CCL

Összesen 12 találat.
#/oldal:
Részletezés:
Rendezés:

1.

001-es BibID:BIBFORM048295
035-os BibID:(dekdb)csiKLT00021510
Első szerző:Bakó Éva (biokémikus)
Cím:Assay of protein phosphatase 1 and 2A in S. Cerevisiae and S. Pombe / Bakó, É., Farkas, L., Zeke, T., Sipiczki, M., Gergely, P.
Dátum:1993
Tárgyszavak:Orvostudományok Elméleti orvostudományok előadáskivonat
Biokémia
Megjelenés:1st international conference of the Hungarian Biochemical Society: August 29 - September 1, 1993 Debrecen, Hungary / organized by Pál Elődi, László Fésűs, Pál Gergely. - p. PM-8
További szerzők:Farkas László (sebész) Zeke Tamás (1970-) (biológus, biokémikus) Sipiczki Mátyás (1948-) (biológus) Gergely Pál (1947-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

2.

001-es BibID:BIBFORM028159
Első szerző:Bakó Éva (biokémikus)
Cím:Purification and partial characterization of protein phosphatases from rat thymus / Éva Bakó, Viktor Dombrádi, Ferenc Erdődi, Lawrence Zumo, Pál Kertai, Pál Gergely
Dátum:1989
ISSN:0167-4889
Megjegyzések:Protein phosphatases assayed with phosphorylase alpha are present in the soluble and particulate fractions of rat thymocytes. Phosphorylase phosphatase activity in the cytosol fraction was resolved by heparin-Sepharose chromatography into type-1 and type-2A enzymes. Similarities between thymocyte and muscle or liver protein phosphatase-1 included preferential dephosphorylation of the beta subunit of phosphorylase kinase, inhibition by inhibitor-2 and retention by heparin-Sepharose. Similarities between thymocyte and muscle or liver protein phosphatase-2A included specificity for the alpha subunit of phosphorylase kinase, insensitivity to the action of inhibitor-2, lack of retention by heparin-Sepharose and stimulation by polycationic macromolecules such as polybrene, protamine and histone H1. Protein phosphatase-1 from the cytosol fraction of thymocytes had an apparent molecular mass of 120 kDa as determined by gel filtration. The phosphatase-2A separated from the cytosol of thymocytes may correspond to phosphatase-2A0, since it was completely inactive (latent) in the absence of polycation and had activity only in the presence of polycations. The apparent molecular mass of phosphatase-2A0 from thymocytes was 240 kDa as determined by gel filtration. The catalytic subunit of thymocyte type-1 protein phosphatase was purified with heparin-Sepharose chromatography followed by gel filtration and fast protein liquid chromatography on Mono Q column. The purified type-1 catalytic subunit exhibited a specific activity of 8.2 U/mg and consisted of a single protein of 35 kDa as judged by SDS-gel electrophoresis. The catalytic subunit of type-2A phosphatase from thymocytes appearing in the heparin-Sepharose flow-through fraction was further purified on protamine-Sepharose, followed by gel filtration. The specific activity of the type-2A catalytic subunit was 2.1 U/mg and consisted of a major protein of 34.5 kDa, as revealed by SDS-gel electrophoresis.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein phosphatase-1
protein phosphatase-2A
polycation
heparin-Sepharose
thymocyte
rat
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1013 : 3 (1989), p. 300-305. -
További szerzők:Kertai Pál (1927-2016) (népegészségügyi szakember) Dombrádi Viktor (1953-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus) Zumo, Lawrence (1966-) Gergely Pál (1947-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Szerző által megadott URL
Borító:

3.

