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001-es BibID:	BIBFORM049141
Első szerző:	Balogh Ágnes (kardiológus)
Cím:	Myofilament protein carbonylation contributes to the contractile dysfunction in the infarcted LV region of mouse hearts / Ágnes Balogh, David Santer, Enikő T. Pásztor, Attila Tóth, Dániel Czuriga, Bruno K. Podesser, Karola Trescher, Kornelia Jaquet, Ferenc Erdődi, István Édes, Zoltán Papp
Dátum:	2014
ISSN:	0008-6363
Megjegyzések:	Aims: The region-specific mechanical function of left ventricular (LV) murinecardiomyocytes and the role of phosphorylation and oxidative modifications of myofilamentproteins were investigated in the process of post-myocardial infarction (MI) remodeling 10weeks after ligation of the left anterior descending (LAD) coronary artery. Methods andResults: Permeabilized murine cardiomyocytes from the remaining anterior and a remotenoninfarcted inferior LV area were compared with those of noninfarcted age-matchedcontrols. Myofilament phosphorylation, sulfhydryl (SH) oxidation and carbonylation werealso assayed. The Ca2+ sensitivity of force production was significantly lower in the anteriorwall (pCa50:5.81?0.03, mean?SEM, at 2.3 ?m sarcomere length) than that in the controls(pCa50:5.91?0.02) or in the MI inferior area (pCa50:5.88?0.02). The level of troponin Iphosphorylation was lower and that of myofilament protein SH oxidation was higher in theanterior location relative to controls, but these changes did not explain the differences in Ca2+sensitivities. On the other hand, significantly higher carbonylation levels [e.g. in myosinheavy chain (MHC) and actin] were observed in the MI anterior wall [carbonylation index(CI), CIMHC:2.06?0.46, CIactin:1.46?0.18] than in the controls (CI:1). In vitro Fenton-basedmyofilament carbonylation in the control cardiomyocytes also decreased the Ca2+ sensitivityof force production irrespective of the phosphorylation status of the myofilaments.Furthermore, the Ca2+ sensitivity correlated strongly with myofilament carbonylation levels inall investigated samples. Conclusions: Post-MI myocardial remodeling involves increasedmyofibrillar protein carbonylation and decreased Ca2+ sensitivity of force production, leadingpotentially to contractile dysfunction in the remaining cardiomyocytes of the infarcted area.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Molekuláris Medicina contractile function infarction myocytes remodeling sarcomere
Megjelenés:	Cardiovascular Research. - 101 : 1 (2014), p. 108-119. -
További szerzők:	Santer, David Pásztorné Tóth Enikő (1966-) (laboratóriumi analitikus) Tóth Attila (1971-) (biológus) Czuriga Dániel (1982-) (kardiológus) Podesser, Bruno Karl Trescher, Karola Jaquet, Kornelia Erdődi Ferenc (1953-) (biokémikus) Édes István (1952-) (kardiológus) Papp Zoltán (1965-) (kardiológus, élettanász)
Pályázati támogatás:	TÁMOP-4.2.2/B-10/1-2010-0024 TÁMOP TÁMOP-4.2.2.A-11/1/KONV-2012-0045 TÁMOP K 109083 OTKA TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Biomolekuláris interakciók jellemzőinek kvantitatív meghatározása
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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:	BIBFORM028850
Első szerző:	Tóth Attila (biológus)
Cím:	Phosphorylation of MYPT1 by protein kinase C attenuates interaction with PP1 catalytic subunit and the 20 kDa light chain of myosin / Attila Tóth, Enikő Kiss, Pál Gergely, Michael P. Walsh, David J. Hartshorne, Ferenc Erdődi
Dátum:	2000
ISSN:	0014-5793
Megjegyzések:	Abstract The effect of phosphorylation in the N-terminal region of myosin phosphatase target subunit 1 (MYPT1) on the interactions with protein phosphatase 1 catalytic subunit (PP1c) and with phosphorylated 20 kDa myosin light chain (P-MLC20) was studied. Protein kinase C (PKC) phosphorylated threonine-34 (1 mol/mol), the residue preceding the consensus PP1c-binding motif ((35)KVKF(38)) in MYPT1(1-38), but this did not affect binding of the peptide to PP1c. PKC incorporated 2 mol P(i) into MYPT1(1-296) suggesting a second site of phosphorylation within the ankyrin repeats (residues 40-296). This phosphorylation diminished the stimulatory effect of MYPT1(1-296) on the P-MLC20 phosphatase activity of PP1c. Binding of PP1c or P-MLC20 to phosphorylated MYPT1(1-296) was also attenuated. It is concluded that phosphorylation of MYPT1 by PKC may therefore result in altered dephosphorylation of myosin.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	Febs Letters. - 484 : 2 (2000), p. 113-117. -
További szerzők:	Kiss Enikő Walsh, Michael P. Hartshorne, David J. Gergely Pál (1947-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus)
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001-es BibID:	BIBFORM028849
Első szerző:	Tóth Attila (biológus)
Cím:	Study of the subunit interactions in myosin phosphatase by surface plasmon resonance / Attila Tóth, Enikő Kiss, Friedrich W. Herberg, Pál Gergely, David J. Hartshorne, Ferenc Erdődi
Dátum:	2000
ISSN:	1432-1033
Megjegyzések:	he interactions of the catalytic subunit of type 1 protein phosphatase (PP1c) and the N-terminal half (residues 1-511) of myosin phosphatase target subunit 1 (MYPT1) were studied. Biotinylated MYPT1 derivatives were immobilized on streptavidin-biosensor chips, and binding parameters with PP1c were determined by surface plasmon resonance (SPR). The affinity of binding of PP1c was: MYPT11-296 > MYPT11-38 > MYPT123-38. No binding was detected with MYPT11-34, suggesting a critical role for residues 35-38, i.e. the PP1c binding motif. Binding of residues 1-22 was inferred from: a higher affinity binding to PP1c for MYPT11-38 compared to MYPT123-38, as deduced from SPR kinetic data and ligand competition assays; and an activation of the myosin light chain phosphatase activity of PP1c by MYPT11-38, but not by MYPT123-38. Residues 40-296 (ankyrin repeats) in MYPT11-296 inhibited the phosphorylase phosphatase activity of PP1c (IC50 = 0.2 nM), whereas MYPT11-38, MYPT123-38 or MYPT11-34 were without effect. MYPT140-511, which alone did not bind to PP1c, showed facilitated binding to the complexes of PP1c-MYPT11-38 and PP1c-MYPT123-38. The inhibitory effect of MYPT140-511 on the phosphorylase phosphatase activity of PP1c also was increased in the presence of MYPT11-38. The binding of MYPT1304-511 to complexes of PP1c and MYPT11-38, or MYPT11-296, was detected by SPR. These results suggest that within the N-terminal half of MYPT1 there are at least four binding sites for PP1c. The essential interaction is with the PP1c-binding motif and the other interactions are facilitated in an ordered and cooperative manner.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban egyetemen (Magyarországon) készült közlemény
Megjelenés:	European Journal Of Biochemistry. - 267 : 6 (2000), p. 1687-1697. -
További szerzők:	Kiss Enikő Herberg, Friedrich W. Hartshorne, David J. Gergely Pál (1947-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus)
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