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1.

001-es BibID:BIBFORM030668
Első szerző:Ait Mou, Younss
Cím:Beneficial effects of SR33805 in failing myocardium / Ait Mou, Y., Toth, A., Cassan, C., Czuriga, D., de Tombe, P. P., Papp, Z., Lacampagne, A., Cazorla, O.
Dátum:2011
ISSN:0008-6363
Megjegyzések:Aims: SR33805, a potent Ca2+ channel blocker, increases cardiac myofilament Ca2+ sensitivity in healthy rat cardiomyocytes. Therefore, the aim of the present study was to evaluate the effects of SR33805 on contractile properties in ischaemic failing hearts after myocardial infarction (MI) in vivo and in vitro at the cellular level. Methods and results: The effect of SR33805 (10 mM) was tested on the excitation?contraction coupling of cardiomyocytes isolated from rat with end-stage heart failure. Cell shortening and Ca2+ transients were measured in intact cardiomyocytes, while contractile properties were determined in Triton X-100 permeabilized myocytes. Acute treatment with SR33805 restored the MI-altered cell shortening without affecting the Ca2+ transient amplitude, suggesting an increase of myofilament Ca2+ sensitivity in MI myocytes. Indeed, a SR33805-induced sensitization of myofilament activation was found to be associated with a slight increase in myosin light chain-2 phosphorylation and a more significant decrease on troponin I (TnI) phosphorylation. Decreased TnI phosphorylation was related to inhibition of protein kinase A activity by SR33805. Finally, administration of a single intra-peritoneal bolus of SR33805 (20 mg/kg) improved endsystolic strain and fractional shortening of MI hearts. Conclusion: The present study indicates that treatment with SR33805 improved contractility of ischaemic failing hearts after MI in the rat by selectively modulating the phosphorylation status of sarcomeric regulatory proteins, which then sensitized the myofilaments to Ca2+. Our results gave a proof of concept that manipulation of the Ca2+ sensitivity of sarcomeric regulatory proteins can be used to improve contractility of a failing heart.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Myocytes
Heart failure
Contractile function
Sarcomere
Ventricular function
Megjelenés:Cardiovascular Research. - 91 : 3 (2011), p. 412-419. -
További szerzők:Tóth Attila (1971-) (biológus) Cassan, Cécile Czuriga Dániel (1982-) (kardiológus) de Tombe, Pieter P. Papp Zoltán (1965-) (kardiológus, élettanász) Lacampagne, Alain Cazorla, Olivier
Pályázati támogatás:INSERM
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Intézményi repozitóriumban (DEA) tárolt változat
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2.

