S100A1 decreases calcium spark frequency and alters their spatial characteristics in permeabilized adult ventricular cardiomyocytes.
Völkers M, Loughrey CM, MacQuaide N, Remppis BA, DeGeorge BR, von Wegner F, Friedrich O, Fink R, Koch WJ, Smith GL, Most P (2007)
Publication Language: English
Publication Status: Published
Publication Type: Journal article, Original article
Publication year: 2007
Journal
Publisher: Elsevier
Book Volume: 41
Pages Range: 135-43
Journal Issue: 2
URI: http://www.sciencedirect.com/science/article/pii/S0143416006001138
DOI: 10.1016/j.ceca.2006.06.001
Abstract
S100A1, a Ca2+-sensor protein of the EF-hand type, exerts positive inotropic effects in the heart via enhanced cardiac ryanodine receptor (RyR2) activity. Here we report that S100A1 protein (0.1microM) interacts with the RyR2 in resting permeabilized cardiomyocytes at free Ca2+-levels comparable to diastolic Ca2+-concentrations ( approximately 150nM). Alterations of RyR2 function due to S100A1 binding was assessed via analysis of Ca2+-spark characteristics. Ca2+-spark frequency, amplitude and duration were all reduced upon perfusion with 0.1microM S100A1 protein by 38%, 14% and 18%, respectively. Most likely, these effects were conveyed through the S100A1 C-terminus (S100A1-ct; amino acids 75-94) as the corresponding S100A1-ct peptide (0.1microM) inhibited S100A1 protein binding to the RyR2 and similarly attenuated frequency, amplitude and duration of Ca2+-sparks by 52%, 8% and 26%, respectively. Accordingly, the sarcoplasmic reticulum (SR) Ca2+-content was slightly increased but the stoichiometry of other accessory RyR2 modulators (sorcin/FKBP12.6) remained unaltered by S100A1. Hence, we propose S100A1 as a novel inhibitory modulator of RyR2 function at diastolic Ca2+-concentrations in rabbit ventricular cardiomyocytes.
Authors with CRIS profile
Involved external institutions
Ruprecht-Karls-Universität Heidelberg
Germany (DE)
Temple University
United States (USA) (US)
University of Glasgow
United Kingdom (GB)
Thomas Jefferson University
United States (USA) (US)
Goethe-Universität Frankfurt am Main
Germany (DE)
Universitätsklinikum Heidelberg
Germany (DE)
Germany (DE)
Temple University
United States (USA) (US)
University of Glasgow
United Kingdom (GB)
Thomas Jefferson University
United States (USA) (US)
Goethe-Universität Frankfurt am Main
Germany (DE)
Universitätsklinikum Heidelberg
Germany (DE)
How to cite
APA:
Völkers, M., Loughrey, C.M., MacQuaide, N., Remppis, B.A., DeGeorge, B.R., von Wegner, F.,... Most, P. (2007). S100A1 decreases calcium spark frequency and alters their spatial characteristics in permeabilized adult ventricular cardiomyocytes. Cell Calcium, 41(2), 135-43. https://dx.doi.org/10.1016/j.ceca.2006.06.001
MLA:
Völkers, Mirko, et al. "S100A1 decreases calcium spark frequency and alters their spatial characteristics in permeabilized adult ventricular cardiomyocytes." Cell Calcium 41.2 (2007): 135-43.
BibTeX: Download