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1.

001-es BibID:BIBFORM029040
Első szerző:Erdődi Ferenc (biokémikus)
Cím:Purification and characterization of three distinct types of protein phosphatase catalytic subunits in bovine platelets / Ferenc Erdődi, Csilla Csortos, Lloyd Sparks, Andrea Murányi, Pál Gergely
Dátum:1992
ISSN:0003-9861
Megjegyzések:The catalytic subunits of bovine platelet protein phosphatases were separated into three distinct forms by chromatography on heparin-Sepharose. Each phosphatase was further purified to apparent homogeneity as judged in sodium dodecyl sulfate-polyacrylamide gel yielding single protein bands of 37, 41, and 36 kDa. The 37-kDa phosphatase was excluded from heparin-Sepharose and preferentially dephosphorylated the alpha-subunit of phosphorylase kinase. It was stimulated by polycations (polybrene or histone H1) and was inhibited by okadaic acid (IC50 = 0.3 nM), but its activity was not influenced by inhibitor-2 or heparin. The 41-kDa phosphatase was eluted from heparin-Sepharose by 0.20-0.25 M NaCl and preferentially dephosphorylated the beta-subunit of phosphorylase kinase. It was stimulated by polycations and inhibited by okadaic acid (IC50 = 2 nM), but its activity was not affected by inhibitor-2 or heparin. The 36-kDa phosphatase was eluted from heparin-Sepharose by 0.45-0.50 M NaCl and preferentially dephosphorylated the beta-subunit of phosphorylase kinase. It was inhibited by inhibitor-2, heparin, histone H1, and okadaic acid (IC50 = 70 nM). The 37- and 36-kDa phosphatases can be classified as type-2A and type-1 enzymes, respectively. The 41-kDa phosphatase does not precisely fit the criteria of either type, showing only partial similarities to both type-1 and type-2A enzymes and it may represent a novel type of protein phosphatase in bovine platelets.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Archives of Biochemistry And Biophysics. - 298 : 2 (1992), p. 682-687. -
További szerzők:Sparks, Lloyd Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus) Murányi Andrea (1966-) (biokémikus)
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2.

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)
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DOI
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3.

001-es BibID:BIBFORM029380
Első szerző:Gergely Pál (biokémikus)
Cím:A foszfoszerin/foszfotreonin-specifikus protein foszfatázokat gátló toxinok élettani hatásai / Gergely Pál, Murányi Andrea, Tóth Béla, Zákány Róza, Módis László, Erdődi Ferenc
Dátum:1999
ISBN:963-03-7600-8
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
egyetemen (Magyarországon) készült közlemény
Megjelenés:Nephrologia / szerk. Kakuk György, Kárpáti István. - p. 13-20. -
További szerzők:Murányi Andrea (1966-) (biokémikus) Tóth Béla (1954-) (vegyész, biokémikus) Zákány Róza (1963-) (anatómus-, kötőszövetbiológus) Módis László (1939-) (anatómus, kötőszövetbiológus) Erdődi Ferenc (1953-) (biokémikus)
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4.

