Regulation of subcellular localization of muscle FBPase in cardiomyocytes. The decisive role of calcium ions
Autor: | Paweł Pomorski, Andrzej Dzugaj, Michał Majkowski, Dorota Wypych |
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Rok vydání: | 2010 |
Předmět: |
chemistry.chemical_element
Calcium Gene Expression Regulation Enzymologic General Biochemistry Genetics and Molecular Biology Dantrolene Calcium in biology chemistry.chemical_compound medicine Animals Myocytes Cardiac Calcimycin Cells Cultured Microscopy Confocal Ionophores Glycogen Subcellular localization Protein subcellular localization prediction Fructose-Bisphosphatase Rats Cell biology Protein Transport medicine.anatomical_structure chemistry Gluconeogenesis Biochemistry Intercalated disc Signal Transduction medicine.drug |
Zdroj: | Scopus-Elsevier |
ISSN: | 1734-154X 0001-527X |
DOI: | 10.18388/abp.2010_2450 |
Popis: | Glyconeogenesis, the synthesis of glycogen from carbohydrate precursors like lactate, seems to be an important pathway participating in replenishing glycogen in cardiomyocytes. Fructose-1,6-bisphosphatase (FBPase), an indispensible enzyme of glyconeogenesis, has been found in cardiomyocytes on the Z-line, in the nuclei and in the intercalated discs. Glyconeogenesis may proceed only when FBPase accumulates on the Z-line. Searching for the mechanism of a FBPase regulation we investigated the effects of the calcium ionophore A23187, a muscle relaxant dantrolene, glucagon, insulin and medium without glucose on the subcellular localization of this enzyme in primary culture of neonatal rat cardiomyocytes. Immunofluorescence was used for protein localization and the intracellular calcium concentration was measured with Fura. We found that the concentration of calcium ions was the decisive factor determining the localization of muscle FBPase on the Z-line. Calcium ions had no effect on the localization of the enzyme in the intercalated discs or in the nuclei, but accumulation of FBPase in the nuclei was induced by insulin. |
Databáze: | OpenAIRE |
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