Force and myosin light chain phosphorylation in dog airway smooth muscle activated in different ways
| Autor: | Joseph Ragozzino, Richard W. Mitchell, Lincoln E. Ford, Theodor Burdyga |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
inorganic chemicals
Pulmonary and Respiratory Medicine medicine.medical_specialty Myosin light-chain kinase Myosin Light Chains Physiology Pyridines macromolecular substances Biology In Vitro Techniques environment and public health Potassium Chloride Wortmannin chemistry.chemical_compound Dogs Internal medicine Isometric Contraction Myosin medicine Animals Enzyme Inhibitors Phosphorylation Oxazoles Tetany Dose-Response Relationship Drug Kinase General Neuroscience Muscle Smooth Amides Acetylcholine Electric Stimulation Y-27632 Androstadienes Trachea enzymes and coenzymes (carbohydrates) Endocrinology chemistry Trachealis muscle Biophysics bacteria Marine Toxins Calyculin |
| Zdroj: | Respiratory physiologyneurobiology. 137(2-3) |
| ISSN: | 1569-9048 |
| Popis: | To assess activation mechanisms of dog trachealis muscle and test whether isometric force generation could be separated from myosin light-chain (MLC) phosphorylation, force and phosphorylation were measured in the presence of wortmannin (a light-chain kinase inhibitor) or Y-27632 (a rho-kinase inhibitor) during electrically stimulated tetani and sustained contractures induced by acetylcholine, KCl, or calyculin A, a light-chain phosphatase inhibitor which caused irreversible contractures and both di- and mono-phosphorylation of light chain. Phosphorylation was not much more than half under any circumstances. A nearly constant proportionality between steady force and phosphorylation existed over a 9-fold force range during contractures and 25-sec tetani, except that force correlated best with the di-phosphorylated light chain produced by calyculin A. Phosphorylation was disproportionately higher than force at the outset of tetani, and this disproportion was exaggerated by Y-27632. The results suggest that about half the light chain is sequestered from kinases and that mechanical activation is tightly linked to phosphorylation, except at the outset of stimulation. |
| Databáze: | OpenAIRE |
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