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1.

001-es BibID:BIBFORM029827
Első szerző:Erdődi Ferenc (biokémikus)
Cím:Endothall thioanhydride inhibits protein phosphatases-1 and -2A in vivo / Ferenc Erdődi, Béla Tóth, Katsuya Hirano, Mayumi Hirano, Davis J. Hartshorne, Pál Gergely
Dátum:1995
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:American Journal of Physiology. - 269 (1995), p. C1176-C1184. -
További szerzők:Hirano, Katsuya Hirano, Mayumi Hartshorne, David J. Tóth Béla (1954-) (vegyész, biokémikus) Gergely Pál (1947-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM029381
Első szerző:Erdődi Ferenc (biokémikus)
Cím:Myosin light chain phosphatase / Ferenc Erdődi, Masaaki Ito, David J. Hartshorne
Dátum:1996
ISBN:0-12-078160-3
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
külföldön készült közlemény
Megjelenés:Biochemistry of smooth muscle contraction / ed. Bárány M. - p. 131-142. -
További szerzők:Ito, Masaaki Hartshorne, David J.
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3.

001-es BibID:BIBFORM028724
Első szerző:Erdődi Ferenc (biokémikus)
Cím:Phosphorylation of protein phosphatase type-1 inhibitory proteins by integrin-linked kinase and cyclic nucleotide-dependent protein kinases / Ferenc Erdődi, Enikő Kiss, Michael P. Walsh, Bjarki Stefansson, Jing Ti Deng, Masumi Eto, David L. Brautigan, David J. Hartshorne
Dátum:2003
ISSN:0006-291X
Megjegyzések:Protein phosphatases play key roles in cellular regulation and are subjected to control by protein inhibitors whose activity is in turn regulated by phosphorylation. Here we investigated the possible regulation of phosphorylation-dependent type-1 protein phosphatase (PP1) inhibitors, CPI-17, PHI-1, and KEPI, by various kinases. Protein kinases A (PKA) and G (PKG) phosphorylated CPI-17 at the inhibitory site (T38), but not PHI-1 (T57). Phosphorylated CPI-17 inhibited the activity of both the PP1 catalytic subunit (PP1c) and the myosin phosphatase holoenzyme (MPH) with IC(50) values of 1-8 nM. PKA predominantly phosphorylated a site distinct from the inhibitory T73 in KEPI, whereas PKG was ineffective. Integrin-linked kinase phosphorylated KEPI (T73) and this dramatically increased inhibition of PP1c (IC(50)=0.1 nM) and MPH (IC(50)=8 nM). These results suggest that the regulatory phosphorylation of CPI-17 and KEPI may involve distinct kinases and signaling pathways.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Biochemical and Biophysical Research Communications. - 306 : 2 (2003), p. 382-387. -
További szerzők:Kiss Enikő Walsh, Michael P. Stefansson, Bjarki Deng, Jing Ti Eto, Masumi Brautigan, David L. Hartshorne, David J.
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4.