001-es BibID:BIBFORM029382
Első szerző:Erdődi Ferenc (biokémikus)
Cím:Autophosphorylation of phosphorylase kinase and its regulatory function in the dephosphorylation of phosphorylase A / F. Erdődi, Éva Bakó, G. Bot, P. Gergely
Dátum:1987
Megjegyzések:Autophosphorylation of phosphorylase kinase was measured under conditions that favoured autoactivation. Heparin and troponin C stimulated the autophosphorylation of phosphorylase kinase at pH 6.8 in a Ca2+-dependent manner. The concentration required for the half-maximal stimulation of autophosphorylation for calcium ions was 2 microM in the absence of effectors, whereas 0.7 microM and 0.1 microM in the presence of troponin C and heparin, respectively. Calmodulin increased the rate of autophosphorylation of the alpha subunit only, resulting in a slight increase in the rate of autoactivation of phosphorylase kinase. Troponin C, heparin and polybrene enhanced the rate of autophosphorylation of both alpha and beta subunits. The increased autophosphorylation coincided with an enhancement of kinase activity. Neither of these stimulatory macromolecules had significant influence on the total number of phosphate groups incorporated into the alpha or beta subunits by autophosphorylation. Thio-autophosphorylated form of phosphorylase kinase behaved as an inhibitor in the dephosphorylation of phosphorylase a by the catalytic subunits of phosphatase-1 or phosphatase-2A and by the latent form of phosphatase-2A. Concentration of phosphorylase kinase needed to 50% inhibition was in the range of 0.05-0.08 microM.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény hazai lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Acta Biochimica et Biophysica Hungarica. - 22 : 4 (1987), p. 425-438. -
További szerzők:Bakó Éva (1958-) (biokémikus) Bot György (1917-1998) (biokémikus, vegyész) Gergely Pál (1947-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

4.

001-es BibID:BIBFORM052862
Első szerző:Farkas Ilona (biokémikus)
Cím:Quantitation of protein phosphatase 1 and 2A in extracts of the budding yeast and fission yeast / Ilona Farkas, Éva Bakó, Andrea Murányi, Tamás Zeke, Mátyás Sipiczki, Pál Gergely
Dátum:1995
ISSN:1357-2725
Megjegyzések:Serine/threonine protein phosphatases are also involved in the control of cell division. The aim of the present study was to compare the activity of protein phosphatase 1 (PP1) and 2A (PP2A) in cell extracts of the budding and fission yeast, made at different phases of growth. The activities of PP1 and PP2A toward phosphorylase were similar in extracts of S. cerevisiae. In S. pombe extracts, PP1 was responsible for more than 80% of the phosphorylase phosphatase activity. Ammonium sulfate-ethanol treatment increased the specific activity of the phosphatases and the percentage of PP2A in S. cerevisiae extracts. No increase in the proportion of PP2A was observed upon the same treatment of S. pombe extracts. The above results were confirmed by fractionation of PP1 and PP2A activities on a heparin-Sepharose column. The proportion of PP1 and PP2A activities did not change significantly during exponential cell growth but cells from stationary phase exhibited lower phosphatase activities. These results may indicate a lower level of expression of the PP2A genes in S. pombe and/or differences in the structure of the holoenzymes or their regulators in the two genera.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Protein phosphatase 1 2A
Yeast
Okadaic acid
Heparin-Sepharose chromatography
accharomyces cerevisiae
Schizosaccharomyces pombe
Megjelenés:International Journal Of Biochemistry & Cell Biology. - 27 : 8 (1995), p. 767-773. -
További szerzők:Bakó Éva (1958-) (biokémikus) Murányi Andrea (1966-) (biokémikus) Zeke Tamás (1970-) (biológus, biokémikus) Sipiczki Mátyás (1948-) (biológus) Gergely Pál (1947-) (biokémikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

5.

