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1.

001-es BibID:BIBFORM004861
035-os BibID:(scopus)14644392200 (wos)000227768400023
Első szerző:Diermeier, Simone
Cím:Epidermal growth factor receptor coexpression modulates susceptibility to Herceptin in HER2/neu overexpressing breast cancer cells via specific erbB-receptor interaction and activation / Diermeier, S., Horvath, G., Knuechel-Clarke, R., Hofstaedter, F., Szollosi, J., Brockhoff, G.
Dátum:2005
ISSN:0014-4827
Megjegyzések:Growth factors and Herceptin specifically and differentially modulate cell proliferation of tumor cells. However, the mechanism of action on erbB-receptor level is incompletely understood. We evaluated Herceptin's capacity to modulate erbB-receptor activation and interaction on the cell surface level and thereby potentially impair cell proliferation of HER2/neu (c-erbB2) overexpressing breast cancer cells, both in the presence and absence of relevant growth factors. METHODS: BT474 and SK-BR-3 breast cancer cell lines were treated with Epidermal Growth Factor (EGF), Heregulin, and with Herceptin in different combinations. Kinetics of cell proliferation were evaluated flow cytometrically based on BrdU-labeling. Fluorescence Resonance Energy Transfer, ELISAs and phosphorylation site specific Western Blotting was performed to investigate erbB-receptor interaction and activation. RESULTS: EGF induced EGFR/EGFR and EGFR/c-erbB2 interactions correlate with stimulation of cell proliferation in BT474 cells. Both homo- and heterodimerization are considerably less pronounced in SK-BR-3 cells and heterointeraction is additionally reduced by EGF treatment, causing inhibition of cell proliferation. Heregulin stimulates cell proliferation extensively in both cell lines. Herceptin drives BT474 cells more efficiently into quiescence than it does with SK-BR-3 cells and thereby blocks cell cycle progress. In SK-BR-3 Herceptin treatment causes c-erbB2 phosphorylation of Y877 and Y1248, EGF induces Y877 and Y1112 phosphorylation. The Y1112 phosphorylation site, activated by EGF in SK-BR-3 cell, is bypassed in BT474. In addition the inhibitory capacity of Herceptin on BT474 and SK-BR-3 cell proliferation depends on the presence and absence of growth factors to a various extent. CONCLUSION: The growth inhibitory effect of Herceptin on c-erbB2 overexpressing breast cancer cells is considerably modulated by EGFR coexpression and consequently EGFR/c-erbB2 homo- and heterointeractions, as well as the presence or absence of growth factors. C-erbB2 overexpression alone is insufficient to predict the impact of growth factors and antibodies on cell proliferation. The optimization and specification of therapeutic approaches based on erbB-receptor targeting requires to account for EGFR coexpression as well as the potential presence of erbB-receptor relevant growth factors.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Antibodies
Antibodies,Monoclonal
Antineoplastic Agents
Breast Neoplasms
Carcinoma
Cell Cycle
Cell Cycle Proteins
Cell Line
Cell Line, Tumor
Cell Proliferation
Cells
drug effects
Drug Resistance,Neoplasm
Drug Synergism
drug therapy
Energy Transfer
Epidermal Growth Factor
Female
Fluorescence
Fluorescence Resonance Energy Transfer
genetics
Growth Inhibitors
Humans
Kinetics
metabolism
methods
Neuregulin-1
pathology
pharmacology
Phosphorylation
physiology
Proteins
Receptor, Epidermal Growth Factor
Receptor, erbB-2
Receptors, Cell Surface
Research
Support
therapeutic use
Megjelenés:Experimental Cell Research. - 304 : 2 (2005), p. 604-619. -
További szerzők:Horváth Gábor (1974-) (biofizikus) Knuechel-Clarke, Ruth Hofstaedter, Ferdinand Szöllősi János (1953-) (biofizikus) Brockhoff, Gero
Internet cím:elektronikus változat
DOI
Borító:

2.

001-es BibID:BIBFORM003553
Első szerző:Kakuk Annamária (molekuláris biológus)
Cím:Nuclear and nucleolar localization signals and their targeting function in phosphatidylinositol 4-kinase PI4K230 / Kakuk A., Friedlander E., Vereb Gy. Jr., Lisboa, D., Bagossi P., Tóth G., Gergely P., Vereb Gy.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
phosphatidylinositol 4-kinase
PI4K230
nuclear localization signal
NLS
nucleolar targeting
NTS
importins
permeabilized HeLa cells
import assay
Megjelenés:Experimental Cell Research. - 314 : 13 (2008), p. 2376-2388. -
További szerzők:Friedländer Elza (1980-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Lisboa, Duarte (1982-) (biotechnológus) Bagossi Péter (1966-2011) (biokémikus, vegyész) Tóth Gábor Gergely Pál (1947-) (biokémikus) Vereb György (1938-) (biokémikus, sejtbiológus)
Internet cím:elektronikus változat
DOI
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3.