001-es BibID:BIBFORM028870
Első szerző:Hartshorne, David J.
Cím:Myosin light chain phosphatase : subunit composition, interactions and regulation / David J. Hartshorne, Masaaki Ito, Ferenc Erdődi
Dátum:1998
ISSN:0142-4319
Megjegyzések:This review has presented some of the recent data on myosin phosphatase from smooth muscle. Although it is not conclusive, it is likely that most of the myosin phosphatase activity is represented by a holoenzyme composed of three subunits. These are: a catalytic subunit of 38 kDa of the type 1 phosphatase, probably the delta isoform (i.e. PP1c delta); a subunit of about 20 kDa whose function is not established; and a larger subunit that is thought to act as a target subunit. This is termed the myosin phosphatase target subunit, MYPT. Various isoforms of MYPT exist and the relatively minor distinctions are in the C-terminal leucine zipper motifs and/or with inserts in the central region. Many regions of the molecule are highly conserved, including the ankyrin repeats in the N-terminal part of the molecule and the sequence around the phosphorylation site. In addition, these isoforms all contain the four residue PP1c-binding motif (Arg/Lys-Val/Ile-Xaa-Phe). MYPT has been detected in a variety of cells and thus is not unique to smooth muscle. With phosphorylated myosin as substrate, the phosphatase activity of PP1c is low and is enhanced on addition of MYPT. It is assumed that MYPT functions as a target subunit and binds to both PP1c and substrate. The N-terminal fragment of MYPT is responsible for the activation of PP1c activity, but how much of the N-terminal sequence is required is not established. An important point is that activation is not a general effect and is specific for myosin. It is not known if other substrates may be targeted to MYPT. There are two binding sites for PP1c on MYPT: a strong site in the N-terminal segment (containing the 4-residue motif) and a weaker site in the ankyrin repeats, possibly in repeats 5, 6 and 7. The location(s) of the myosin-binding sites on MYPT is controversial, and binding of myosin, or light chain, to both N- and C-terminal fragments has been reported. Regulation of myosin phosphatase activity involves changes in subunit interactions, although molecular mechanisms are not defined. There are basically two theories proposed for phosphatase inhibition (i.e. as seen in the agonist-induced increase in Ca2+ sensitivity). One hypothesis is that phosphorylation of Myosin light chain phosphatase MYPT (at residue 654 or 695 of the gizzard MYPT isoforms or an equivalent residue) inhibits the activity of the MP holoenzyme. The kinase involved is not established, but may be an unidentified endogenous kinase or a RhoA-activated kinase. The latter is an attractive possibility because there is convincing evidence that RhoA plays a crucial role in the Ca(2+)-sensitizing process in smooth muscle. A second idea involves arachidonic acid. This is released via phospholipase A2 and could either interact directly with MYPT and cause dissociation of the holoenzyme (thus effectively reducing the phosphatase activity to that of the isolated catalytic subunit), or it could activate a kinase that would phosphorylate MYPT and inhibit the phosphatase. It is possible that MP activity may also be activated, for example, following increases in cAMP and/or cGMP. Evidence in support of this is very limited and under in vivo conditions the phosphorylation of MYPT by the respective kinases has not been demonstrated. There is, however, a tentative hypothesis based on in vitro data that phosphorylation of MYPT by PKA alters its cellular localization. This involves a shuttle between the dephosphorylated membrane-bound and inhibited state (at least towards P-myosin) to a phosphorylated cytosolic or cytoskeletal, and active state. The pathway(s) discussed above originates at the cell membrane and is carried via one or more messengers to the level of the contractile apparatus where it is manifested by regulation of phosphatase activity. Various components of the route have been identified, including RhoA and the atypical PKC isoforms, but more remain to be discovered. It is possible that more than one pathway, or cascade, is
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Journal of Muscle Research And Cell Motility. - 19 : 4 (1998), p. 325-341. -
További szerzők:Ito, Masaaki Erdődi Ferenc (1953-) (biokémikus)
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5.

001-es BibID:BIBFORM028722
Első szerző:Hartshorne, David J.
Cím:Role of protein phosphatase type 1 in contractile functions : myosin phosphatase / David J. Hartshorne, Masaaki Ito, Ferenc Erdödi
Dátum:2004
ISSN:0021-9258
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Journal of Biological Chemistry. - 279 : 36 (2004), p. 37211-37214. -
További szerzők:Ito, Masaaki Erdődi Ferenc (1953-) (biokémikus)
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6.

001-es BibID:BIBFORM028872
Első szerző:Hirano, Katsuya
Cím:Interaction of protein phosphatase type 1 with a splicing factor / Katsuya Hirano, Ferenc Erdődi, James G. Patton, David J. Hartshorne
Dátum:1996
ISSN:0014-5793
Megjegyzések:A gizzard cDNA library was screened by the two-hybrid system using as bait the delta isoform of the catalytic subunit of protein phosphatase 1 (PP1delta). Among the proteins identified was a fragment of the polypyrimidine tract-binding protein-associated splicing factor (PSF) and for 242 residues was 97.1% identical to the human isoforms. Binding of PSF and PP1delta was confirmed by inhibition of phosphatase activity and by an overlay technique. The PP1delta binding site was contained in the N-terminal 82 residues of the PSF fragment. PSF may therefore act as a PP1 target molecule in the spliceosome.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Febs Letters. - 389 : 2 (1996), p. 191-194. -
További szerzők:Patton, James G. Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
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7.

