CCL

Összesen 9 találat.
#/oldal:
Részletezés:
Rendezés:

1.

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:

2.

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:

3.

001-es BibID:BIBFORM086696
035-os BibID:(WoS)000553333300022 (Scopus)85088493600
Első szerző:Fadel, Lina (gyógyszerész)
Cím:Agonist binding directs dynamic competition among nuclear receptors for heterodimerization with retinoid X receptor / Lina Fadel, Bálint Rehó, Julianna Volkó, Dóra Bojcsuk, Zsuzsanna Kolostyák, Gergely Nagy, Gabriele Müller, Zoltán Simándi, Éva Hegedüs, Gábor Szabó, Katalin Tóth, Laszlo Nagy, György Vámosi
Dátum:2020
ISSN:0021-9258 1083-351X
Megjegyzések:Retinoid X receptor (RXR) plays a pivotal role as a transcriptional regulator and serves as an obligatory heterodimerization partner for at least 20 other nuclear receptors (NRs). Given a potentially limiting/sequestered pool of RXR and simultaneous expression of several RXR partners, we hypothesized that NRs compete for binding to RXR and that this competition may be directed by specific agonist treatment. Here, we tested this hypothesis on three NRs: peroxisome proliferator-activated receptor γ (PPARγ), vitamin D receptor (VDR), and retinoic acid receptor α (RARα). Evaluation of competition relied on a nuclear-translocation assay applied in a three-color imaging model system by detecting changes in heterodimerization between RXRα and one of its partners (NR1), in the presence of another competing partner (NR2). Our results indicated dynamic competition between the NRs governed by two mechanisms. First, in the absence of agonist treatment, there is a hierarchy of affinities between RXRα and its partners in the following order: RARα>PPARγ>VDR. Second, upon agonist treatment, RXRα favors the liganded partner. We conclude that recruiting RXRα by the liganded NR not only facilitates a stimulus-specific cellular response, but might also impede other NR pathways involving RXRα.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal of Biological Chemistry. - 295 : 29 (2020), p. 10045-10061. -
További szerzők:Rehó Bálint (1992-) Volkó Julianna (1983-) (biotechnológus) Bojcsuk Dóra (1990-) (klinikai laboratóriumi kutató) Kolostyák Zsuzsanna Nagy Gergely (1986-) (molekuláris biológus) Müller, Gabriele Simándi Zoltán (1984-) (Ph.D. hallgató, molekuláris biológus) Hegedűs Éva (1978-) (biofizikus) Szabó Gábor (1953-) (biofizikus) Tóth Katalin Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:NKFIH NN129371
egyéb
NKFIH KKP129909
egyéb
NKFIH K124298
egyéb
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
Borító:

4.

001-es BibID:BIBFORM015975
Első szerző:Liebl, Johanna
Cím:Cyclin-dependent Kinase 5 Regulates Endothelial Cell Migration and Angiogenesis / Johanna Liebl, Sabine B. Weitensteiner, György Vereb, Lili Takács, Robert Fürst, Angelika M. Vollmar, Stefan Zahler
Dátum:2010
ISSN:0021-9258
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal Of Biological Chemistry. - 285 : 46 (2010), p. 35932-35943. -
További szerzők:Weitensteiner, Sabine B. Vereb György (1965-) (biofizikus, orvos) Takács Lili (1969-) (szemész) Fürst Robert Vollmar, Angelika M. Zahler, Stefan
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

5.

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:

6.

001-es BibID:BIBFORM014036
Első szerző:Özvegy-Laczka Csilla
Cím:Interaction with the 5D3 Monoclonal Antibody Is Regulated by Intramolecular Rearrangements but Not by Covalent Dimer Formation of the Human ABCG2 Multidrug Transporter / Ozvegy-Laczka, C., Laczko, R., Hegedus, C., Litman, T., Varady, G., Goda, K., Hegedus, T., Dokholyan, N. V., Sorrentino, B. P., Varadi, A., Sarkadi, B.
Dátum:2008
ISSN:0021-9258
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
P-glycoprotein
Multidrug resistance
UIC2 monoclonal antibody
Megjelenés:Journal Of Biological Chemistry. - 283 : 38 (2008), p. 26059-26070. -
További szerzők:Laczkó Rozália Hegedűs Csilla Litman Thomas Várady György Goda Katalin (1969-) (biofizikus) Hegedűs Tamás Dokholyan, Nikolay V. Sorrentino, Brian P. Váradi András Sarkadi Balázs
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

7.

