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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Kiewitz R,Acklin C,Schäfer BW,Maco B,Uhrík B,Wuytack F,Erne P,Heizmann CWdoi
10.1016/s0006-291x(03)00987-2subject
Has Abstractpub_date
2003-06-27 00:00:00pages
550-7issue
2eissn
0006-291Xissn
1090-2104pii
S0006291X03009872journal_volume
306pub_type
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