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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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2.

001-es BibID:BIBFORM047051
035-os BibID:PMID:2157500
Első szerző:Csortos Csilla (biokémikus)
Cím:Phosphorylase phosphatase activities of rat liver in streptozotocin-diabetes / Csilla Csortos, Ilona Farkas, Lloyd Sparks, Tamás Bányász, Tibor Kovács, Pál Gergely
Dátum:1990
ISSN:0167-4889
Megjegyzések:Protein phosphatase-1 and 2A, accounting for all the hepatic activity regulating phosphorylase, were assayed in streptozotocin-induced (8 weeks) diabetic Wistar rats. Cytosolic protein phosphatase-1 and 2A were distinguished by chromatography on heparin-Sepharose and by inhibition with inhibitor-2. Approx. 25-35% increases in type-1 phosphorylase phosphatase activity measured in cytosols were registered in diabetic rats when compared with control and 24 h fasting animals. The enrichment of protein phosphatase-1 in the cytosol of streptozotocin-treated rat livers could not be attributed to the reduced glycogen content with the onset of diabetes, since this elevated level of type-1 phosphatase was not observed in fasting rats with low glycogen content. The translocation of type-1 phosphatase from the particulate fraction into the cytosol was also recorded in trypsin-treated samples of diabetic rat livers. The apparent molecular weight of type-1 phosphatase in the cytosol of control and fasted rats was 160,000 as judged by gel filtration. The type-1 phosphatase activity that was released from the particulate fraction by streptozotocin-induced diabetes identified a further enzyme species (Mr 110,000) in the cytosol. Our data imply that the higher levels of cytosolic protein phosphatase-1 in diabetic rat liver could be a consequence of the dissociation of the catalytic subunit of protein phosphatase-1 and the glycogen-binding subunit in rat livers.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Protein phosphatase
Hepatic metabolism
Diabetes
Fasting
Streptozotocin
Rat liver
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1052 : 1 (1990), p. 235-241. -
További szerzők:Farkas Ilona (1953-) (biokémikus) Sparks, Lloyd Bányász Tamás (1960-) (élettanász) Kovács Tibor (1929-1994) (élettanász) Gergely Pál (1947-) (biokémikus)
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3.

001-es BibID:BIBFORM040381
Első szerző:Lakatos Petra (Molekuláris biológus)
Cím:3-Aminobenzamide protects primary human keratinocytes from UV-induced cell death by a poly(ADP-ribosyl)ation independent mechanism / Petra Lakatos, Éva Szabó, Csaba Hegedűs, György Haskó, Pál Gergely, Péter Bai, László Virág
Dátum:2013
ISSN:0167-4889
Megjegyzések:Poly(ADP-ribosyl)ation (PARylation) is a NAD(+)-dependent protein modification carried out by PARP [poly(ADP-ribose) polymerase] enzymes. Here we set out to investigate whether PARylation regulates UVB-induced cell death in primary human keratinocytes. We used the benchmark PARP inhibitor 3-aminobenzamide (3AB) and a more potent and specific inhibitor PJ34 and found that UVB (0.05-0.2J/cm(2)) induced a dose dependent loss of viability that was prevented by 3AB but not by PJ34. Similarly to PJ34, two other new generation PARP inhibitors also failed to protect keratinocytes from UVB-induced loss of viability. Moreover, silencing PARP-1 in HaCaT human keratinocytes sensitized cells to UVB toxicity but 3AB provided protection to both control HaCaT cells and to PARP-1 silenced cells indicating that the photoprotective effect of 3AB is independent of PARP inhibition. Lower UVB doses (0.0125-0.05J/cm(2)) caused inhibition of proliferation of keratinocytes which was prevented by 3AB but augmented by PJ34. UVB-induced keratinocyte death displayed the characteristics of both apoptosis (morphology, caspase activity, DNA fragmentation) and necrosis (morphology, LDH release) with all of these parameters being inhibited by 3AB and apoptotic parameters slightly enhanced by PJ34. UVA also caused apoptotic and necrotic cell death in keratinocytes with 3AB protecting and PJ34 sensitizing cells to UVA-induced toxicity. 3AB prevented UVB-induced mitochondrial membrane depolarization and generation of hydrogen peroxide. In summary, PARylation is a survival mechanism in UV-treated keratinocytes. Moreover, 3-aminobenzamide is photoprotective and acts by a PARP-independent mechanism at a premitochondrial step of phototoxicity.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Molekuláris Medicina
Ultraviolet radiation
Poly(ADP-ribose) polymerase
3-Aminobenzamide
Cell death
Apoptosis
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1833 : 3 (2013), p. 743-751. -
További szerzők:Szabó Éva (1965-) (bőrgyógyász, kozmetológus) Hegedűs Csaba (1980-) (biokémikus, molekuláris biológus) Haskó György (1967-) (biokémikus) Gergely Pál (1947-) (biokémikus) Bai Péter (1976-) (biokémikus) Virág László (1965-) (biokémikus, sejtbiológus, farmakológus)
Pályázati támogatás:TÁMOP-4.2.2-08/1-2008-0019
TÁMOP
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Oxidatív stressz és ADP-riboziláció kapcsolatának vizsgálata
TÁMOP-4.2.2.A-111/1/KONV-2012-0025
TÁMOP
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