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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Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM078999
035-os BibID:(cikkazonosító)P568
Első szerző:Bánhegyi Viktor (kardiológus)
Cím:Old dogma, new aspects : role of angiotensin converting enzymes in the cardiovascular continuum / V. Bánhegyi, M. Fagyas, I. Mányiné Siket, A. Enyedi, K. Bottyán, I. Édes, Z. Papp, A. Tóth
Dátum:2018
ISSN:0008-6363
Megjegyzések:The renin angiotensin aldosterone system (RAAS) plays a pivotal role in the cardiovascular pathophysiology and represents a starting point of cardiovascular diseases. Textbooks agree that the angiotensin converting enzyme (ACE) is produced in human endothelia related tissues. The goal of my work is to investigate this fact and the endothelia related enzymes (ACE, ACE2) in contrast of their endogenous regulation and secretion processes in a clinical based study. Lung tissue- and blood samples were collected from patients with lung surgery at the Department of Thoracic Surgery, University of Debrecen (n=71). We performed fluorescent based ACE, ACE2 activity measurements and ELISA experiments. In addition, we determined the ACE genotype and recorded the medical history. To the investigation of the ACE secretion mechanism, primary Human Aortic Endothelial Cells (HAOEC) was used under cell cultured circumstances. To measure the proper activity of tissue bound ACE2 we performed experiments with the special fluorescent substrate Abz-SPY (3-nitro). We found a significantly elevated ACE activity in the circulation respectively genotype groups ID (9.645 ± 0.4223 U/ml, n=36, p=0.0043) and DD (11.20 ± 0.6203 U/ml, n=26, p=0.0005) when compared to II (6.966 ± 0.5166 U/ml, n=9) group. Surprisingly, we did not find any genotype difference among the ACE activities in the lung tissue (ID: 3.034 ± 0.1996 U/ml, n=36, p=0.6421; DD: 2.709 ± 0.2495 U/ml, n=26, p=0.7920) when compared to the II (2.833 ± 0.3179 U/ml, n=9) patient group. Furthermore, signs for endogenous ACE inhibition were found. The direct administration of ACE specific substrate Abz-FRK (Dnp) to our HAOEC cell culture resulted 299.6 U/ml ACE activity which was inhibited over 90% via 200 nM Captopril. On the contrary, we cannot reveal any ACE2 specific activity in our cell culture system. Experiments with fluorescent substrate Abz-SPY (3-nitro) did not reveal any ACE2 signal in circulation in contrary at tissue related milieu we were able to measure ACE2 activity with high specificity. Our data suggests that the genotype dependent source of ACE significantly contributes to the circulating ACE, which is different from the lung. The endogenous inhibition of ACE conveys the idea that ACE activity is endogenously regulated in vivo. HAOEC cell culture provides an optimal model system for investigation of the mechanism of ACE secretion. Abz-SPY (3-nitro) is a specific fluorescent substrate for tissue related ACE2 activity measurement which can help us to understand how the ACE2 shed into the circulation. All in all, these results could help us in the understanding of how a cardiovascular disease starts and evolves.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idézhető absztrakt
Megjelenés:Cardiovascular Research. - 114 : Suppl1 (2018), p. S139. -
További szerzők:Fagyas Miklós (1984-) (orvos) Mányiné Siket Ivetta (1962-) (laborasszisztens) Enyedi Attila (1975-) (sebész) Bottyán Klaudia Édes István (1952-) (kardiológus) Papp Zoltán (1965-) (kardiológus, élettanász) Tóth Attila
Pályázati támogatás:GINOP-2.3.2-15-2016-00043
GINOP
OTKA 116940
OTKA
EFOP-3.6.2-16-2017-00006
EFOP
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Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM004074
Első szerző:Birinyi Péter (élettanász)
Cím:The Na+/Ca2+ exchange blocker SEA0400 fails to enhance cytosolic Ca2+ transient and contractility in canine ventricular cardiomyocytes / Birinyi P., Tóth A., Jóna I., Acsai K., Almássy J., Nagy N., Prorok J., Gherasim I., Papp Z., Hertelendi Z., Szentandrássy N., Bányász T., Fülöp F., Papp J. G., Varró A., Nánási P. P., Magyar J.
Dátum:2008
Megjegyzések:Aims This study was designed to evaluate the effects of the Na+/Ca2+ exchange (NCX) inhibitor SEA0400 on Ca2+ handling in isolated canine ventricular myocytes. Methods and results Intracellular Ca2+ ([Ca2+](i)) transients, induced by either field stimulation or caffeine flush, were monitored using Ca2+ indicator dyes. [Ca2+](i)-dependent modulation of the inhibitory effect of SEA0400 on NCX was characterized by the changes in Ni2+-sensitive current in voltage-clamped myocytes. Sarcoplasmic reticulum (SR) Ca2+ release and uptake were studied in SIR membrane vesicles. Gating properties of single-ryanodine receptors were analysed in lipid bilayers. Ca2+ sensitivity of the contractile machinery was evaluated in chemically skinned myocytes. In myocytes paced at 1 Hz, neither diastolic [Ca2+](i) nor the amplitude of [Ca2+](i) transients was significantly altered by SEA0400 up to the concentration of 1 mu M, which was shown to inhibit the exchange current. The blocking effect of SEA0400 on NCX decreased with increasing [Ca2+](i), and it was more pronounced in reverse than in forward mode operation at every [Ca2+](i) examined. The rate of decay of the caffeine-induced [Ca2+](i) transients was decreased significantly by 1 mu M SEA0400; however, this effect was only a fraction of that observed with 10 mM NiCl2. Neither SR Ca2+ release and uptake nor cell shortening and Ca2+ sensitivity of the contractile proteins were influenced by SEA0400. Conclusion The lack of any major SEA0400-induced shift in Ca2+ transients or contractility of myocytes can well be explained by its limited inhibitory effect on NCX (further attenuated by elevated [Ca2+](i) levels) and a concomitant reduction in Ca2+ influx due to the predominantly reverse mode blockade of NCX and suppression of L-type Ca2+ current.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cardiovascular Research. - 78 : 3 (2008), p. 476-484. -
További szerzők:Tóth András (farmakológus) Jóna István (1948-) (élettanász, fizikus) Acsai Károly Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Nagy Norbert (1977-) (kísérletes farmakológus) Prorok János Gherasim, Iuliana Papp Zoltán (1965-) (kardiológus, élettanász) Hertelendi Zita (1978-) (orvos) Szentandrássy Norbert (1976-) (élettanász) Bányász Tamás (1960-) (élettanász) Fülöp Ferenc Papp Gy. Julius (Szeged) Varró András (1954-) (farmakológus, klinikai farmakológus) Nánási Péter Pál (1956-) (élettanász) Magyar János (1961-) (élettanász)
Internet cím:elektronikus változat
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5.

001-es BibID:BIBFORM003575
Első szerző:Borbély Attila (kardiológus)
Cím:Peroxynitrite-induced alpha-actinin nitration and contractile alterations in isolated human myocardial cells / Borbély A., Tóth A., Édes I., Virág L., Papp J. G., Varró A., Paulus W. J., van der Velden J., Stienen G. J. M., Papp Z.
Dátum:2005
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
myocytes
contractile function
peroxynitrite
alpha-actinin
human myocardium
Megjelenés:Cardiovascular Research. - 67 : 2 (2005), p. 225-233. -
További szerzők:Tóth Attila (1971-) (biológus) Édes István (1952-) (kardiológus) Virág László (1965-) (biokémikus, sejtbiológus, farmakológus) Papp Gy. Julius (Szeged) Varró András (1954-) (farmakológus, klinikai farmakológus) Paulus, Walter J. Velden, Jolanda, van der Stienen, Ger J. M. Papp Zoltán (1965-) (kardiológus, élettanász)
Internet cím:elektronikus változat
DOI
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6.

001-es BibID:BIBFORM086625
035-os BibID:(WoS)000613754100027 (Scopus)85089611909
Első szerző:Kolijn, Detmar
Cím:Empagliflozin Improves Endothelial and Cardiomyocyte Function in Human Heart Failure With Preserved Ejection Fraction via Reduced Pro-Inflammatory-Oxidative Pathways and Protein Kinase Gα Oxidation / Detmar Kolijn, Steffen Pabel, Yanna Tian, Mária Lódi, Melissa Herwig, Albino Carrizzo, Saltanat Zhazykbayeva, Árpád Kovács, Gábor Á. Fülöp, Inês Falcao-Pires, Peter H. Reusch, Sophie Van Linthout, Zoltán Papp, Loek van Heerebeek, Carmine Vecchione, Lars S. Maier, Michele Ciccarelli, Carsten Tschöpe, Andreas Mügge, Zsolt Bagi, Samuel Sossalla, Nazha Hamdani
Dátum:2021
ISSN:0008-6363
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Cardiovascular Research. - 117 : 2 (2021), p. 495-507. -
További szerzők:Pabel, Steffen Tian, Yanna Lódi Mária (1991-) Herwig, Melissa Carrizzo, Albino Zhazykbayeva, Saltanat Kovács Árpád (1986-) (kardiológus) Fülöp Gábor Áron (1988-) (általános orvos) Falcao-Pires, Ines Reusch, Peter H. Linthout, Sophie Van Papp Zoltán (1965-) (kardiológus, élettanász) Heerebeek, Loek, van Vecchione, Carmine Maier, Lars S. Ciccarelli, Michele Tschöpe, Carsten Mügge, Andreas Bagi Zsolt (1974-) (orvos) Sossalla, Samuel Hamdani, Nazha
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Intézményi repozitóriumban (DEA) tárolt változat
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7.

001-es BibID:BIBFORM040577
Első szerző:Papp Zoltán (kardiológus, élettanász)
Cím:Calpain-I induced alterations in the cytoskeletal structure and impaired mechanical properties of single myocytes of rat heart / Zoltán Papp, Jolanda van der Velden, G. J. M. Stienen
Dátum:2000
ISSN:0008-6363
Megjegyzések:Objective: The involvement of Calpain-I mediated proteolysis has been implicated in myofibrillar dysfunction of reperfused myocardium following ischemia (stunning). This study addresses the question whether ultrastructural alterations might be responsible for the depressed contractility. Methods: Mechanical properties and protein composition of isolated myocytes after Calpain-I exposure (1.25 U/ml; 10 min; 15°C; pCa 5.0) and of ischemic rat hearts following reperfusion were characterized. Results: Maximal isometric force (44±5 kN/m2) at pCa 4.5 (pCa=-log[Ca2+]) decreased by 42.5% in Triton permeabilized myocytes (n=11) after Calpain-I treatment. Force (and consequent myofilament disarrangement) during Calpain-I treatment was prevented by 40 mM BDM. The contractile force of Calpain-I exposed myocytes was significantly higher at submaximal levels of activation (pCa 5.5, 5.4 and 5.3) before maximal force development (pCa 4.5) than after maximal force development. The pCa50 value (5.40±0.02) determined from these initial test contractures did not differ significantly from that of untreated controls (5.44±0.03). However, after full activation Ca2+-sensitivity of force production in Calpain-I treated myocytes was significantly reduced (pCa50 5.34±0.02). This change in pCa50 was positively correlated with the reduction in maximal isometric force and was accompanied by sarcomere disorder. These findings imply that at least part of the Calpain-I induced mechanical alterations are dependent on force history. Measurements of the rate of force redevelopment after unloaded shortening suggested that Calpain-I did not affect cross-bridge kinetics. SDS gel electrophoresis and Western immunoblotting of Calpain-I treated myocytes revealed desmin degradation. The desmin content of postischemic myocardium was also reduced. Conclusion: Our results indicate that ultrastructural alterations may play an important role in the Calpain-I mediated cardiac dysfunction.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cardiovascular Research. - 45 : 4 (2000), p. 981-993. -
További szerzők:Velden, Jolanda, van der Stienen, Ger J. M.
Pályázati támogatás:NWO-OTKA
Egyéb
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8.

001-es BibID:BIBFORM018436
Első szerző:Rutkai Ibolya (molekuláris biológus)
Cím:Activation of prostaglandin E2 EP1 receptor increases arteriolar tone and blood pressure in mice with type 2 diabetes / Rutkai, I., Feher, A., Erdei, N., Henrion, D., Papp, Z., Edes, I., Koller, A., Kaley, G., Bagi, Z.
Dátum:2009
ISSN:0008-6363
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
diabetes
hypertension
arteriole
prostanoid
EP receptor
Megjelenés:Cardiovascular Research. - 83 : 1 (2009), p. 148-154. -
További szerzők:Fehér Attila (1982-) (orvos) Erdei Nóra (1979-) (orvos) Henrion, Daniel Papp Zoltán (1965-) (kardiológus, élettanász) Édes István (1952-) (kardiológus) Koller Ákos Kaley Gábor Bagi Zsolt (1974-) (orvos)
Pályázati támogatás:449/2006
OTKA
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Intézményi repozitóriumban (DEA) tárolt változat
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9.

001-es BibID:BIBFORM040584
Első szerző:Velden, Jolanda, van der
Cím:The effect of myosin light chain 2 dephosphorylation on Ca2+ -sensitivity of force is enhanced in failing human hearts / van der Velden J., Papp Z., Boontje N. M., Zaremba R., de Jong J. W., Janssen P. M., Hasenfuss G., Stienen G. J.
Dátum:2003
ISSN:0008-6363
Megjegyzések:OBJECTIVE: Phosphorylation of the myosin light chain 2 (MLC-2) isoform expressed as a percentage of total MLC-2 was decreased in failing (21.1+/-2.0%) compared to donor (31.9+/-4.8%) hearts. To assess the functional implications of this change, we compared the effects of MLC-2 dephosphorylation on force development in failing and non-failing (donor) human hearts. METHODS: Cooperative effects in isometric force and rate of force redevelopment (K(tr)) were studied in single Triton-skinned human cardiomyocytes at various [Ca(2+)] before and after protein phosphatase-1 (PP-1) incubation. RESULTS: Maximum force and K(tr) values did not differ between failing and donor hearts, but Ca(2+)-sensitivity of force (pCa(50)) was significantly higher in failing myocardium (Deltap Ca(50)=0.17). K(tr) decreased with decreasing [Ca(2+)], although this decrease was less in failing than in donor hearts. Incubation of the myocytes with PP-1 (0.5 U/ml; 60 min) decreased pCa(50) to a larger extent in failing (0.20 pCa units) than in donor cardiomyocytes (0.10 pCa units). A decrease in absolute K(tr) values was found after PP-1 in failing and donor myocytes, while the shape of the K(tr)-Ca(2+) relationships remained unaltered. CONCLUSIONS: Surprisingly, the contractile response to MLC-2 dephosphorylation is enhanced in failing hearts, despite the reduced level of basal MLC-2 phosphorylation. The enhanced response to MLC-2 dephosphorylation in failing myocytes might result from differences in basal phosphorylation of other thin and thick filament proteins between donor and failing hearts. Regulation of Ca(2+)-sensitivity via MLC-2 phosphorylation may be a potential compensatory mechanism to reverse the detrimental effects of increased Ca(2+)-sensitivity and impaired Ca(2+)-handling on diastolic function in human heart failure.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cardiovascular Research. - 57 : 2 (2003), p. 505-514. -
További szerzők:Papp Zoltán (1965-) (kardiológus, élettanász) Boontje, Nicky M. Zaremba, Ruud de Jong, J. W. Janssen, P. M. L. Hasenfuß, Gerd Stienen, Ger J. M.
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

10.

001-es BibID:BIBFORM040582
Első szerző:Velden, Jolanda, van der
Cím:Increased Ca2+-sensitivity of the contractile apparatus in end-stage human heart failure results from altered phosphorylation of contractile proteins / van der Velden J., Papp Z., Zaremba R., Boontje N. M., de Jong J. W., Owen V. J., Burton P. B., Goldmann P., Jaquet K., Stienen G. J.
Dátum:2003
ISSN:0008-6363
Megjegyzések:OBJECTIVE: The alterations in contractile proteins underlying enhanced Ca(2+)-sensitivity of the contractile apparatus in end-stage failing human myocardium are still not resolved. In the present study an attempt was made to reveal to what extent protein alterations contribute to the increased Ca(2+)-responsiveness in human heart failure. METHODS: Isometric force and its Ca(2+)-sensitivity were studied in single left ventricular myocytes from non-failing donor (n=6) and end-stage failing (n=10) hearts. To elucidate which protein alterations contribute to the increased Ca(2+)-responsiveness isoform composition and phosphorylation status of contractile proteins were analysed by one- and two-dimensional gel electrophoresis and Western immunoblotting. RESULTS: Maximal tension did not differ between myocytes obtained from donor and failing hearts, while Ca(2+)-sensitivity of the contractile apparatus (pCa(50)) was significantly higher in failing myocardium (deltapCa(50)=0.17). Protein analysis indicated that neither re-expression of atrial light chain 1 and fetal troponin T (TnT) nor degradation of myosin light chains and troponin I (TnI) are responsible for the observed increase in Ca(2+)-responsiveness. An inverse correlation was found between pCa(50) and percentage of phosphorylated myosin light chain 2 (MLC-2), while phosphorylation of MLC-1 and TnT did not differ between donor and failing hearts. Incubation of myocytes with protein kinase A decreased Ca(2+)-sensitivity to a larger extent in failing (deltapCa(50)=0.20) than in donor (deltapCa(50)=0.03) myocytes, abolishing the difference in Ca(2+)-responsiveness. An increased percentage of dephosphorylated TnI was found in failing hearts, which significantly correlated with the enhanced Ca(2+)-responsiveness.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cardiovascular Research. - 57 : 1 (2003), p. 37-47. -
További szerzők:Papp Zoltán (1965-) (kardiológus, élettanász) Zaremba, Ruud Boontje, Nicky M. de Jong, J. W. Owen, V. J. Burton, P. B. Goldmann, P. Jaquet, Kai Stienen, Ger J. M.
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

11.

001-es BibID:BIBFORM015092
Első szerző:Velden, Jolanda, van der
Cím:Functional effects of protein kinase C-mediated myofilament phosphorylation in human myocardium / van der Velden J., Narolska N. A., Lamberts R. R., Boontje N. M., Borbély A., Zaremba R., Bronzwaer J. G. F., Papp Z., Jaquet K., Paulus W. J., Stienen G. J.
Dátum:2006
ISSN:0008-6363
Megjegyzések:In human heart failure beta-adrenergic-mediated protein kinase A (PKA) activity is down-regulated, while protein kinase C (PKC) activity is up-regulated. PKC-mediated myofilament protein phosphorylation might be detrimental for contractile function in cardiomyopathy. This study was designed to reveal the effects of PKC on myofilament function in human myocardium under basal conditions and upon modulation of protein phosphorylation by PKA and phosphatases.METHODS: Isometric force was measured at different [Ca(2+)] in single permeabilized cardiomyocytes from non-failing and failing human left ventricular tissue. Basal phosphorylation of myofilament proteins and the influence of PKC, PKA, and phosphatase treatments were analyzed by one- and two-dimensional gel electrophoresis, Western immunoblotting, and ELISA.RESULTS: Troponin I (TnI) phosphorylation at the PKA sites was decreased in failing compared to non-failing hearts and correlated well with myofilament Ca(2+) sensitivity (pCa(50)). Incubation with the catalytic domain of PKC slightly decreased maximal force under basal conditions, but not following PKA and phosphatase pretreatments. PKC reduced Ca(2+) sensitivity to a larger extent in failing (DeltapCa(50)=0.19+/-0.03) than in non-failing (DeltapCa(50)=0.08+/-0.01) cardiomyocytes. This shift was reduced, though still significant, when PKC was preceded by PKA, while PKA following PKC did not further decrease pCa(50). Protein analysis indicated that PKC phosphorylated PKA sites in human TnI and increased phosphorylation of troponin T, while myosin light chain phosphorylation remained unaltered.CONCLUSION: In human myocardium PKC-mediated myofilament protein phosphorylation only has a minor effect on maximal force development. The PKC-mediated decrease in Ca(2+) sensitivity may serve to improve diastolic function in failing human myocardium in which PKA-mediated TnI phosphorylation is decreased.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cardiovascular Research. - 69 : 4 (2006), p. 876-887. -
További szerzők:Narolska, Nadiya A. Lamberts, Regis Boontje, Nicky M. Borbély Attila (1978-) (kardiológus) Zaremba, Ruud Bronzwaer, Jean G. F. Papp Zoltán (1965-) (kardiológus, élettanász) Jaquet, Kornelia Paulus, Walter J. Stienen, Ger J. M.
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