001-es BibID:BIBFORM049124
035-os BibID:PMID:24333667
Első szerző:Juhász Tamás (biológus, orvosbiológus)
Cím:Mechanical loading stimulates chondrogenesis via the PKA/CREB-Sox9 and PP2A pathways in chicken micromass cultures / Tamás Juhász, Csaba Matta, Csilla Somogyi, Éva Katona, Roland Takács, Rudolf Ferenc Soha, István A. Szabó, Csaba Cserháti, Róbert Sződy, Zoltán Karácsonyi, Éva Bakó, Pál Gergely, Róza Zákány
Dátum:2014
ISSN:0898-6568
Megjegyzések:Biomechanical stimuli play important roles in the formation of articular cartilage during early foetal life, and optimal mechanical load is a crucial regulatory factor of adult chondrocyte metabolism and function. In this study, we undertook to analyse mechanotransduction pathways during in vitro chondrogenesis. Chondroprogenitor cells isolated from limb buds of 4-day-old chicken embryos were cultivated as high density cell cultures for 6days. Mechanical stimulation was carried out by a self-designed bioreactor that exerted uniaxial intermittent cyclic load transmitted by the culture medium as hydrostatic pressure and fluid shear to differentiating cells. The loading scheme (0.05Hz, 600Pa; for 30min) was applied on culturing days 2 and 3, when final commitment and differentiation of chondroprogenitor cells occurred in this model. The applied mechanical load significantly augmented cartilage matrix production and elevated mRNA expression of several cartilage matrix constituents, including collagen type II and aggrecan core protein, as well as matrix-producing hyaluronan synthases through enhanced expression, phosphorylation and nuclear signals of the main chondrogenic transcription factor Sox9. Along with increased cAMP levels, a significantly enhanced protein kinase A (PKA) activity was also detected and CREB, the archetypal downstream transcription factor of PKA signalling, exhibited elevated phosphorylation levels and stronger nuclear signals in response to mechanical stimuli. All the above effects were diminished by the PKA-inhibitor H89. Inhibition of the PKA-independent cAMP-mediators Epac1 and Epac2 with HJC0197 resulted in enhanced cartilage formation, which was additive to that of the mechanical stimulation, implying that the chondrogenesis-promoting effect of mechanical load was independent of Epac. At the same time, PP2A activity was reduced following mechanical load and treatments with the PP2A-inhibitor okadaic acid were able to mimic the effects of the intervention. Our results indicate that proper mechanical stimuli augment in vitro cartilage formation via promoting both differentiation and matrix production of chondrogenic cells, and the opposing regulation of the PKA/CREB-Sox9 and the PP2A signalling pathways is crucial in this phenomenon.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Doktori iskola
Mechanotransduction
Chondrocyte differentiation
Extracellular matrix
H89
Okadaic acid
Epac
Megjelenés:Cellular Signalling. - 26 : 3 (2014), p. 468-482. -
További szerzők:Matta Csaba (1980-) (molekuláris biológus, genetikus, angol szakfordító) Somogyi Csilla (1983-) (biológus, angol-magyar szakfordító) Katona Éva (1986-) (molekuláris biológus) Takács Roland Ádám (1985-) (molekuláris biológus, biokémikus) Soha Rudolf Ferenc (1986-) (fizikus) Szabó István András (1956-) (fizikus) Cserháti Csaba (1963-) (fizikus) Sződy Róbert Karácsonyi Zoltán (1975-) (ortopéd és baleseti sebész) Bakó Éva (1958-) (biokémikus) Gergely Pál (1947-) (biokémikus) Zákány Róza (1963-) (anatómus-, kötőszövetbiológus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Molekuláris Orvostudomány Doktori Iskola
TÁMOP-4.2.2.A-11/1/KONV-2012-0036
TÁMOP
TÁMOP-4.2.4.A/2-11-1-2012-0001
TÁMOP
CNK80709
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

6.

