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The role of S‐nitrosylated profilin‐1 and myosin regulatory light chain 9 in human myometrial contractile dynamics
Author(s) -
Barnett Scott Danielson,
Ulrich Craig,
Baker Josh,
Buxton Iain L.O.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.879.1
Subject(s) - myosin , profilin , actin , myosin light chain kinase , heavy meromyosin , microbiology and biotechnology , chemistry , meromyosin , motility , actin remodeling , biophysics , biology , actin cytoskeleton , biochemistry , myosin head , cytoskeleton , cell
We hypothesize that S‐nitrosylation of profilin‐1 and myosin regulatory light chain 9 (MYL9) alters smooth muscle contractile dynamics by modifying actin polymerization and myosin‐based actin sliding velocities/actin‐myosin ATPase activity. Analysis of the human myometrial S‐nitrosylproteome revealed that profilin‐1 and MYL9 are differentially S‐nitrosylated based upon the state of labor. We test the effect of profilin‐1 S‐nitrosylation on actin polymerization using an actin polymerization assay and a G‐actin/F‐actin assay. Using an actin‐motility assay, we test whether the S‐nitrosylation of MYL9 affects myosin‐based actin velocities and actin‐myosin ATPase activity. Previous research employing S‐nitrosylated heavy meromyosin from striated muscle determined that actin velocity is decreased while force is increased. A similar finding in smooth muscle would suggest that the force of contraction during labor may increase if MYL9 is S‐nitrosylated. This research will lead to a better understanding of myometrial contractile dynamics and may provide additional insight into the onset of labor as well as the potential for developing novel therapeutics for preterm labor. Supported by NIH HD053028 to ILOB