001-es BibID:BIBFORM039005
035-os BibID:PMID:15572026
Első szerző:Kashuba, Elena
Cím:Epstein-Barr virus-encoded EBNA-5 binds to Epstein-Barr virus-induced Fte1/S3a protein / Elena Kashuba, Mariya Yurchenko, Krisztina Szirák, Joachim Stahl, George Klein, László Székely
Dátum:2005
ISSN:0014-4827
Megjegyzések:Epstein-Barr virus (EBV) transforms resting human B cells into immortalized immunoblasts. EBV-encoded nuclear antigens EBNA-5 (also called EBNA-LP) is one of the earliest viral proteins expressed in freshly infected B cells. We have recently shown that EBNA-5 binds p14ARF, a nucleolar protein that regulates the p53 pathway. Here, we report the identification of another protein with partially nucleolar localization, the v-fos transformation effector Fte-1 (Fte-1/S3a), as an EBNA-5 binding partner. In transfected cells, Fte-1/S3a and EBNA-5 proteins showed high levels of colocalization in extranucleolar inclusions. Fte-1/S3a has multiple biological functions. It enhances v-fos-mediated cellular transformation and is part of the small ribosomal subunit. It also interacts with the transcriptional factor CHOP and apoptosis regulator poly(ADP-ribose) polymerase (PARP). Fte-1/S3a is regularly expressed at high levels in both tumors and cancer cell lines. Its high expression favors the maintenance of malignant phenotype and undifferentiated state, whereas its down-regulation is associated with cellular differentiation and growth arrest. Here, we show that EBV-induced B cell transformation leads to the up-regulation of Fte-1/S3a. We suggest that EBNA-5 through binding may influence the growth promoting, differentiation inhibiting, or apoptosis regulating functions of Fte-1/S3a.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Epstein-Barr virus
EBNA-5
Fte-1/S3a ribosomal protein
Cell transformation
Yeast two-hybrid system
külföldön készült közlemény
Megjelenés:Experimental Cell Research. - 303 : 1 (2005), p. 47-55. -
További szerzők:Yurchenko, Mariya Stahl, Joachim Klein, George Székely László Szirák Krisztina (1973-) (molekuláris genetikus)
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DOI
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4.