001-es BibID:BIBFORM028726
Első szerző:Kiss Enikő
Cím:Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton / Enikő Kiss, Andrea Murányi, Csilla Csortos, Pál Gergely, Masaaki Ito, David J. Hartshorne, Ferenc Erdődi
Dátum:2002
ISSN:0264-6021
Megjegyzések:The myosin phosphatase (MP) composed of the catalytic subunit of type 1 protein phosphatase and myosin phosphatase target subunit isoform 1 (MYPT1) was identified as the major serine/threonine phosphatase component in the platelet-cytoskeleton fraction. MYPT1 was phosphorylated by cytoskeletal kinase(s), but the identity of the kinase(s) and the effect of phosphorylation were not established. Incubation of platelet-cytoskeletal fraction with MgATP or MgATP[S] (magnesium adenosine 5'-[gamma-thio]triphosphate) caused a decrease in the 20 kDa light-chain of smooth-muscle myosin (MLC20) phosphatase and phosphorylase phosphatase activities. MYPT1 contains a phosphorylation site, Thr-695, involved in the inhibition of MP in a RhoA/Rho kinase-dependent manner. The cytoskeletal kinase(s) phosphorylated Thr-695 of glutathione S-transferase (GST)-MYPT1, as determined with an antibody specific for phosphorylated Thr-695. The level of Rho kinase was low in the cytoskeletal fraction and was detected primarily in the membrane and cytosolic fractions. The phosphorylation of Thr-695 by the cytoskeletal kinase(s) was not affected by Rho kinase inhibitor, Y-27632, suggesting that kinase(s) other than Rho kinase were involved. In-gel kinase assay identified a kinase at 54-59 kDa that phosphorylated the C-terminal fragment of MYPT1 (GST-MYPT1(667-1004)). Western blots detected both zipper-interacting protein kinase (ZIPK) and integrin-linked kinase (ILK) at 54-59 kDa in the cytoskeleton and membrane fractions. Cytoskeletal ZIPK and ILK were separated and partially purified by chromatography on SP-Sepharose and on MonoQ. ZIPK preferentially phosphorylated MLC20 and had low activity on MYPT1. ILK phosphorylated both MLC20 and MYPT1 and phosphorylation of MYPT1 occured on Thr-695. The above results raise the potential for regulation of MP activity in platelet cytoskeleton by ILK and suggest an alternative to the Rho-linked pathway.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochemical Journal. - 365 : 1 (2002), p. 79-87. -
További szerzők:Murányi Andrea (1966-) (biokémikus) Ito, Masaaki Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus) Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus)
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5.

001-es BibID:BIBFORM090749
Első szerző:Murányi Andrea (biokémikus)
Cím:Protein Phosphatase 2A Plays a Role in the Suckling-Induced Changes in the Responsiveness of Pituitary Mammotropes / Murányi Andrea, Gergely Pál, Fekete Márton I. K., Nagy M. György
Dátum:1998
ISSN:0013-7227
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Endocrinology. - 139 : 11 (1998), p. 4590-4597. -
További szerzők:Gergely Pál (1947-) (biokémikus) Fekete I. K. Márton Nagy M. György
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6.

001-es BibID:BIBFORM048293
035-os BibID:(dekdb)csiKLT00021510
Első szerző:Murányi Andrea (biokémikus)
Cím:Thrombocyta protein phosphatases : properties of serine/threonine specific phosphatase 1 and 2A / Murányi, A., Erdődi, F., 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-6
További szerzők:Erdődi Ferenc (1953-) (biokémikus) Gergely Pál (1947-) (biokémikus)
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7.

001-es BibID:BIBFORM028868
Első szerző:Murányi Andrea (biokémikus)
Cím:Identification and localization of myosin phosphatase in human platelets / Andrea Murányi, Ferenc Erdődi, Masaaki Ito, Pál Gergely, David J. Hartshorne
Dátum:1998
ISSN:0264-6021
Megjegyzések:Type 1 (PP1) and type 2A (PP2A) phosphatase activity was measured in three subcellular fractions of human platelets. About 80% of the activity was in the high-speed supernatant. Western blots showed that the catalytic subunit of PP1 (PP1c), including alpha- and delta-isoforms, was present in each fraction, but the level of the catalytic subunit of PP2A was very low in the low-speed pellet (cytoskeletal fraction). Various antibodies detected a subunit similar to the 130 kDa subunit (M130) of myosin phosphatase (MP) of smooth muscle in the low- and the high-speed pellets of human platelets. PP1c and associated proteins were isolated by microcystin-Sepharose. Many proteins were separated from each fraction, including myosin, actin and PP1c. M130 was separated only from the low-speed and the high-speed pellets. Kinase activities were detected in the unbound fractions, and fractions from the low- and high-speed pellets phosphorylated M130 and myosin respectively. Treatment of platelets with calyculin A increased the phosphorylation level of many proteins, including myosin heavy- and light-chains, and caused association of cytoskeletal proteins with the low-speed pellet. No marked change in the distribution of PP1c and M130 was detected. These results suggest that the MP in human platelets is composed of PP1c plus a subunit similar to M130 of the smooth muscle phosphatase.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:The Biochemical Journal. - 330 : 1 (1998), p. 225-231. -
További szerzők:Ito, Masaaki Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus) Gergely Pál (1947-) (biokémikus)
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