Ca2+ -dependent interaction of S100A1 with the sarcoplasmic reticulum Ca2+ -ATPase2a and phospholamban in the human heart.

Abstract	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.
Authors	Roland Kiewitz, Christian Acklin, Beat W Schäfer, Bohumil Maco, Branislav Uhrík, Frank Wuytack, Paul Erne, Claus W Heizmann
Journal	Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 306 Issue 2 Pg. 550-7 (Jun 27 2003) ISSN: 0006-291X [Print] United States
PMID	12804600 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Calcium-Binding Proteins S100 Proteins S100A1 protein phospholamban Sarcoplasmic Reticulum Calcium-Transporting ATPases Calcium-Transporting ATPases
Topics	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, metabolism) Precipitin Tests Protein Binding S100 Proteins Sarcoplasmic Reticulum Calcium-Transporting ATPases Tissue Distribution

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