001-es BibID:BIBFORM028721
Első szerző:Ito, Masaaki
Cím:Myosin phosphatase : structure, regulation and function / Masaaki Ito, Takeshi Nakano, Ferenc Erdődi, David J. Hartshorne
Dátum:2004
ISSN:0300-8177
Megjegyzések:Phosphorylation of myosin II plays an important role in many cell functions, including smooth muscle contraction. The level of myosin II phosphorylation is determined by activities of myosin light chain kinase and myosin phosphatase (MP). MP is composed of 3 subunits: a catalytic subunit of type 1 phosphatase, PPlc; a targeting subunit, termed myosin phosphatase target subunit, MYPT; and a smaller subunit, M20, of unknown function. Most of the properties of MP are due to MYPT and include binding of PP1c and substrate. Other interactions are discussed. A recent discovery is the existence of an MYPT family and members include, MYPT1, MYPT2, MBS85, MYPT3 and TIMAP. Characteristics of each are outlined. An important discovery was that the activity of MP could be regulated and both activation and inhibition were reported. Activation occurs in response to elevated cyclic nucleotide levels and various mechanisms are presented. Inhibition of MP is a major component of Ca2+-sensitization in smooth muscle and various molecular mechanisms are discussed. Two mechanisms are cited frequently: (1) Phosphorylation of an inhibitory site on MYPT1, Thr696 (human isoform) and resulting inhibition of PP1c activity. Several kinases can phosphorylate Thr696, including Rho-kinase that serves an important role in smooth muscle function; and (2) Inhibition of MP by the protein kinase C-potentiated inhibitor protein of 17 kDa (CPI-17). Examples where these mechanisms are implicated in smooth muscle function are presented. The critical role of RhoA/Rho-kinase signaling in various systems is discussed, in particular those vascular smooth muscle disorders involving hypercontractility.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
külföldön készült közlemény
Megjelenés:Molecular and Cellular Biochemistry. - 259 : 1-2 (2004), p. 197-209. -
További szerzők:Nakano, Takeshi Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
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8.

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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9.

001-es BibID:BIBFORM014011
Első szerző:Lontay Beáta (biokémikus)
Cím:Localization of myosin phosphatase target subunit 1 in rat brain and in primary cultures of neuronal cells / Lontay Beáta, Serfőző Zoltán, Gergely Pál, Ito Masaaki, Hartshorne David J., Erdődi Ferenc
Dátum:2004
ISSN:0021-9967
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
myosin phosphatase target subunit (MYPT)
protein phosphatase-1 (PP1)
Rho-kinase (ROK)
synaptophysin
immunohistochemistry
Megjelenés:Journal of Comparative Neurology. - 478 : 1 (2004), p. 72-87. -
További szerzők:Serfőző Zoltán Gergely Pál (1947-) (biokémikus) Ito, Masaaki Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
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10.

001-es BibID:BIBFORM003579
Első szerző:Lontay Beáta (biokémikus)
Cím:Okadaic acid induces phosphorylatio and translocation of myosin phosphatase target subunit 1 influencing myosin phosphorylation, stress fiber assembly and cell migration in HepG2 cells / Lontay B., Kiss A., Gergely P., Hartshorne D. J., Erdődi F.
Dátum:2005
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
myosin phosphatase target subunit (MYPT)
protein phosphatase-1 (PP1) and -2A (PP2A)
Rho-kinase (ROK)
okadaic acid
HepG2 cells
confocal microscopy
cell migration
Megjelenés:Cellular Signalling. - 17 : 10 (2005), p. 1265-1275. -
További szerzők:Kiss Andrea (1979-) (biokémikus, vegyész) Gergely Pál (1947-) (biokémikus) Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
Internet cím:elektronikus változat
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11.

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
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12.

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)
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