Browsing by Author "Papp, Zoltan"

In 2014, the Heart Failure Association (HFA) of the European Society of Cardiology (ESC) founded the first open access journal focusing on heart failure, called ESC Heart Failure (ESC-HF). In the first 5 years, in ESC-HF we published more than 450 articles. Through ESC-HF, the HFA gives room for heart failure research output from around the world. A transfer process from the European Journal of Heart Failure to ESC-HF has also been installed. As a consequence, in 2018 ESC-HF received 289 submissions, and published 148 items (acceptance rate 51%). The journal is listed in Scopus since 2014 and on the PubMed website since 2015. In 2019, we received our first impact factor from ISI Web of Knowledge / Thomson-Reuters, which is 3.407 for 2018. This report reviews which papers get best cited. Not surprisingly, many of the best cited papers are reviews and facts & numbers mini reviews, but original research is also well cited.

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 (Kt,) were studied in single Triton-skinned human cardiomyocytes at various [Ca2+] before and after protein phosphatase-1 (PP-1) incubation. Results: Maximum force and K, values did not differ between failing and donor hearts, but Ca2+-sensitivity of force (pCa(50)) was significantly higher in failing myocardium (DeltapCa(50)=0.17). K-tr decreased with decreasing [Ca2+], 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-Ca2+ 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 Ca2+-sensitivity via MLC-2 phosphorylation may be a potential compensatory mechanism to reverse the detrimental effects of increased Ca2+-sensitivity and impaired Ca2+-handling on diastolic function in human heart failure. (C) 2003 European Society of Cardiology. Published by Elsevier Science B.V. All rights reserved.