Smooth muscle myosin phosphatase inhibition and force enhancement by black sponge toxin
- 8 June 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 217 (1) , 81-84
- https://doi.org/10.1016/0014-5793(87)81247-4
Abstract
Smooth muscle contraction depends on the state of myosin phosphorylation and hence on the balance of myosin light chain kinase and phosphatase activity. Effects of okadaic acid isolated from black sponge on both enzyme activities and contractility were studied in chemically skinned fibers from guinea pig taenia coli. The toxin strongly inhibits myosin phosphatase and enhances tension development.Keywords
This publication has 11 references indexed in Scilit:
- Electromechanical effects of okadaic acid isolated from black sponge in guinea-pig ventricular muscles.The Journal of Physiology, 1986
- A New Heat-Stable Regulatory Factor is Associated with Aortic Polycation-Modulated (PCM)-PhosphataseExperimental Biology and Medicine, 1985
- cGMP and cAMP inhibit tension development in skinned coronary arteriesPflügers Archiv - European Journal of Physiology, 1984
- Skinned coronary smooth muscle: Calmodulin, calcium antagonists, and cAMP influence contractilityBasic Research in Cardiology, 1983
- An aortic spontaneously active phosphatase dephosphorylates myosin and inhibits actin-myosin interactionBiochemical and Biophysical Research Communications, 1983
- [30] Smooth muscle myosin light chain kinasePublished by Elsevier ,1983
- Okadaic acid, a cytotoxic polyether from two marine sponges of the genus HalichondriaJournal of the American Chemical Society, 1981
- Activation of skeletal muscle myosin light chain kinase by calcium(2+) and calmodulinBiochemistry, 1980
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951