Skip to main content

Some NLM-NCBI services and products are experiencing heavy traffic, which may affect performance and availability. We apologize for the inconvenience and appreciate your patience. For assistance, please contact our Help Desk at info@ncbi.nlm.nih.gov.

. 2010 Jun 25;285(35):27213–27223. doi: 10.1074/jbc.M109.087791

FIGURE 6.

FIGURE 6.

Integrin-ILK-Akt signaling was also enhanced in GD3+ cells. A, phosphorylation of Akt during adhesion to CL type I in GD3+ cells (G5) and GD3− cells (V4) was examined. Cells were prepared as described in the legend to Fig. 3, and immunoblotting was performed using anti-phospho-Akt (Ser-473), anti-phospho-Akt (Thr-308), and anti-total Akt antibodies. B, band intensities were plotted after correction with those of total Akt. C, knockdown of ILK. To knockdown ILK, 4 kinds of anti-ILK siRNAs were analyzed. siRNA:si-ILK3 suppressed ILK levels most efficiently (70–80%), and was used hereafter. GL-2 (anti-firefly luciferase siRNA) was used as a control. D, ILK is involved in Akt phosphorylation. Effects of ILK knockdown on phosphorylation levels of Akt in GD3+ (a) and GD3− cells (b) during adhesion to CL type I were examined. After 48 h of transfection, cells were plated on pre-coated CL type I, and lysed for immunoblotting at incubation time 0 and 20 min. Definite reduction in Akt phosphorylation was detected in GD3+ cells. Bars indicate mean ± S.D. (n = 3). *, p < 0.05; **, p < 0.01. These were representative results among experiments repeated at least 3 times with similar results (C and D).

HHS Vulnerability Disclosure