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 contractilit...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2003-06, Vol.306 (2), p.550-557
Main Authors: Kiewitz, Roland, Acklin, Christian, Schäfer, Beat W, Maco, Bohumil, Uhrík, Branislav, Wuytack, Frank, Erne, Paul, Heizmann, Claus W
Format: Article
Language:English
Subjects:
Animals
Blotting, Northern
Blotting, Western
Calcium-Binding Proteins - metabolism
Calcium-Transporting ATPases - metabolism
Cells, Cultured
Chromatography
Electrophoresis, Polyacrylamide Gel
Humans
Mice
Microscopy, Confocal
Microscopy, Electron
Microscopy, Fluorescence
Microscopy, Immunoelectron
Myocardium - cytology
Myocardium - metabolism
Precipitin Tests
Protein Binding
S100 Proteins
Sarcoplasmic Reticulum Calcium-Transporting ATPases
Tissue Distribution
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Summary: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.
ISSN:0006-291X
DOI:10.1016/S0006-291X(03)00987-2