001-es BibID:BIBFORM107128
035-os BibID:(cikkazonosító)102896 (WoS)001009016200001 (Scopus)85147540608
Első szerző:Rehó Bálint
Cím:Agonist-controlled competition of RAR and VDR nuclear receptors for heterodimerization with RXR is manifested in their DNA-binding / Rehó Bálint, Fadel Lina, Brazda Peter, Benziane Anass, Hegedüs Éva, Sen Pialy, Gadella Theodorus W. Jr., Tóth Katalin, Nagy László, Vámosi György
Dátum:2023
ISSN:0021-9258 1083-351X
Megjegyzések:We found previously that nuclear receptors (NRs) compete for heterodimerization with their common partner, retinoid X receptor (RXR), in a ligand-dependent manner. To investigate potential competition in their DNA binding, we monitored the mobility of retinoic acid receptor (RAR) and vitamin D receptor (VDR) in live cells by fluorescence correlation spectroscopy. First, specific agonist treatment and RXR coexpression additively increased RAR DNA binding, while both agonist and RXR were required for increased VDR DNA binding, indicating weaker DNA binding of the VDR/RXR dimer. Second, coexpression of RAR, VDR, and RXR resulted in competition for DNA binding. Without ligand, VDR reduced the DNA-bound fraction of RAR and vice versa, i.e., a fraction of RXR molecules was occupied by the competing partner. The DNA-bound fraction of either RAR or VDR was enhanced by its own and diminished by the competing NR`s agonist. When treated with both ligands, the DNA-bound fraction of RAR increased as much as due to its own agonist, whereas that of VDR increased less. RXR agonist also increased DNA binding of RAR at the expense of VDR. In summary, competition between RAR and VDR for RXR is also manifested in their DNA binding in an agonist-dependent manner: RAR dominates over VDR in the absence of agonist or with both agonists present. Thus, side effects of NR-ligand-based (retinoids, thiazolidinediones) therapies may be ameliorated by other NR ligands and be at least partly explained by reduced DNA binding due to competition. Our results also complement the model of NR action by involving competition both for RXR and for DNA sites.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal Of Biological Chemistry. - 299 : 2 (2023), p. 1-16. -
További szerzők:Fadel, Lina (1988-) (gyógyszerész) Brázda Péter (1980-) (biológus, angol-magyar szakfordító) Benziane, Anass (1990-) (molekuláris biológus) Hegedűs Éva (1978-) (biofizikus) Sen, Pialy Gadella, Theodorus W. Jr. Tóth Katalin (biofizikus) Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00026
GINOP
NN129371
OTKA
ANN135107
OTKA
Tempus Public Foundation: Stipendium Hungaricum scholarship
Egyéb
German Academic Exchange Service and the Tempus Public Foundation #273478
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

8.

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:

9.

001-es BibID:BIBFORM005097
Első szerző:Szatmári István (biológus)
Cím:Peroxisome proliferator-activated receptor gamma-regulated ABCG2 expression confers cytoprotection to human dendritic cells / Szatmari, I., Vamosi, G., Brazda, P., Balint, B. L., Benko, S., Szeles, L., Jeney, V., Ozvegy-Laczka, C., Szanto, A., Barta, E., Balla, J., Sarkadi, B., Nagy, L.
Dátum:2006
ISSN:021-9258 (Print)
Megjegyzések:ABCG2, a member of the ATP-binding cassette transporters has been identified as a protective pump against endogenous and exogenous toxic agents. ABCG2 was shown to be expressed at high levels in stem cells and variably regulated during cell differentiation. Here we demonstrate that functional ABCG2 is expressed in human monocyte-derived dendritic cells by the activation of a nuclear hormone receptor, PPARgamma. We identified and characterized a 150-base pair long conserved enhancer region, containing three functional PPAR response elements (PPARE), upstream of the human ABCG2 gene. We confirmed the binding of the PPARgamma x RXR heterodimer to this enhancer region, suggesting that PPARgamma directly regulates the transcription of ABCG2. Consistent with these results, elevated expression of ABCG2 mRNA was coupled to enhanced protein production, resulting in increased xenobiotic extrusion capacity via ABCG2 in PPARgamma-activated cells. Furthermore PPARgamma instructed dendritic cells showed increased Hoechst dye extrusion and resistance to mitoxantrone. Collectively, these results uncovered a mechanism by which up-regulation of functional ABCG2 expression can be achieved via exogenous or endogenous activation of the lipid-activated transcription factor, PPARgamma. The increased expression of the promiscuous ABCG2 transporter can significantly modify the xenobiotic and drug resistance of human myeloid dendritic cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
agonists
Animals
antagonists & inhibitors
ATP-Binding Cassette Transporters
Base Sequence
biosynthesis
Cattle
Cell Differentiation
Cells
cytology
Cytoprotection
Dendritic Cells
Dogs
Drug Resistance
Drug Resistance,Neoplasm
genetics
Human
Humans
Hungary
metabolism
Mice
Molecular Sequence Data
Neoplasm Proteins
Phenotype
physiology
PPAR gamma
Proteins
Research
Support
Up-Regulation
Xenobiotics
Megjelenés:The Journal of Biological Chemistry. - 281 : 33 (2006), p. 23812-23823. -
További szerzők:Vámosi György (1967-) (biofizikus) Brázda Péter (1980-) (biológus, angol-magyar szakfordító) Bálint Bálint László (1971-) (kutató orvos) Benkő Szilvia (1973-) (molekuláris biológus) Széles Lajos (1971-) (molekuláris biológus) Jeney Viktória (1971-) (vegyész, kémia tanár) Özvegy-Laczka Csilla Szántó Attila (1976-) (orvos, biokémikus) Barta Endre (1963-) (molekuláris biológus) Balla József (1959-) (belgyógyász, nephrológus) Sarkadi Balázs Nagy László (1966-) (molekuláris sejtbiológus, biokémikus)
Internet cím:elektronikus változat
DOI
Borító:
Rekordok letöltése1 
Corvina könyvtári katalógus v8.2.27 © 2023 Monguz kft. Minden jog fenntartva.