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J. Biol. Chem., Vol. 261, Issue 14, 6293-6299, 05, 1986
A Persechini, KE Kamm and JT Stull
Calmodulin-dependent myosin light chain kinase phosphorylates two light
chain subunits on each myosin molecule. We have developed a method for
measuring nonphosphorylated, monophosphorylated, and diphosphorylated forms
of myosin in smooth muscle. Four protein bands were separated in tissue
extracts by nondenaturing polyacrylamide gel electrophoresis in the
presence of pyrophosphate. Immunoblots demonstrated that three forms
(designated M, MP, and MP2) reacted with rabbit antisera prepared against
the purified phosphorylatable light chain (P-light chain) from bovine
tracheal smooth muscle. Evidence was obtained that M, MP, and MP2
represented nonphosphorylated, monophosphorylated, and diphosphorylated
myosin, respectively, and that the other protein band was probably filamin.
The formation of different phosphorylated forms of myosin was measured in
bovine trachealis strips neurally stimulated from 1.0 to 3.5 s and
quick-frozen. There was no detectable MP or MP2 in unstimulated muscles;
the extent of P-light chain phosphorylation measured directly was 0.02 +/-
0.01 mol of phosphate/mol of P-light chain. After 2.5-s stimulation,
maximal values of 0.63 +/- 0.06 mol of phosphate/mol of P-light chain and
0.40 +/- 0.06 MP2/myosintotal were obtained. During continuous neural
stimulation from 1.0 to 3.5 s, the relationship between the extent of
P-light chain phosphorylation (measured directly or calculated) and the
relative amount of MP2 is consistent with a random phosphorylation process.
Different phosphorylated forms of myosin in contracting tracheal smooth muscle
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