S-100ab increases Ca2+ release in purified sarcoplasmic reticulum vesicles of frog skeletal muscle
| Autor: | G. Menchetti, Stefania Fulle, Loretta Mancinelli, Valeria Marsili, Giorgio Fanò, F. Baldoni |
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| Rok vydání: | 1992 |
| Předmět: |
Ruthenium red
Ranidae Physiology S100 Calcium Binding Protein beta Subunit Biology Biochemistry chemistry.chemical_compound medicine Myocyte Animals Nerve Growth Factors Ryanodine receptor Ryanodine Endoplasmic reticulum Binding protein Vesicle Muscles Calcium-Binding Proteins S100 Proteins Skeletal muscle Cell Biology Ruthenium Red Sarcoplasmic Reticulum medicine.anatomical_structure chemistry Biophysics GRENOUILLE Calcium Cattle Calcium Channels Biomarkers Muscle Contraction |
| Zdroj: | Journal of muscle research and cell motility. 13(5) |
| ISSN: | 0142-4319 |
| Popis: | The S-100ab protein, a mixed isoform member of the S-100 family, stimulates Ca(2+)-induced Ca(2+)-release from sarcoplasmic reticulum vesicles purified from frog skeletal muscle cells. The effects of S-100ab appear to be specific and result from its peculiar characteristics rather than the fact that it is a calcium-binding protein. Moreover, the addition of S-100ab to the solution completely abolished the inhibition provoked when Ruthenium Red was added alone. Experiments that added labelled Ryanodine with and without S-100 indicated that the protein diminished the affinity of the alkaloid at its receptor site. |
| Databáze: | OpenAIRE |
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