scholarly journals Down-Regulation of Myosin Light Chain Kinase Expression in Vascular Smooth Muscle Cells Accelerates Cell Proliferation: Requirement of Its Actin-binding Domain for Reversion to Normal Rates

2012 ◽  
Vol 119 (1) ◽  
pp. 91-96 ◽  
Author(s):  
Hong Hui Wang ◽  
Akio Nakamura ◽  
Shinji Yoshiyama ◽  
Ryoki Ishikawa ◽  
Na Cai ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Actin Binding ◽  
Actin Binding Domain ◽  
Kinase Expression

scholarly journals The Structure and Function of the Actin-binding Domain of Myosin Light Chain Kinase of Smooth Muscle

1997 ◽  
Vol 272 (51) ◽  
pp. 32182-32189 ◽  
Author(s):  
Li-Hong Ye ◽  
Kohichi Hayakawa ◽  
Hiroko Kishi ◽  
Michihiro Imamura ◽  
Akio Nakamura ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Structure And Function ◽  
Binding Domain ◽  
Actin Binding ◽  
Actin Binding Domain ◽  
And Function

scholarly journals 2-Methoxyestradiol blocks the RhoA/ROCK1 pathway in human aortic smooth muscle cells

2015 ◽  
Vol 309 (12) ◽  
pp. E995-E1007 ◽  
Author(s):  
Lisa Rigassi ◽  
Federica Barchiesi Bozzolo ◽  
Eliana Lucchinetti ◽  
Michael Zaugg ◽  
Jürgen Fingerle ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Molecular Mechanisms ◽  
Muscle Cells ◽  
Myosin Phosphatase ◽  
Downstream Signaling

2-Methoxyestradiol (2-ME), a metabolite of estradiol with little affinity for estrogen receptors, inhibits proliferation of vascular smooth muscle cells; however, the molecular mechanisms underlying this effect are incompletely understood. Our previous work shows that 2-ME inhibits initiation (blocks phosphorylation of ERK and Akt) and progression (reduces cyclin expression and increases expression of cyclin inhibitors) of the mitogenic pathway and interferes with mitosis (disrupts tubulin organization). Because the RhoA/ROCK1 pathway (RhoA → ROCK1 → myosin phosphatase targeting subunit → myosin light chain) is involved in cytokinesis, herein we tested the concept that 2-ME also blocks the RhoA/ROCK1 pathway. Because of the potential importance of 2-ME for preventing/treating vascular diseases, experiments were conducted in female human aortic vascular smooth muscle cells. Microarray transcriptional profiling suggested an effect of 2-ME on the RhoA/ROCK1 pathway. Indeed, 2-ME blocked mitogen-induced GTP-bound RhoABC expression and membrane-bound RhoA, suggesting interference with the activation of RhoA. 2-ME also reduced ROCK1 expression, suggesting reduced production of the primary downstream signaling kinase of the RhoA pathway. Moreover, 2-ME inhibited RhoA/ROCK1 pathway downstream signaling, including phosphorylated myosin phosphatase targeting subunit and myosin light chain; the ROCK1 inhibitor H-1152 mimicked these effects of 2-ME; both 2-ME and H-1152 blocked cytokinesis. 2-ME also reduced the expression of tissue factor, yet another downstream signaling component of the RhoA/ROCK1 pathway. We conclude that 2-ME inhibits the pathway RhoA → ROCK1 → myosin phosphatase targeting subunit → myosin light chain, and this likely contributes to the reduced cytokinesis in 2-ME treated HASMCs.

scholarly journals Apelin Stimulates Myosin Light Chain Phosphorylation in Vascular Smooth Muscle Cells

2006 ◽  
Vol 26 (6) ◽  
pp. 1267-1272 ◽  
Author(s):  
Tatsuo Hashimoto ◽  
Minoru Kihara ◽  
Junji Ishida ◽  
Nozomi Imai ◽  
Shin-ichiro Yoshida ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Muscle Cells ◽  
Myosin Light Chain Phosphorylation
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