Myosin light chain and caldesmon phosphorylation in arterial muscle stimulated with endothelin-1
| Autor: | Lorraine Milio, Blair Brengle, Leonard P. Adam, David R. Hathaway |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Myosin light-chain kinase
Calmodulin Swine macromolecular substances In Vitro Techniques Myosins Immunoglobulin light chain Muscle Smooth Vascular Potassium Chloride Myosin Animals Phosphorylation Protein kinase A Molecular Biology Actin biology Angiotensin II Endothelins Caldesmon Biochemistry Vasoconstriction biology.protein Biophysics Calmodulin-Binding Proteins Cardiology and Cardiovascular Medicine |
| Zdroj: | Journal of Molecular and Cellular Cardiology. 22:1017-1023 |
| ISSN: | 0022-2828 |
| Popis: | Endothelin-1 contracts porcine carotid arterial smooth muscle with an ED 50 of 10 n m . Contraction is associated with phosphorylation of the 20 000 dalton-regulatory light chain subunits of vascular myosin. Phosphopeptide mapping of light chains isolated from 32 PO 4 -loaded muscle strips stimulated by endothelin-1 (5 × 10 −8 m ) and comparison with maps generated from light chains phosphorylated in vitro or muscles stimulated with KCl (110 m m ) or angiotensin-II (5 × 10 −8 m ) indicates that Ca 2+ -calmodulin activation of myosin light chain kinase is a biochemical pathway stimulated by all three agonists. However, a small amount of phosphate (17%) was detected in a light chain peptide phosphorylated by protein kinase C. Endothelin-1 also stimulated phosphorylation of the thin filament protein, caldesmon, (from 0.35 mol PO 4 /mol caldesmon to 0.52 mol PO 4 /mol). Collectively, these results provide evidence that the effects of endothelin-1 on force generation and maintenance in vascular muscle may be dependent upon myosin light chain phosphorylation by Ca 2+ calmodulin—requiring myosin light chain kinase and upon a thin filament mechanism that is modulated by phosphorylation of caldesmon. |
| Databáze: | OpenAIRE |
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