001-es BibID:BIBFORM037161
Első szerző:Kolozsvári Bernadett (molekuláris biológus, genetikus)
Cím:Calcineurin regulates endothelial barrier function by interaction with and dephosphorylation of myosin phosphatase / Kolozsvári B., Bakó É., Bécsi B., Kiss A., Czikora Á., Tóth A., Vámosi Gy., Gergely P., Erdődi F.
Dátum:2012
ISSN:0008-6363
Megjegyzések:AIMS: Calcineurin (CN) influences myosin phosphorylation and alters endothelial barrier function; however, the molecular mechanism is still obscure. Here we examine whether CN controls myosin phosphorylation via mediating the phosphorylation state of Thr696 in myosin phosphatase (MP) target subunit 1 (MYPT1), the phosphorylation site inhibitory to the catalytic activity of MP. METHODS AND RESULTS: Exposure of bovine or human pulmonary artery endothelial cells (BPAECs or HPAECs) to the CN inhibitor cyclosporin A (CsA) induces a rise in intracellular Ca(2+) and increases the phosphorylation level of cofilin(Ser3) and MYPT1(Thr696) in a Ca(2+)-and Rho-kinase-dependent manner. An active catalytic fragment of CN overexpressed in tsA201 cells decreases endogenous MYPT-phospho-Thr696 (MYPT1(pThr696)) levels. Purified CN dephosphorylates (32)P-labelled MYPT1, suggesting direct action of CN on this substrate. Interaction of MYPT1 with CN is revealed by MYPT1 pull-down experiments and colocalization in both BPAECs and HPAECs as well as by surface plasmon resonance (SPR)-based binding studies. Stabilization of the MYPT1-CN complex occurs via the MYPT1(300PLIEST305) sequence similar to the CN substrate-docking PxIxIT-motif. Thrombin induces a transient increase of MYPT1(pThr696) in BPAECs, whereas its combination with CsA results in maintained phosphorylation levels of both MYPT1(pThr696) and myosin. These phosphorylation events might correlate with changes in endothelial permeability since CsA slows down the recovery from the thrombin-induced decrease of the transendothelial electrical resistance of the BPAEC monolayer. CONCLUSION: CN may improve endothelial barrier function via inducing dephosphorylation of cofilin(pSer3) and by interaction with MYPT1 and activating MP through MYPT1(pThr696) dephosphorylation, thereby affecting actin polymerization and decreasing myosin phosphorylation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Molekuláris Medicina
Megjelenés:Cardiovascular Research. - 96 : 3 (2012), p. 494-503. -
További szerzők:Bakó Éva (1958-) (biokémikus) Bécsi Bálint (1981-) (vegyészmérnök) Kiss Andrea (1979-) (biokémikus, vegyész) Czikora Ágnes (1982-) (molekuláris biológus) Tóth Attila (1971-) (biológus) Vámosi György (1967-) (biofizikus) Gergely Pál (1947-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.2-08/1-2008-0019
TÁMOP
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Biomolekuláris interakciók jellemzőinek kvantitatív meghatározása
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
I. Protein foszfatázok szerepe az in vitro porcdifferenciációban és a mechano-transzdukcióban II. Hypoglykaemiás szerek tervezése a glikogén foszforilázra (foszforilációval és defoszforilációval szabályozott kulcsenzim) ható molekulákkal
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

7.

001-es BibID:BIBFORM037160
Első szerző:Kolozsvári Bernadett (molekuláris biológus, genetikus)
Cím:Role of calcineurin in thrombin-mediated endothelial cell contraction / Kolozsvári Bernadett, Szíjgyártó Zsolt, Bai Péter, Gergely Pál, Verin Alexander, Garcia Joe G. N., Bakó Éva
Dátum:2009
ISSN:1552-4922
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cytometry. Part A. - 75 : 5 (2009), p. 405-411. -
További szerzők:Szíjgyártó Zsolt (1978-) (vegyész) Bai Péter (1976-) (biokémikus) Gergely Pál (1947-) (biokémikus) Verin, Alexander Garcia, Joe G. N. Bakó Éva (1958-) (biokémikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

8.

001-es BibID:BIBFORM028068
Első szerző:Szöőr Balázs (biokémikus)
Cím:Isolation and characterization of the catalytic subunit of protein phosphatase 2A from Neurospora crassa / Balázs Szöőr, Zsigmond Fehér, Éva Bakó, Ferenc Erdődi, Gábor Szabó, Pál Gergely, Viktor Dombrádi
Dátum:1995
ISSN:1096-4959
Megjegyzések:The catalytic subunit of protein phosphatase 2A (PP2Ac) was purified from Neurospora crassa extract by (NH4)2SO4-ethanol precipitation followed by DEAE-Sephacel, heparin-Sepharose, and MonoQ chromatography steps about 900-fold to a specific activity of 1200 U/g with a 2% yield. The apparent M(r) of PP2Ac was estimated to be 35 kDa by gel filtration and 33 kDa by SDS polyacrylamide gel electrophoresis. Half maximal inhibition of PP2Ac was achieved at 0.3 nM okadaic acid, 0.1 nM microcystin-LR, 56 nM cantharidin and 280 nM endothall concentrations. The preparation was completely inhibited by 20 mM NaF, was insensitive to rabbit muscle inhibitor-2, and was specific for the alpha-subunit of rabbit muscle phosphorylase kinase. According to its biochemical properties, N. crassa PP2Ac is very similar to its mammalian counterparts. Antipeptide antibodies raised against the N-terminal and C-terminal ends of human PP2Ac did not cross-react with N. crassa PP2Ac, indicating sequence differences outside the catalytic core of the enzyme.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein phosphorylation
protein phosphatase 2A
Neurospora crassa
heparin-Sepharose
okadaic acid
microcystin-LR
cantharidin
endothall
Megjelenés:Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology. - 112 : 3 (1995), p. 515-522. -
További szerzők:Fehér Zsigmond (1949-) (molekuláris genetikus) Szabó Gábor (1927-1996) (biológus, genetikus) Bakó Éva (1958-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus) Gergely Pál (1947-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

