Premium
Smooth muscle myosin phosphatase inhibition and force enhancement by black sponge toxin
Author(s) -
Takai Akira,
Bialojan Corinna,
Troschka Monika,
Caspar Rüegg J.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81247-4
Subject(s) - taenia coli , okadaic acid , myosin light chain kinase , myosin , phosphatase , chemistry , contractility , biophysics , biochemistry , muscle contraction , contraction (grammar) , phosphorylation , toxin , microbiology and biotechnology , biology , anatomy , endocrinology
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.