Figure 2
Figure 2. KLF2 induces early cytoskeleton changes, inhibits FAK S732 phosphorylation, and activates RhoA. (A) HUVECs were cultured on glass coated with fibronectin and fixed after 24, 48, or 72 hours of lentiviral overexpression. Nuclei were stained with Hoechst 33342 (blue) and actin filaments with Phalloidin-TRITC (red), and fluorescent microscopy was performed. (B) Western blot analysis of levels of FAK phosphorylated on serine residue 732 in mock- (□) and KLF2-transduced HUVECs (■) at 24, 48, and 72 hours after transduction. α-Tubulin was used as a loading control. (Bottom) Densitometric quantification of the Western blot (n = 4). (C) Active RhoA was isolated with glutathione S-transferase–tagged Rhotekin, and a representative subsequent Western blot for RhoA is shown. Three independent experiments were quantified and corrected for α-tubulin. *P < .05, **P < .01.

KLF2 induces early cytoskeleton changes, inhibits FAK S732 phosphorylation, and activates RhoA. (A) HUVECs were cultured on glass coated with fibronectin and fixed after 24, 48, or 72 hours of lentiviral overexpression. Nuclei were stained with Hoechst 33342 (blue) and actin filaments with Phalloidin-TRITC (red), and fluorescent microscopy was performed. (B) Western blot analysis of levels of FAK phosphorylated on serine residue 732 in mock- (□) and KLF2-transduced HUVECs (■) at 24, 48, and 72 hours after transduction. α-Tubulin was used as a loading control. (Bottom) Densitometric quantification of the Western blot (n = 4). (C) Active RhoA was isolated with glutathione S-transferase–tagged Rhotekin, and a representative subsequent Western blot for RhoA is shown. Three independent experiments were quantified and corrected for α-tubulin. *P < .05, **P < .01.

Close Modal

or Create an Account

Close Modal
Close Modal