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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)
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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)
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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
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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)
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