9.

001-es BibID:BIBFORM048296
035-os BibID:(dekdb)csiKLT00021510
Első szerző:Szöőr E.
Cím:Partial purification and characterization of the catalytic subunit of protein phosphatase 2A from neurospora crassa / Szöőr, E., Fehér, Zs., Bakó, É., Szabó, G., Gergely, P., Dombrádi, V.
Dátum:1993
Tárgyszavak:Orvostudományok Elméleti orvostudományok előadáskivonat
Biokémia
Megjelenés:1st international conference of the Hungarian Biochemical Society : August 29 - September 1, 1993 Debrecen, Hungary / organized by Pál Elődi, László Fésűs, Pál Gergely. - p. PM-9
További szerzők:Fehér Zsigmond (1949-) (molekuláris genetikus) Bakó Éva (1958-) (biokémikus) Szabó Gábor (1927-1996) (biológus, genetikus) Gergely Pál (1947-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

10.

001-es BibID:BIBFORM027865
Első szerző:Vissi Emese (biokémikus, biológus)
Cím:Functional analysis of the Neurospora crassa PZL-1 protein phosphatase by expression in budding and fission yeast / Emese Vissi, Josef Clotet, Eulalia de Nadal, Anna Barceló, Éva Bakó, Pál Gergely, Viktor Dombrádi, Joaquín Ariño
Dátum:2001
ISSN:0749-503X
Megjegyzések:The gene pzl-1 from the filamentous fungus Neurospora crassa encodes a putative Ser/Thr protein phosphatase that is reminiscent of the Ppz1/Ppz2 and Pzh1 phosphatases from Saccharomyces cerevisiae and Schizosaccharomyces pombe, respectively. The entire PZL-1 protein, as well as its carboxyl-terminal domain, have been expressed in Escherichia coli as active protein phosphatases. To characterize its cellular role, PZL-1 was also expressed in Sz. pombe and in S. cerevisiae. Expression of PZL-1 in S. cerevisiae from the PPZ1 promoter was able to rescue the altered sensitivity to caffeine and lithium ions of a ppz1 strain. Furthermore, high copy number expression of PZL-1 alleviated the lytic phenotype of a S. cerevisiae slt2/mpk1 mitogen-activated protein (MAP) kinase mutant, similarly to that described for PPZ1, and mimicked the effects of high levels of Ppz1 on cell growth. Expression of PZL-1 in fission yeast from a weak version of the nmt1 promoter fully rescued the growth defect of a pzh1Delta strain in high potassium, but only partially complemented the sodium-hypertolerant phenotype. Strong overexpression of the N. crassa phosphatase in Sz. pombe affected cell growth and morphology. Therefore, PZL-1 appears to fulfil every known function carried out by its S. cerevisiae counterpart, despite the marked divergence in sequence within their NH(2)-terminal moieties.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
PPZ phosphatases
functional expression
yeast
salt tolerance
külföldön készült közlemény
Megjelenés:Yeast. - 18 (2001), p. 115-124. -
További szerzők:Clotet, Josef de Nadal, Eulalia Barceló, Anna Ariño, Joaquín Bakó Éva (1958-) (biokémikus) Gergely Pál (1947-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

11.

