Ultrastructural distribution of the S100A1 Ca2+-binding protein in the human heart

Maco, B, Mandinova, A, Durrenberger, MB, Schafer, BW, Uhrik, B and Heizmann, CW (2001) Ultrastructural distribution of the S100A1 Ca2+-binding protein in the human heart. Physiological Research, 50 6: 567-574.

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Author Maco, B
Mandinova, A
Durrenberger, MB
Schafer, BW
Uhrik, B
Heizmann, CW
Title Ultrastructural distribution of the S100A1 Ca2+-binding protein in the human heart
Journal name Physiological Research   Check publisher's open access policy
ISSN 0862-8408
Publication date 2001
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 50
Issue 6
Start page 567
End page 574
Total pages 8
Place of publication Prague, Czech Republic
Publisher Acad Sciences Czech Republic, Inst Physiology
Language eng
Abstract Impaired calcium homeostasis and altered expression of Ca2+-binding proteins are associated with cardiomyopathies, myocardial hypertrophy, infarction or ischemia. S100A1 protein with its modulatory effect on different target proteins has been proposed as one of potential candidates which could participate in these pathological processes. The exact localization of S100A1 in human heart cells on the ultrastructural level accompanied with biochemical determination of its target proteins may help clarify the role of S100A1 in heart muscle. In the present study the distribution of the S100A1 protein using postembedding (Lowicryl K4M) immunocytochemical method in human heart muscle has been determined quantitatively, relating number of antigen sites to the unit area of a respective structural component. S100A1 antigen sites have been detected in elements of sarcoplasmic reticulum (SR), in myofibrils at all levels of sarcomere and in mitochondria, the density of immunolabeling at Z-lines being about 3 times and at SR more than 5 times higher than immunolabeling of remaining structural components. The presence of the S100A1 in SR and myofibrils may be related to the known target proteins for S100A1 at these sites.
Keyword Physiology
Human heart muscle
Calcium binding Proteins
Sarcoplasmic reticulum Vesicles
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
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Citation counts: TR Web of Science Citation Count  Cited 16 times in Thomson Reuters Web of Science Article | Citations
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Created: Fri, 25 Jan 2008, 15:32:14 EST