The Release of Cyclophilin A from Rapamycin-Stimulated Vascular Smooth Muscle Cells Mediated by Myosin II Activation: Involvement of Apoptosis but Not Autophagy

2020 ◽  
Vol 57 (5) ◽  
pp. 254-260 ◽  
Author(s):  
Zizhuo Su ◽  
Maohuan Lin ◽  
Haijun Zhang ◽  
Jiajie Li ◽  
Meiping Wu ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Myosin Ii ◽  
Cyclophilin A ◽  
Muscle Cells

scholarly journals Cyclophilin A Is Required for Angiotensin II–Induced p47phox Translocation to Caveolae in Vascular Smooth Muscle Cells

2013 ◽  
Vol 33 (9) ◽  
pp. 2147-2153 ◽  
Author(s):  
Nwe Nwe Soe ◽  
Mark Sowden ◽  
Padmamalini Baskaran ◽  
Elaine M. Smolock ◽  
Yeonghwan Kim ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Angiotensin Ii ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Cyclophilin A ◽  
Muscle Cells

scholarly journals Cyclophilin A Is Secreted by a Vesicular Pathway in Vascular Smooth Muscle Cells

2006 ◽  
Vol 98 (6) ◽  
pp. 811-817 ◽  
Author(s):  
Jun Suzuki ◽  
Zheng-Gen Jin ◽  
David F. Meoli ◽  
Tetsuya Matoba ◽  
Bradford C. Berk
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Cyclophilin A ◽  
Muscle Cells

Blebbistatin inhibits the chemotaxis of vascular smooth muscle cells by disrupting the myosin II-actin interaction

2008 ◽  
Vol 294 (5) ◽  
pp. H2060-H2068 ◽  
Author(s):  
Hong Hui Wang ◽  
Hideyuki Tanaka ◽  
Xiaoran Qin ◽  
Tiejun Zhao ◽  
Li-Hong Ye ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Myosin Ii ◽  
Muscle Cells ◽  
Smooth Muscle Myosin ◽  
A7r5 Cells ◽  
Microscopic Evaluation ◽  
Muscle Myosin

Blebbistatin is a myosin II-specific inhibitor. However, the mechanism and tissue specificity of the drug are not well understood. Blebbistatin blocked the chemotaxis of vascular smooth muscle cells (VSMCs) toward sphingosylphosphorylcholine (IC50 = 26.1 ± 0.2 and 27.5 ± 0.5 μM for GbaSM-4 and A7r5 cells, respectively) and platelet-derived growth factor BB (IC50 = 32.3 ± 0.9 and 31.6 ± 1.3 μM for GbaSM-4 and A7r5 cells, respectively) at similar concentrations. Immunofluorescence and fluorescent resonance energy transfer analysis indicated a blebbistatin-induced disruption of the actin-myosin interaction in VSMCs. Subsequent experiments indicated that blebbistatin inhibited the Mg2+-ATPase activity of the unphosphorylated (IC50 = 12.6 ± 1.6 and 4.3 ± 0.5 μM for gizzard and bovine stomach, respectively) and phosphorylated (IC50 = 15.0 ± 0.6 μM for gizzard) forms of purified smooth muscle myosin II, suggesting a direct effect on myosin II motor activity. It was further observed that the Mg2+-ATPase activities of gizzard myosin II fragments, heavy meromyosin (IC50 = 14.4 ± 1.6 μM) and subfragment 1 (IC50 = 5.5 ± 0.4 μM), were also inhibited by blebbistatin. Assay by in vitro motility indicated that the inhibitory effect of blebbistatin was reversible. Electron-microscopic evaluation showed that blebbistatin induced a distinct conformational change (i.e., swelling) of the myosin II head. The results suggest that the site of blebbistatin action is within the S1 portion of smooth muscle myosin II.

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