Abstract
BackgroundActin is an essential cellular protein that assembles into microfilaments and regulates numerous processes such as cell migration, maintenance of cell shape, and material transport.MethodsIn this study, we explored the effect of actin polymerization state on the osteogenic differentiation of human adipose-derived stem cells (hASCs). The hASCs were treated for 7 days with different concentrations (0, 1, 5, 10, 20, and 50 nM) of jasplakinolide (JAS), a reagent that directly polymerizes F-actin. The effects of the actin polymerization state on cell proliferation, apoptosis, migration, and the maturity of focal adhesion-related proteins were assessed. In addition, western blotting and alizarin red staining assays were performed to assess osteogenic differentiation.ResultsCell proliferation and migration in the JAS (0, 1, 5, 10, and 20 nM) groups were higher than in the control group and the JAS (50 nM) group. The FAK, vinculin, paxillin, and talin protein expression levels were highest in the JAS (20 nM) group, while zyxin expression was highest in the JAS (50 nM) group. Western blotting showed that osteogenic differentiation in the JAS (0, 1, 5, 10, 20, and 50 nM) group was enhanced compared with that in the control group, and was strongest in the JAS (50 nM) group.ConclusionsIn summary, our data suggest that the actin polymerization state may promote the osteogenic differentiation of hASCs by regulating the protein expression of focal adhesion-associated proteins in a concentration-dependent manner. Our findings provide valuable information for exploring the mechanism of osteogenic differentiation in hASCs.
Highlights
Actin is an essential cellular protein that assembles into microfilaments and regulates numerous processes such as cell migration, maintenance of cell shape, and material transport
Effect of different actin polymerization states on proliferation of human adipose-derived stem cells (hASCs) We evaluated the effects of different polymerization states of actin on the proliferation of hASCs
The results revealed that the cell proliferation rate in the JAS (1, 5, 10, 20, and 50 nM) groups was higher than that in the control; it gradually increased with the increasing JAS concentrations, but significantly decreased in the JAS (50 nM) group (Fig. 1a)
Summary
Actin is an essential cellular protein that assembles into microfilaments and regulates numerous processes such as cell migration, maintenance of cell shape, and material transport. Several substances involved in the regulation of actin polymerization and depolymerization have been investigated. These include phalloidin [15], cytochalasin D [16], and latrunculin A [17, 18], which can alter intracellular actin organization [19]. A major advantage of JAS is that it is membrane permeable [28], which makes it an ideal tool for stabilizing or polymerizing actin filaments in live cells. It induces the nucleation of actin filaments, reduces the rate of dissociation of actin subunits from F-actin filaments, and prevents cofilin from severing F-actin filaments, resulting in filament stabilization [27, 29, 30]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