001-es BibID:BIBFORM015613
035-os BibID:11195086
Első szerző:Zákány Róza (anatómus-, kötőszövetbiológus)
Cím:Okadaic acid-induced inhibition of protein phosphatase 2A enhances chondrogenesisin chicken limb bud micromass cell cultures / Róza Zákány, Éva Bakó, Szabolcs Felszeghy, Krisztina Holló, Margit Balázs, Helga Bárdos, Pál Gergely, László Módis
Dátum:2001
ISSN:0340-2061 (Linking)
Megjegyzések:The role of major cellular serine/threonine-specific protein phosphatases,protein phosphatase 1 and 2A, was investigated during chicken cartilagedifferentiation under in vitro conditions. Activity of protein phosphatase 2Adecreased parallel to differentiation of chondrogenic cells, whereas activity ofprotein phosphatase 1 remained unchanged as assayed in the supernatants of thehomogenised chicken limb bud micromass cell cultures. When okadaic acid, a potentinhibitor of protein phosphatase 1 and 2A was applied in 20 nM concentration for4 h during the second and third culturing days, it significantly increased thesize of metachromatic cartilage areas measured in 6-day-old colonies. Followingokadaic acid treatments, a significant inhibition in the activity of proteinphosphatase 2A was found, while the activity of protein phosphatase 1 wasunaffected as measured an days 2 and 3. TRITC-phalloidin labelling demonstratedthat okadaic acid disorganised actin filaments and induced rounding ofchondrogenic cells. This deterioration of actin filaments was reversible.Electron microscopy and biochemical analysis of colonies revealed that theultrastructure and major components of cartilage matrix remained unchanged underthe effect of okadaic acid. Okadaic acid-treatment applied to cultures containingpredominantly differentiated chondrocytes (after day 4) did not influence thecartilage formation. 3H-thymidine and bromodeoxyuridine incorporation-assaysdemonstrated enhanced cell proliferation in the okadaic acid-treated coloniescompared to that of the untreated ones. Our results indicate, for the first time,that protein phosphatase 2A is involved in the regulation of chondrogenesis.Inhibition of protein phosphatase 2A with okadaic acid may result in increasedchondrogenesis via modulation of proliferation and cytoskeletal organisation, aswell as via alteration of protein kinase A-signaling pathway of the chondrogeniccells.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
78111-17-8 (Okadaic Acid)
EC 3.1.3.16 (Phosphoprotein Phosphatases)
EC 3.1.3.16 (Protein Phosphatase 1)
EC 3.1.3.16 (Protein Phosphatase 2)
Animals
Cartilage/*embryology/metabolism/ultrastructure
Cell Differentiation/drug effects/physiology
Cell Division/drug effects/physiology
Cells, Cultured/drug effects/metabolism/ultrastructure
Chick Embryo
Chondrocytes/drug effects/*metabolism/ultrastructure
Chondrogenesis/drug effects/*physiology
Cytoskeleton/drug effects/metabolism/ultrastructure
Dose-Response Relationship, Drug
Limb Buds/*embryology/metabolism/ultrastructure
Microfilaments/drug effects/metabolism/ultrastructure
Okadaic Acid/*pharmacology
Phosphoprotein Phosphatases/drug effects/*metabolism
Phosphorylation/drug effects
Protein Phosphatase 1
Protein Phosphatase 2
Signal Transduction/drug effects/physiology
egyetemen (Magyarországon) készült közlemény
Megjelenés:Anatomy and Embryology. - 203 : 1 (2001), p. 23-34. -
További szerzők:Bakó Éva (1958-) (biokémikus) Felszeghy Szabolcs Béla (1972-) (fogorvos, anatómus, kötőszövetbiológus) Holló Krisztina (1967-) (vegyész) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Bárdos Helga (1969-) (megelőző orvostan és népegészségtan szakorvos) Gergely Pál (1947-) (biokémikus) Módis László (1939-) (anatómus, kötőszövetbiológus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
elektronikus változat
DOI
Borító:

12.

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:
Rekordok letöltése1 
Corvina könyvtári katalógus v8.2.27 © 2023 Monguz kft. Minden jog fenntartva.