001-es BibID:BIBFORM077512
Első szerző:Kristóf Endre (általános orvos)
Cím:Interleukin-6 released from differentiating human beige adipocytes improves browning / Endre Kristóf, Ágnes Klusóczki, Roland Veress, Abhirup Shaw, Zsolt Sándor Combi, Klára Varga, Ferenc Győry, Zoltán Balajthy, Péter Bai, Zsolt Bacso, László Fésüs
Dátum:2019
ISSN:0014-4827
Megjegyzések:Brown and beige adipocytes contribute significantly to the regulation of whole body energy expenditure and systemic metabolic homeostasis not exclusively by thermogenesis through mitochondrial uncoupling. Several studies have provided evidence in rodents that brown and beige adipocytes produce a set of adipokines ("batokines") which regulate local tissue homeostasis and have beneficial effects on physiological functions of the entire body. We observed elevated secretion of Interleukin (IL)-6, IL-8 and monocyte chemoattractant protein (MCP)-1, but not tumor necrosis factor alpha (TNFα) or IL-1β pro-inflammatory cytokines, by ex vivo differentiating human beige adipocytes (induced by either PPARγ agonist or irisin) compared to white. Higher levels of IL-6, IL-8 and MCP-1 were released from human deep neck adipose tissue biopsies (enriched in browning cells) than from subcutaneous ones. IL-6 was produced in a sustained manner and mostly by the adipocytes and not by the undifferentiated progenitors. Continuous blocking of IL-6 receptor by specific antibody during beige differentiation resulted in downregulation of brown marker genes and increased morphological changes that are characteristic of white adipocytes. The data suggest that beige adipocytes adjust their production of IL-6 to reach an optimal level for differentiation in the medium enhancing browning in an autocrine manner.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Experimental Cell Research. - 377 : 1-2 (2019), p. 47-55. -
További szerzők:Klusóczki Ágnes (1991-) (biotechnológus) Veress Roland (1992-) (molekuláris biológus) Shaw, Abhirup (1992-) Combi Zsolt Varga Klára Győry Ferenc (1969-) (kardiológus) Balajthy Zoltán (1957-) (biokémikus, sejtbiológus) Bai Péter (1976-) (biokémikus) Bacsó Zsolt (1963-) (biofizikus) Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00006
GINOP
OTKA-NK105046
OTKA
OTKA-K123975
OTKA
ÚNKP-18-4
ÚNKP
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM004735
Első szerző:Nagy Péter (biofizikus)
Cím:Small interfering RNAs suppress the expression of endogenous and GFP-fused epidermal growth factor receptor (erbB1) and induce apoptosis in erbB1-overexpressing cells / Nagy, P., Arndt-Jovin, D. J., Jovin, T. M.
Dátum:2003
ISSN:014-4827 (Print)
Megjegyzések:Deregulated and excessive expression of epidermal growth factor receptor (EGFR or erbB1), a transmembrane receptor tyrosine kinase specific for the epidermal growth factor (EGF), is a feature and/or cause of a wide range of human cancers, and thus inhibition of its expression is potentially therapeutic. In RNA interference (RNAi), duplexes of 21-nucleotide RNAs (small interfering RNA, siRNA) corresponding to mRNA sequences of particular genes are used to efficiently inhibit the expression of the target proteins in mammalian cells. Here we show that by using RNAi the expression of endogenous erbB1 can be specifically and extensively (90%) suppressed in A431 human epidermoid carcinoma cells. As a consequence, EGF-induced tyrosine phosphorylation was inhibited and cell proliferation was reduced due to induction of apoptosis. We established an inverse correlation between the level of expressed erbB1 and EGF sensitivity on a cell-by-cell basis using flow cytometry. A431 cells expressing endogenous erbB1 were transfected with erbB1 fused C-terminally to enhanced green fluorescent protein (EGFP). Selective inhibition of the expression of the fusion protein was achieved with an siRNA specific for the EGFP mRNA, whereas the erbB1-specific siRNAs inhibited the expression of both molecules. siRNA-mediated inhibition of erbB1 and other erbB tyrosine kinases may constitute a useful therapeutic approach in the treatment of human cancer.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animals
Apoptosis
Carcinoma
Cell Cycle
Cell Line
Cell Proliferation
Cells
chemistry
Epidermal Growth Factor
Flow Cytometry
genetics
Green Fluorescent Proteins
Human
Humans
Indicators and Reagents
Luminescent Proteins
metabolism
Microscopy,Fluorescence
Phosphorylation
physiology
Proteins
Receptor, Epidermal Growth Factor
Recombinant Fusion Proteins
Research
RNA,Small Interfering
Support
Tyrosine
Megjelenés:Experimental Cell Research. - 285 : 1 (2003), p. 39-49. -
További szerzők:Arndt-Jovin, Donna J. Jovin, Thomas M.
Internet cím:DOI
elektronikus változat
Borító:

6.

