Ca2+-dependent interaction of S100A1 with the sarcoplasmic reticulum Ca2+-ATPase2a and phospholamban in the human heart
Copyright policy )Ca2+-dependent interaction of S100A1 with the sarcoplasmic reticulum Ca2+-ATPase2a and phospholamban in the human heart
The Ca(2+)-binding S100A1 protein displays a specific and high expression level in the human myocardium and is considered to be an important regulator of heart contractility. Diminished protein levels detected in dilated cardiomyopathy possibly contribute to impaired Ca(2+) handling and contractility in heart failure. To elucidate the S100A1 signaling pathway in the human heart, we searched for S100A1 target proteins by applying S100A1-specific affinity chromatography and immunoprecipitation techniques. We detected the formation of a Ca(2+)-dependent complex of S100A1 with SERCA2a and PLB in the human myocardium. Using confocal laser scanning microscopy, we showed that all three proteins co-localize at the level of the SR in primary mouse cardiomyocytes and confirmed these results by immunoelectron microscopy in human biopsies. Our results support a regulatory role of S100A1 in the contraction-relaxation cycle in the human heart.
- University of Zurich Switzerland
- Slovak Academy of Sciences Slovakia
- University of Queensland Australia
- University of Queensland Australia
- KU Leuven Belgium
Biochemistry & Molecular Biology, Subcellular-localization, 570, Mouse, 572, Blotting, Western, Biophysics, Expression, Calcium-Transporting ATPases, Ca2+-binding Protein, Contractility, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Mice, Animals, Humans, Family, Tissue Distribution, Microscopy, Immunoelectron, Cells, Cultured, Chromatography, Microscopy, Confocal, Myocardium, Calcium-Binding Proteins, S100 Proteins, Blotting, Northern, Precipitin Tests, Ca2+, Microscopy, Electron, calcium-binding proteins, Microscopy, Fluorescence, Electrophoresis, Polyacrylamide Gel, human heart, S100 proteins, cardiomyopathy, Protein Binding
Biochemistry & Molecular Biology, Subcellular-localization, 570, Mouse, 572, Blotting, Western, Biophysics, Expression, Calcium-Transporting ATPases, Ca2+-binding Protein, Contractility, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Mice, Animals, Humans, Family, Tissue Distribution, Microscopy, Immunoelectron, Cells, Cultured, Chromatography, Microscopy, Confocal, Myocardium, Calcium-Binding Proteins, S100 Proteins, Blotting, Northern, Precipitin Tests, Ca2+, Microscopy, Electron, calcium-binding proteins, Microscopy, Fluorescence, Electrophoresis, Polyacrylamide Gel, human heart, S100 proteins, cardiomyopathy, Protein Binding
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).72 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
Citations provided by BIP!Popularity provided by BIP!