CCL

Összesen 9 találat.
#/oldal:
Részletezés:
Rendezés:

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)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

2.

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)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

3.

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)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

4.

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)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

5.

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)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

6.

001-es BibID:BIBFORM028725
Első szerző:Murányi Andrea (biokémikus)
Cím:Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase / Andrea Murányi, Justin A. MacDonald, Jing Ti Deng, David P. Wilson, Timothy A. J. Haystead, Michael P. Walsh, Ferenc Erdődi, Enikő Kiss, Yue Wu, David J. Hartshorne
Dátum:2002
ISSN:0264-6021
Megjegyzések:A mechanism proposed for regulation of myosin phosphatase (MP) activity is phosphorylation of the myosin phosphatase target subunit (MYPT1). Integrin-linked kinase (ILK) is associated with the contractile machinery and can phosphorylate myosin at the myosin light-chain kinase sites. The possibility that ILK may also phosphorylate and regulate MP was investigated. ILK was associated with the MP holoenzyme, shown by Western blots and in-gel kinase assays. MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). One of the sites for cAMP-dependent protein kinase (PKA) was Ser(694). Assays with the catalytic subunit of type 1 phosphatase indicated that only the C-terminal fragment of MYPT1 phosphorylated by zipper-interacting protein kinase, and ILK inhibited activity. The phosphorylated N-terminal fragment activated phosphatase activity and phosphorylation by PKA was without effect. Using full-length MYPT1 constructs phosphorylated by various kinases it was shown that Rho kinase gave marked inhibition; ILK produced an intermediate level of inhibition, which was considerably reduced for the Thr(695)-->Ala mutant; and PKA had no effect. In summary, phosphorylation of the various sites indicated that Thr(695) was the major inhibitory site, Thr(709) had only a slight inhibitory effect and Ser(694) had no effect. The findings that ILK phosphorylated both MYPT1 and myosin and the association of ILK with MP suggest that ILK may influence cytoskeletal structure or function.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Biochemical Journal. - 366 (2002), p. 211-216. -
További szerzők:MacDonald, Justin A. Deng, Jing Ti Wilson, David P. Haystead, Timothy A. J. Walsh, Michael P. Kiss Enikő Wu, Yue Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

7.

001-es BibID:BIBFORM003573
Első szerző:Murányi Andrea (biokémikus)
Cím:Phosphorylation of Thr695 and Thr850 on the myosin phosphatase target subunit: inhibitory effects and occurrence in A7r5 cells / Murányi A., Derkach D., Erdődi F., Kiss A., Ito M., Hartshorne D. J.
Dátum:2005
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
myosin target subunit
myosin phosphatase
Rho-kinase
type 1 phosphatase
A7r5 cells
lysophosphatidic acid
Megjelenés:FEBS Letters. - 579 : 29 (2005), p. 6611-6615. -
További szerzők:Derkach, Dmitry Erdődi Ferenc (1953-) (biokémikus) Kiss Andrea (1979-) (biokémikus, vegyész) Ito, Masaaki Hartshorne, David J.
Internet cím:elektronikus változat
DOI
Borító:

8.

001-es BibID:BIBFORM028723
Első szerző:Wu, Yue
Cím:Myosin phosphatase and myosin phosphorylation in differentiating C2C12 cells / Yue Wu, Ferenc Erdődi, Andrea Murányi, Kevin D. Nullmeyer, Ronald M. Lynch, David J. Hartshorne
Dátum:2003
ISSN:0142-4319
Megjegyzések:C2C12 cells offer a useful model to study the differentiation of non-muscle cells to skeletal muscle cells. Myosin phosphorylation and changes in related enzymes, with an emphasis on myosin phosphatase (MP) were analyzed over the first 6 days of C2C12 differentiation. There was a transition from myosin phosphatase target subunit 1 (MYPT1), predominant in the non-muscle cells to increased expression of MYPT2. Levels of MYPT1/2 were estimated, and both isoforms were higher in non- or partially differentiated cells compared to the concentrations in the differentiated isolated myotubes from day 6. A similar profile of expression was estimated for the type 1 protein phosphatase catalytic subunit, delta isoform (PP1c delta). Phosphatase activities, using phosphorylated smooth and skeletal muscle myosins, were estimated for total cell lysates and isolated myotubes. In general, smooth muscle myosin was the preferred substrate. Although the expression of MYPT1/2 and PP1c delta was considerably reduced in isolated myotubes the phosphatase activities were not reduced to corresponding levels. Most of the MP activity was due to PP1c, as indicated by okadaic acid. In spite of relatively high expression of MYPT1/2 and PP1c delta, marked phosphorylation of non-muscle myosin (over 50% of total myosin) was observed at day 2 (onset of expression of muscle-specific proteins) and both mono- and diphosphorylated light chains were observed. Partial inhibition of MLCK by 1-(5-chloronaphthalene-1-sulphonyl)-1H-hexahydro-1,4-diazepine HCl (ML-9) or by a construct designed from the autoinhibitory domain of MLCK, resulted in an increase in small myotubes (3-5 nuclei) after 3 days of differentiation and a decrease in larger myotubes (compared to control). The effect of ML-9 was not due to a reduction in intracellular Ca2+ levels. These results suggest that phosphorylation of non-muscle myosin is important in growth of myotubes, either in the fusion process to form larger myotubes or indirectly, by its role in sarcomere organization.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Journal of Muscle Research and Cell Motility. - 24 : 8 (2003), p. 499-511. -
További szerzők:Murányi Andrea (1966-) (biokémikus) Nullmeyer, Kevin D. Lynch, Ronald M. Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

9.

001-es BibID:BIBFORM003572
Első szerző:Wu, Yue
Cím:Localization of myosin phosphatase target subunit and its mutants / Wu Y., Murányi A., Erdődi F., Hartshorne D. J.
Dátum:2005
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
smooth muscle
MYPT
nuclear localization
transient transfection
Megjelenés:Journal of Muscle Research and Cell Motility. - 26 : 2-3 (2005), p. 123-134. -
További szerzők:Murányi Andrea (1966-) (biokémikus) Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
Internet cím:elektronikus változat
Borító:
Rekordok letöltése1