001-es BibID:BIBFORM014363
Első szerző:Zákány Róza (anatómus-, kötőszövetbiológus)
Cím:Protein Phosphatase 2A Is Involved in the Regulation of Protein Kinase A Signaling Pathway during in Vitro Chondrogenesis / Róza Zákány, Kornélia Szűcs, Éva Bakó, Szabolcs Felszeghy, Gabriella Czifra, Tamás Bíró, László Módis, Pál Gergely
Dátum:2002
ISSN:0014-4827
Megjegyzések:aWe have evaluated the importance of the Ser/Thr protein phosphorylation anddephosphorylation for chondrogenesis in high-density chicken limb bud mesenchymalcell cultures (HDCs) by using H89, a cell-permeable protein kinase inhibitor, andokadaic acid (OA), a phosphoprotein phosphatase (PP)-specific inhibitor molecule.When 20 nM OA was applied to the HDCs on Days 2 and 3 of culturing, itsignificantly inhibited protein phosphatase 2A (PP2A), enhanced cartilageformation, and elevated the activity of cAMP-dependent protein kinase (PKA).Application of 20 microM H89 significantly decreased the activity of PKA andblocked the chondrogenesis in HDCs. Furthermore, OA enhanced cartilage formationand elevated the suppressed activity of PKA even in the H89-pretreated HDCs.cGMP-dependent protein kinase was not detected in HDCs, while protein kinase Cmu(PKCmu), which is also inhibited by nanomolar concentrations of H89, was presentthroughout the culturing period. Neither OA nor H89 influenced the expression ofthe catalytic subunit of PKA or the cAMP response element binding protein, CREB.However, a significantly elevated amount of Ser-133-phosphorylated-CREB (P-CREB)was detected following addition of OA, while H89 treatment resulted in a decreaseof the amount of P-CREB. Our results demonstrate that PP2A plays a role in theregulation of the PKA signaling pathway and that the phosphorylation level ofCREB is influenced by the activity of both enzymes during in vitrochondrogenesis.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
a0 (Cyclic AMP Response Element-Binding Protein)
0 (Enzyme Inhibitors)
0 (Isoquinolines)
0 (Sulfonamides)
127243-85-0 (N-(2-(4-bromocinnamylamino)ethyl)-5-isoquinolinesulfonamide)
56-45-1 (Serine)
72-19-5 (Threonine)
78111-17-8 (Okadaic Acid)
EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
EC 3.1.3.16 (Phosphoprotein Phosphatases)
EC 3.1.3.16 (Protein Phosphatase 2)
Animals
Cartilage/drug effects/embryology/metabolism
Cell Differentiation/drug effects/physiology
Cell Division/drug effects/physiology
Cells, Cultured
Chick Embryo
Chondrocytes/drug effects/metabolism
Chondrogenesis/drug effects/*physiology
Cyclic AMP Response Element-Binding Protein/metabolism
Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors/*metabolism
Dose-Response Relationship, Drug
Enzyme Inhibitors/*pharmacology
Isoquinolines/pharmacology
Limb Buds/embryology/metabolism
Okadaic Acid/pharmacology
Phosphoprotein Phosphatases/drug effects/*metabolism
Phosphorylation
Protein Phosphatase
Serine/chemistrySignal Transduction
Sulfonamides
Threonine/chemistry
Time Factors
egyetemen (Magyarországon) készült közlemény
Megjelenés:Experimental Cell Research. - 275 : 1 (2002), p. 1-8. -
További szerzők:Szűcs Kornélia (1945-) (biokémikus) Bakó Éva (1958-) (biokémikus) Felszeghy Szabolcs Béla (1972-) (fogorvos, anatómus, kötőszövetbiológus) Czifra Gabriella (1975-) (élettanász) Bíró Tamás (1968-) (élettanász) Módis László (1939-) (anatómus, kötőszövetbiológus) Gergely Pál (1947-) (biokémikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

7.

001-es BibID:BIBFORM013302
Első szerző:Zákány Róza (anatómus-, kötőszövetbiológus)
Cím:Hydrogen peroxide inhibits formation of cartilage in chicken micromass cultures and decreases the activity of calcineurin : implication of ERK1/2 and Sox9 pathways / Zákány Róza, Szíjgyártó Zsolt, Matta Csaba, Juhász Tamás, Csortos Csilla, Szűcs Kornélia, Czifra Gabriella, Bíró Tamás, Módis László, Gergely Pál
Dátum:2005
ISSN:0014-4827
Megjegyzések:Calcineurin was found as a positive regulator of chondrogenesis in chondrifying chicken micromass cultures (HDCs), as cyclosporine A (CsA) reduced both the amount of cartilage and the expression of mRNAs of aggrecan and the chondrogenic transcription factor Sox9. Cartilage formation was inhibited by H(2)O(2) in a concentration-dependent manner without loss of cellular viability or severe decrease of cell number. Expression of both the mRNA and the unphosphorylated protein Sox9 was decreased, while its phosphorylation was stimulated by either H(2)O(2) or CsA. Oxidative stress decreased the activity of calcineurin but the phosphorylation of the member of MAPK family ERK1/2 was extremely elevated either by 1 mM H(2)O(2) or 2 muM CSA. The ERK inhibitor PD098059 attenuated the depletion of cartilage matrix as well as decreased the expression and phosphorylation of Sox9 in cultures treated with H(2)O(2) or CsA. Our results suggest that the chondrogenesis-inhibiting effect of H(2)O(2) is mediated, at least partly, by inhibition of calcineurin and by activation of ERK1/2. We also propose a regulatory role of calcineurin in the phosphorylation level of either ERK1/2 or Sox9 and a positive role of ERK1/2 in regulating both the expression level and the phosphorylation state of Sox9 in chicken HDCs.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Chondrogenesis
Oxidative stress
Protein phosphorylation
Protein phosphatases
Calcineurin
e A
Cyclosporin
ERK1/2
PD098059
Sox9
Megjelenés:Experimental Cell Research. - 305 : 1 (2005), p. 190-199. -
További szerzők:Szíjgyártó Zsolt (1978-) (vegyész) Matta Csaba (1980-) (molekuláris biológus, genetikus, angol szakfordító) Juhász Tamás (1976-) (biológus, orvosbiológus) Csortos Csilla (1956-) (biokémikus) Szűcs Kornélia (1945-) (biokémikus) Czifra Gabriella (1975-) (élettanász) Bíró Tamás (1968-) (élettanász) Módis László (1939-) (anatómus, kötőszövetbiológus) Gergely Pál (1947-) (biokémikus)
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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