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

Title:

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

Creator:

Bohumil Maco, Mandinova, A., Dürrenberger, M. B., Schäfer, B. W., Uhrík, B., and Heizmann, C. W.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:1a466339-5461-45f6-84b7-23bebdf4f9df
uuid:1a466339-5461-45f6-84b7-23bebdf4f9df
issn:0862-8408

Subject:

Fyziologie člověka a srovnávací fyziologie, imunocytochemie, immunocytochemistry, human heart muscle, Ca2+-binding proteins, S100A1, 14, and 612

Type:

article, články, model:article, and TEXT

Format:

print, bez média, and svazek

Description:

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., B. Maco, A. Mandinová, M.B. Dürrenberger, B.W. Schäfer, B. Uhrík, C.W. Heizmann., and Obsahuje bibliografii

Language:

English

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Source:

Physiological research | 2001 Volume:50 | Number:6

Harvested from:

CDK

Metadata only:

false