	Sebestyén Zsolt Gamble, John Nagy Péter (1971-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Alldridge, Lou Doe, Senam Holmes, Nick Goff, Lindsey K. Beverley, Peter Szöllősi János (1953-) (biofizikus) Alexander, Denis R.
Internet cím:	elektronikus változat elektronikus változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM004734
Első szerző:	Mosesson, Yaron
Cím:	Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation / Mosesson, Y., Shtiegman, K., Katz, M., Zwang, Y., Vereb, G., Szollosi, J., Yarden, Y.
Dátum:	2003
ISSN:	021-9258 (Print)
Megjegyzések:	Growth factors stimulate specific receptor tyrosine kinases, but subsequent receptor endocytosis terminates signaling. The ubiquitin ligase c-Cbl targets epidermal growth factor receptors (EGFRs) to endocytosis by tagging them with multiple ubiquitin molecules. However, the type of ubiquitylation is unknown; whereas polyubiquitin chains signal proteasomal degradation, ubiquitin monomers control other processes. We report that in isolation c-Cbl mediates monoubiquitylation rather than polyubiquitylation of EGFRs. Consistent with the sufficiency of monoubiquitylation, when fused to the tail of EGFR, a single ubiquitin induces receptor endocytosis and degradation in cells. By using receptor and ubiquitin mutants, we infer that c-Cbl attaches a founder monoubiquitin to the kinase domain of EGFR and this is complemented by the conjugation of additional monoubiquitins. Hence, receptor tyrosine kinases are desensitized through conjugation of multiple monoubiquitins, which is distinct from polyubiquitin-dependent proteasomal degradation.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Animals Cells chemistry Cho Cells Cricetinae Electrophoresis,Polyacrylamide Gel Endocytosis Epidermal Growth Factor Genetic Vectors Immunoblotting Ligases metabolism Mice Microscopy,Fluorescence Plasmids Precipitin Tests Protein Structure,Tertiary Protein-Tyrosine Kinases Proteins Proto-Oncogene Proteins Proto-Oncogene Proteins c-cbl Receptor Protein-Tyrosine Kinases Research Support Time Factors Transfection Ubiquitin Ubiquitin-Protein Ligases
Megjelenés:	The Journal of Biological Chemistry. - 278 : 24 (2003), p. 21323-21326. -
További szerzők:	Shtiegman, K. Katz, M. Zwang, Y. Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus) Yarden, Yosef
Internet cím:	elektronikus változat elektronikus változat DOI
Borító:
Saját polcon:

001-es BibID:	BIBFORM004638
Első szerző:	Sullam, Paul M.
Cím:	Physical proximity and functional interplay of the glycoprotein Ib-IX-V complex and the Fc receptor FcgammaRIIA on the platelet plasma membrane / Sullam, P. M., Hyun, W. C., Szollosi, J., Dong, J., Foss, W. M., Lopez, J. A.
Dátum:	1998
ISSN:	021-9258
Megjegyzések:	Although the glycoprotein (GP) Ib-IX-V complex and FcgammaRIIA are distinct platelet membrane receptors, previous studies have suggested that these structures may be co-localized. To determine more directly the proximity of GP Ib-IX-V and FcgammaRIIA, we assessed the effects of anti-GP Ibalpha monoclonal antibodies on FcgammaRIIA-mediated platelet aggregation and on the direct binding of polymeric IgG to human platelets. In addition, we directly examined the proximity of FcgammaRII and GP Ib-IX-V using flow cytometric fluorescence energy transfer and immunoprecipitation studies. Preincubation of platelets with either of two monoclonal antibodies (AN51 or SZ2) directed against GP Ibalpha completely blocked platelet aggregation by polymeric IgG. Similarly, these antibodies totally inhibited platelet aggregation by two strains of viridans group streptococci known to induce aggregation via FcgammaRIIA. In addition, AN51 and SZ2 significantly reduced the binding of polymeric IgG to washed fixed platelets. When assessed by flow cytometry, significant levels of bidirectional energy transfer were detected between FcgammaRIIA and GP Ibalpha, indicating a physical proximity of less than 10 nm between these receptors. This energy transfer was not due to high receptor density, because no homoassociative energy transfer was seen. Moreover, immunoprecipitation of FcgammaRIIA from platelet lysates also co-precipitated GP Ibalpha. These results indicate that GP Ibalpha and FcgammaRIIA are co-localized on the platelet membrane and that this association is not random
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Antibodies Antibodies, Monoclonal Antigens, CD blood Blood Coagulation Factors Blood Platelets Cell Membrane drug effects Dyes Energy Transfer Flow Cytometry Fluorescence Fluorescent Dyes Human Immunoglobulin G immunology isolation and purification metabolism pharmacology Platelet Aggregation Platelet Glycoprotein GPIb-IX Complex Precipitin Tests Protein Binding Receptors, IgG Support, Non-U.S.Gov't Support, U.S.Gov't, P.H.S. ultrastructure
Megjelenés:	The Journal of Biological Chemistry. - 273 : 9 (1998), p. 5331-5336. -
További szerzők:	Hyun, William C. Szöllősi János (1953-) (biofizikus) Dong, Jing-fei Foss, Wendy M. Lopez, José A.
Internet cím:	elektronikus változat elektronikus változat
Borító:
Saját polcon: