CCL

Összesen 12 találat.
#/oldal:
Részletezés:
Rendezés:

1.

001-es BibID:BIBFORM015074
Első szerző:Borbély Attila (kardiológus)
Cím:Cardiomyocyte Stiffness in Diastolic Heart Failure / Borbély A., van der Velden J., Papp Z., Bronzwaer J. G. F., Edes I., Stienen G. J. M., Paulus W. J.
Dátum:2005
ISSN:0009-7322
Megjegyzések:Heart failure with preserved left ventricular (LV) ejection fraction (EF) is increasingly recognized and usually referred to as diastolic heart failure (DHF). Its pathogenetic mechanism remains unclear, partly because of a lack of myocardial biopsy material. Endomyocardial biopsy samples obtained from DHF patients were therefore analyzed for collagen volume fraction (CVF) and sarcomeric protein composition and compared with control samples. Single cardiomyocytes were isolated from these biopsy samples to assess cellular contractile performance.METHODS AND RESULTS: DHF patients (n=12) had an LVEF of 71+/-11%, an LV end-diastolic pressure (LVEDP) of 28+/-4 mm Hg, and no significant coronary artery stenoses. DHF patients had higher CVFs (7.5+/-4.0%, P<0.05) than did controls (n=8, 3.8+/-2.0%), and no conspicuous changes in sarcomeric protein composition were detected. Cardiomyocytes, mechanically isolated and treated with Triton X-100 to remove all membranes, were stretched to a sarcomere length of 2.2 microm and activated with solutions containing varying [Ca2+]. Compared with cardiomyocytes of controls, cardiomyocytes of DHF patients developed a similar total isometric force at maximal [Ca2+], but their resting tension (F(passive)) in the absence of Ca2+ was almost twice as high (6.6+/-3.0 versus 3.5+/-1.7 kN/m2, P<0.001). F(passive) and CVF combined yielded stronger correlations with LVEDP than did either alone. Administration of protein kinase A (PKA) to DHF cardiomyocytes lowered F(passive) to control values.CONCLUSIONS: DHF patients had stiffer cardiomyocytes, as evident from a higher F(passive) at the same sarcomere length. Together with CVF, F(passive) determined in vivo diastolic LV dysfunction. Correction of this high F(passive) by PKA suggests that reduced phosphorylation of sarcomeric proteins is involved in DHF.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Circulation. - 111 : 6 (2005), p. 774-781. -
További szerzők:Velden, Jolanda, van der Papp Zoltán (1965-) (kardiológus, élettanász) Bronzwaer, Jean G. F. Édes István (1952-) (kardiológus) Stienen, Ger J. M. Paulus, Walter J.
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

2.

001-es BibID:BIBFORM010416
Első szerző:Borbély Attila (kardiológus)
Cím:Molecular determinants of heart failure with normal left ventricular ejection fraction / Borbely, A., Papp, Z., Edes, I., Paulus, W. J.
Dátum:2009
ISSN:1734-1140 (Print)
Megjegyzések:In population-based studies, heart failure with normal left ventricular (LV) ejection fraction (HFNEF) is now increasingly recognized and referred to as diastolic heart failure. However, the pathogenic mechanisms underlying HFNEF are incompletely understood, mainly because of limited availability of human myocardial biopsy material. Nevertheless, recent studies have examined in vivo hemodynamics, in vitro cardiomyocyte function, myofilamentary protein composition, collagen content and deposition of advanced glycation end products from LV endomyocardial biopsies. These measures were compared between HFNEF patients, subjects without symptoms of heart failure (controls), patients with heart failure and reduced ejection function (HFREF), and patients with HFNEF and HFREF with diabetes mellitus. This article summarizes the various findings of these studies and focuses on the possible correlations among altered LV myocardial structure, cardiomyocyte function, myofilamentary proteins, and extracellular matrices. These findings revealed novel mechanisms responsible for diastolic LV dysfunction, and they have important therapeutic implications, particularly HFNEF, for which a specific heart failure treatment strategy is largely lacking.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Diabetes Complications
Fibrosis
Glycosylation End Products, Advanced
Heart Failure, Diastolic
Hemodynamics
Humans
Microfilaments
Myocardium
Myocytes, Cardiac
Ventricular Dysfunction, Left
Ventricular Function, Left
Megjelenés:Pharmacological Reports. - 61 : 1 (2009), p. 139-145. -
További szerzők:Papp Zoltán (1965-) (kardiológus, élettanász) Édes István (1952-) (kardiológus) Paulus, Walter J.
Internet cím:elektronikus változat
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

3.

001-es BibID:BIBFORM010415
Első szerző:Borbély Attila (kardiológus)
Cím:Hypophosphorylation of the Stiff N2B titin isoform raises cardiomyocyte resting tension in failing human myocardium / Borbely, A., Falcao-Pires, I., van Heerebeek, L., Hamdani, N., Edes, I., Gavina, C., Leite-Moreira, A. F., Bronzwaer, J. G. F., Papp, Z., van der Velden, J., Stienen, G. J. M., Paulus, W. J.
Dátum:2009
ISSN:1524-4571 (Electronic)
Megjegyzések:High diastolic stiffness of failing myocardium results from interstitial fibrosis and elevated resting tension (F(passive)) of cardiomyocytes. A shift in titin isoform expression from N2BA to N2B isoform, lower overall phosphorylation of titin, and a shift in titin phosphorylation from N2B to N2BA isoform can raise F(passive) of cardiomyocytes. In left ventricular biopsies of heart failure (HF) patients, aortic stenosis (AS) patients, and controls (CON), we therefore related F(passive) of isolated cardiomyocytes to expression of titin isoforms and to phosphorylation of titin and titin isoforms. Biopsies were procured by transvascular technique (44 HF, 3 CON), perioperatively (25 AS, 4 CON), or from explanted hearts (4 HF, 8 CON). None had coronary artery disease. Isolated, permeabilized cardiomyocytes were stretched to 2.2-microm sarcomere length to measure F(passive). Expression and phosphorylation of titin isoforms were analyzed using gel electrophoresis with ProQ Diamond and SYPRO Ruby stains and reported as ratio of titin (N2BA/N2B) or of phosphorylated titin (P-N2BA/P-N2B) isoforms. F(passive) was higher in HF (6.1+/-0.4 kN/m(2)) than in CON (2.3+/-0.3 kN/m(2); P<0.01) or in AS (2.2+/-0.2 kN/m(2); P<0.001). Titin isoform expression differed between HF (N2BA/N2B=0.73+/-0.06) and CON (N2BA/N2B=0.39+/-0.05; P<0.001) and was comparable in HF and AS (N2BA/N2B=0.59+/-0.06). Overall titin phosphorylation was also comparable in HF and AS, but relative phosphorylation of the stiff N2B titin isoform was significantly lower in HF (P-N2BA/P-N2B=0.77+/-0.05) than in AS (P-N2BA/P-N2B=0.54+/-0.05; P<0.01). Relative hypophosphorylation of the stiff N2B titin isoform is a novel mechanism responsible for raised F(passive) of human HF cardiomyocytes.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Aged
Biopsy
Elasticity
Female
Heart Failure
Humans
Male
Middle Aged
Muscle Proteins
Myocardium
Myocytes, Cardiac
Phosphorylation
Protein Isoforms
Protein Kinases
Sarcomeres
Megjelenés:Circulation Research. - 104 : 6 (2009), p. 780-786. -
További szerzők:Falcao-Pires, Ines Heerebeek, Loek, van Hamdani, Nazha Édes István (1952-) (kardiológus) Gavina, Cristina Leite-Moreira, Adelino F. Bronzwaer, Jean G. F. Papp Zoltán (1965-) (kardiológus, élettanász) Velden, Jolanda, van der Stienen, Ger J. M. Paulus, Walter J.
Internet cím:DOI
elektronikus változat
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

4.

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
Borító:

5.

001-es BibID:BIBFORM030682
Első szerző:Czuriga Dániel (kardiológus)
Cím:Cellular mechanisms for diastolic dysfunction in the human heart / Czuriga D., Paulus W. J., Czuriga I., Edes I., Papp Z., Borbély A.
Dátum:2012
Megjegyzések:Left ventricular (LV) diastolic dysfunction is an important contributor to many different cardiovascular diseases. LV diastolic dysfunction can manifest itself as slow LV relaxation, slow LV filling or high diastolic LV stiffness. Diastolic abnormalities have been described in the senescent heart, in heart failure with normal ejection fraction (HFNEF), in diabetic cardiomyopathy, in aortic valve stenosis (AVS), in hypertrophic cardiomyopathy (HCM), as well as in Fabry disease (FD), however, exact cellular and molecular alterations behind the diastolic deterioration in these diseases are not yet completely characterized. Several studies thoroughly investigated altered cardiomyocyte function, changes of contractile myofilaments, extracellular collagen deposition and advanced glycation end products (AGEs) cross-linking in the background of diastolic dysfunction. These clinical and experimental data suggest that underlying mechanisms of LV diastolic dysfunction are divergent in different cardiac pathologies, therefore the present review aims to summarize mechanisms at the cellular level of diastolic abnormalities in various cardiovascular diseases.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Cardiomyocytes
Contractile dysfunction
Diabetes mellitus
Diastole
Fibrosis
Human heart
Megjelenés:Current Pharmaceutical Biotechnology. - 13 : 13 (2012), p. 2532-2538. -
További szerzők:Paulus, Walter J. Czuriga István (1948-2018) (kardiológus) Édes István (1952-) (kardiológus) Papp Zoltán (1965-) (kardiológus, élettanász) Borbély Attila (1978-) (kardiológus)
Pályázati támogatás:MEDIA-261409
FP7
Internet cím:Szerző által megadott URL
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

6.

001-es BibID:BIBFORM005631
Első szerző:Hamdani, Nazha
Cím:Myofilament dysfunction in cardiac disease from mice to men / Hamdani, N., de Waard, M., Messer, A. E., Boontje, N. M., Kooij, V., van Dijk, S., Versteilen, A., Lamberts, R., Merkus, D., Dos Remedios, C., Duncker, D. J., Borbely, A., Papp, Z., Paulus, W., Stienen, G. J. M., Marston, S. B., van der Velden, J.
Dátum:2008
ISSN:0142-4319 (Print)
Megjegyzések:In healthy human myocardium a tight balance exists between receptor-mediated kinases and phosphatases coordinating phosphorylation of regulatory proteins involved in cardiomyocyte contractility. During heart failure, when neurohumoral stimulation increases to compensate for reduced cardiac pump function, this balance is perturbed. The imbalance between kinases and phosphatases upon chronic neurohumoral stimulation is detrimental and initiates cardiac remodelling, and phosphorylation changes of regulatory proteins, which impair cardiomyocyte function. The main signalling pathway involved in enhanced cardiomyocyte contractility during increased cardiac load is the beta-adrenergic signalling route, which becomes desensitized upon chronic stimulation. At the myofilament level, activation of protein kinase A (PKA), the down-stream kinase of the beta-adrenergic receptors (beta-AR), phosphorylates troponin I, myosin binding protein C and titin, which all exert differential effects on myofilament function. As a consequence of beta-AR down-regulation and desensitization, phosphorylation of the PKA-target proteins within the cardiomyocyte may be decreased and alter myofilament function. Here we discuss involvement of altered PKA-mediated myofilament protein phosphorylation in different animal and human studies, and discuss the roles of troponin I, myosin binding protein C and titin in regulating myofilament dysfunction in cardiac disease. Data from the different animal and human studies emphasize the importance of careful biopsy procurement, and the need to investigate localization of kinases and phosphatases within the cardiomyocyte, in particular their co-localization with cardiac myofilaments upon receptor stimulation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Muscle Research and Cell Motility. - 29 : 6-8 (2008), p. 189-201. -
További szerzők:de Waard, Monique Messer, Andrew E. Boontje, Nicky M. Kooij, Viola Dijk, Sabine, van Versteilen, Amanda Lamberts, Regis Merkus, Daphne Dos Remedios, Cris Duncker, Dirk J. Borbély Attila (1978-) (kardiológus) Papp Zoltán (1965-) (kardiológus, élettanász) Paulus, Walter J. Stienen, Ger J. M. Marston, Steven B. Velden, Jolanda, van der
Internet cím:elektronikus változat
DOI
Borító:

7.

001-es BibID:BIBFORM075606
035-os BibID:(Wos)000453600400007 (Scopus)85054323122
Első szerző:Papp Zoltán (kardiológus, élettanász)
Cím:Molecular and pathophysiological links between heart failure with preserved ejection fraction and type 2 diabetes mellitus / Zoltán Papp, Tamás Radovits, Walter J. Paulus, Nazha Hamdani, Petar M. Seferović
Dátum:2018
ISSN:1388-9842 1879-0844
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:European Journal Of Heart Failure. - 20 : 12 (2018), p. 1649-1652. -
További szerzők:Radovits Tamás Paulus, Walter J. Hamdani, Nazha Seferović, Petar M.
Pályázati támogatás:NVKP-16-1-2016-0017
Egyéb
GINOP-2.3.2-15-2016-00043
GINOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

8.

001-es BibID:BIBFORM065595
Első szerző:Papp Zoltán (kardiológus, élettanász)
Cím:Rebuttal from Zoltán Papp, Attila Borbély and Walter J. Paulus / Zoltan Papp, Attila Borbely, Walter J. Paulus
Dátum:2014
ISSN:0022-3751
Tárgyszavak:Orvostudományok Elméleti orvostudományok hozzászólás
Megjelenés:Journal Of Physiology-London. - 592 : 3 (2014), p. 421-422. -
További szerzők:Borbély Attila (1978-) (kardiológus) Paulus, Walter J.
Pályázati támogatás:Health-2010 MEDIA-261409
FP7
TÁMOP-4.2.2.A-11/1/KONV-2012-0045
TÁMOP
Kardiológia Kutatócsoport
4.2.4. A/2?11?1?2012?0001
TÁMOP
K 109083
OTKA
PD 108614
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

9.

001-es BibID:BIBFORM092357
Első szerző:Stienen, Susan
Cím:Enhanced clinical phenotyping by mechanistic bioprofiling in heart failure with preserved ejection fraction: insights from the MEDIA-DHF study (The Metabolic Road to Diastolic Heart Failure) / Susan Stienen, Joao Pedro Ferreira, Masatake Kobayashi, Gregoire Preud'homme, Daniela Dobre, Jean-Loup Machu, Kevin Duarte, Emmanuel Bresso, Marie-Dominique Devignes, Natalia López, Nicolas Girerd, Svend Aakhus, Giuseppe Ambrosio, Hans-Peter Brunner-La Rocca, Ricardo Fontes-Carvalho, Alan G. Fraser, Loek van Heerebeek, Stephane Heymans, Gilles de Keulenaer, Paolo Marino, Kenneth McDonald, Alexandre Mebazaa, Zoltán Papp, Riccardo Raddino, Carsten Tschöpe, Walter J. Paulus, Faiez Zannad, Patrick Rossignol
Dátum:2020
ISSN:1354-750X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biomarkers. - 25 : 2 (2020), p. 201-211. -
További szerzők:Ferreira, João Pedro Kobayashi, Masatake Preud'homme, Gregoire Dobre, Daniela Machu, Jean-Loup Duarte, Kevin Bresso, Emmanuel Devignes, Marie-Dominique López, Natalia Girerd, Nicolas Aakhus, Svend Ambrosio, Giuseppe Brunner-La Rocca, Hans-Peter Fontes-Carvalho, Ricardo Fraser, Alan G. Heerebeek, Loek, van Heymans, Stephane De Keulenaer, Gilles Marino, Paolo McDonald, Kenneth Mebazaa, Alexandre Papp Zoltán (1965-) (kardiológus, élettanász) Raddino, Riccardo Tschöpe, Carsten Paulus, Walter J. Zannad, Faiez Rossignol, Patrick
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

10.

001-es BibID:BIBFORM090886
035-os BibID:(cikkazonosító)47 (WoS)000571013300001 (Scopus)85090068683
Első szerző:Stienen, Susan
Cím:Sex differences in circulating proteins in heart failure with preserved ejection fraction / Stienen Susan, Ferreira João Pedro, Kobayashi Masatake, Preud'homme Gregoire, Dobre Daniela, Machu Jean-Loup, Duarte Kevin, Bresso Emmanuel, Devignes Marie-Dominique, López Andrés Natalia, Girerd Nicolas, Aakhus Svend, Ambrosio Giuseppe, Brunner-La Rocca Hans-Peter, Fontes-Carvalho Ricardo, Fraser Alan G., van Heerebeek Loek, de Keulenaer Gilles, Marino Paolo, McDonald Kenneth, Mebazaa Alexandre, Papp Zoltan, Raddino Riccardo, Tschöpe Carsten, Paulus Walter J., Zannad Faiez, Rossignol Patrick
Dátum:2020
ISSN:2042-6410
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biology of Sex Differences. - 11 : 1 (2020), p. 1-14. -
További szerzők:Ferreira, João Pedro Kobayashi, Masatake Preud'homme, Gregoire Dobre, Daniela Machu, Jean-Loup Duarte, Kevin Bresso, Emmanuel Devignes, Marie-Dominique López Andrés, Natalia Girerd, Nicolas Aakhus, Svend Ambrosio, Giuseppe Brunner-La Rocca, Hans-Peter Fontes-Carvalho, Ricardo Fraser, Alan G. Heerebeek, Loek, van De Keulenaer, Gilles Marino, Paolo McDonald, Kenneth Mebazaa, Alexandre Papp Zoltán (1965-) (kardiológus, élettanász) Raddino, Riccardo Tschöpe, Carsten Paulus, Walter J. Zannad, Faiez Rossignol, Patrick
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

11.

001-es BibID:BIBFORM065084
Első szerző:Úri Katalin
Cím:Circulating ACE2 activity correlates with cardiovascular disease development / Katalin Úri, Miklós Fagyas, Attila Kertész, Attila Borbély, Csaba Jenei, Orsolya Bene, Zoltán Csanádi, Walter J. Paulus, István Édes, Zoltán Papp, Attila Tóth, Erzsébet Lizanecz
Dátum:2016
Megjegyzések:Abstract It was shown recently that Angiotensin Converting Enzyme activity is limited by endogenous inhibition in vivo, highlighting the importance of Angiotensin II elimination (ACE2). Potential contribution of the ACE2 to cardiovascular disease progression was addressed. Serum ACE2 activities were measured in different clinical states (healthy, n=45; hypertensive, n=239; heart failure (HF) with reduced ejection fraction (HFrEF), n=141 and HF with preserved ejection fraction (HFpEF), n=47). ACE2 activity was significantly higher in hypertensive patients (24.8?0.8U/ml) than that in healthy volunteers (16.2?0.8U/ml, P=0.01). ACE2 activity further increased in HFrEF patients (43.9?2.1U/ml, P=0.001) but not in HFpEF patients (24.6?1.9U/ml) when compared to hypertensive patients. Serum ACE2 activity negatively correlated with left ventricular systolic function in HFrEF, but not in hypertensive, HFpEF or healthy populations. Serum ACE2 activity had a fair diagnostic value to differentiate HFpEF from HFrEF patients in this study.Serum ACE2 activity correlates with cardiovascular disease development: it increases when hypertension developes and further increases when the cardiovascular disease further progresses to systolic dysfunction, suggesting that ACE2 metabolism plays a role in these processes. In contrast, serum ACE2 activity does not change when hypertension progresses to HFpEF, suggesting a different pathomechanism for HFpEF and proposing a biomarker based identification of these HF forms.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Angiotensin converting enzyme 2
diastolic heart failure
systolic heart failure
hypertension
renin-angiotensin-aldosterone system
biomarker
Megjelenés:Journal of the Renin-Angiotensin-Aldosterone System 17 : 4 (2016), p. 1-11. -
További szerzők:Fagyas Miklós (1984-) (orvos) Kertész Attila Béla (1973-) (kardiológus) Borbély Attila (1978-) (kardiológus) Jenei Csaba (1976-) (kardiológus) Bene Orsolya (1980-) (kardiológus) Csanádi Zoltán (1960-) (kardiológus) Paulus, Walter J. Édes István (1952-) (kardiológus) Papp Zoltán (1965-) (kardiológus, élettanász) Tóth Attila (1971-) (biológus) Lizanecz Erzsébet (1978-) (orvos)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

12.

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.
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Rekordok letöltése1