ACTA, a fluorescent analogue of thapsigargin, is a potent inhibitor and a conformational probe of skeletal muscle Ca2+-ATPase
| Autor: | Casper Caspersen, Hasse Kromann, Søren Brøgger Christensen, Kristina Procida, Marek Treiman |
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| Rok vydání: | 1998 |
| Předmět: |
Thapsigargin
SERCA Protein Conformation ATPase Biophysics Calcium-Transporting ATPases Biochemistry Fluorescence chemistry.chemical_compound Structural Biology Genetics medicine Sarco-endoplasmic reticulum Ca2+-ATPase pump Enzyme Inhibitors Muscle Skeletal Molecular Biology Fluorescent Dyes biology Endoplasmic reticulum Vesicle technology industry and agriculture Skeletal muscle Cell Biology medicine.anatomical_structure chemistry cardiovascular system biology.protein Calcium Ca2+ -ATPase Intracellular |
| Zdroj: | FEBS Letters. 439:127-132 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(98)01352-0 |
| Popis: | Thapsigargin is a highly potent and selective inhibitor of sarco-endoplasmic reticulum (SERCA) family of Ca2+-ATPases and a useful tool in research concerning the function of intracellular Ca2+ stores. We describe here a novel fluorescent derivative (8-O-(4-aminocinnamoyl)-8-O-debutanoylthapsigargin, termed ACTA) of this compound, acting as a Ca2+-ATPase inhibitor with a potency approaching that of thapsigargin. Binding of ACTA to the skeletal muscle sarcoplasmic reticulum vesicles results in a strong fluorescence enhancement, approximately 66% of which depends on ACTA association with Ca2+-ATPase. This specific component of ACTA fluorescence is sensitive to the E1-E2 conformational equilibrium of the pump. The combined properties of high potency and binding-dependent fluorescence suggest ACTA to be a useful probe for a range of studies involving the SERCA class of ATPases. |
| Databáze: | OpenAIRE |
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