A novel protein phosphatase inhibitor, tautomycin Effect on smooth muscle
Open Access
- 8 July 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 285 (1) , 145-148
- https://doi.org/10.1016/0014-5793(91)80745-o
Abstract
The antibiotic, tautomycin, was found to be a potent inhibitor of protein phosphatases and equally effective for the type‐1 and type‐2A enzymes. For the catalytic subunits of the type‐1 and type‐2A phosphatases the IC50 value was 22 to 32 nM. For the phosphatase activity present in chicken gizzard actomyosin the IC50 value was 6 nM. Tautomycin had no effect on myosin light chain kinase activity. Tautomycin induced a Ca2+‐independent contraction of intact and permeabilized smooth muscle fibers and this was accompanied by an increase in the level of myosin phosphorylation. Thus, tautomycin by virtue of its ability to inhibit phosphatase activity is a valuable addition for studying the role of protein phosphorylation.Keywords
This publication has 12 references indexed in Scilit:
- Okadaic acid uncouples myosin light chain phosphorylation and tension in smooth muscleFEBS Letters, 1990
- Phosphorylation of smooth muscle myosin by type II Ca2+/calmodulin-dependent protein kinaseMolecular and Cellular Biochemistry, 1990
- The structure of tautomycin, a dialkylmaleic anhydride antibiotic.The Journal of Antibiotics, 1990
- The structure of tautomycin, a regulator of eukaryotic cell growthJournal of the Chemical Society, Chemical Communications, 1990
- Inhibitory effect of a toxin okadaic acid, isolated from the black sponge on smooth muscle and plateletsBritish Journal of Pharmacology, 1989
- Calyculin A and okadaic acid: Inhibitors of protein phosphatase activityBiochemical and Biophysical Research Communications, 1989
- A new antibiotic, tautomycin.The Journal of Antibiotics, 1987
- The Function of Myosin and Myosin Light Chain Kinase Phosphorylation in Smooth MuscleAnnual Review of Pharmacology and Toxicology, 1985
- Myosin light‐chain kinase, a new enzyme from striated muscleFEBS Letters, 1974