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J. Biol. Chem., Vol. 268, Issue 32, 23850-23855, 11, 1993
MS Kolodney and EL Elson
In vitro studies have indicated that the enzymatic activity of myosin II
from non-muscle cells is controlled by phosphorylation of its regulatory
light chain (LC20). We have studied one likely functional consequence of
phosphorylating LC20 in living chick embryo fibroblasts (CEF) by measuring
contractile force developed by these cells. Using a recently developed
method, we recorded quantitative changes in isometric force generated by a
population of cells following mitogenic stimulation. Fetal bovine serum,
thrombin, and lysophosphatidic acid stimulate rapid isometric contraction
of CEF. Cells stimulated with thrombin develop maximal force within 5-10
min. Force development correlates temporally with a 3-5-fold increase in
the overall fraction of LC20 phosphorylated and with the fractions of LC20
in both the monophosphorylated and diphosphorylated states. Unloaded
shortening velocity also increases after thrombin stimulation. Although
both force and phosphorylation begin to decline 10 min after stimulation,
the level of phosphorylation declined more rapidly than the force. These
results suggest that the role of LC20 phosphorylation in regulating
fibroblast contractility is analogous to its well established role in
regulating smooth muscle contraction and that quantitative measurements of
the force developed by populations of fibroblasts (or other cultured cells)
can be used to study the regulation of non-sarcomeric myosin at the
molecular level in vivo.
Correlation of myosin light chain phosphorylation with isometric contraction of fibroblasts
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110.
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