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. Author manuscript; available in PMC: 2017 Mar 15.
Published in final edited form as: Cancer Res. 2015 Dec 30;76(6):1560–1568. doi: 10.1158/0008-5472.CAN-15-2401

Figure 2.

Figure 2

DDR1 knockdown enhances inhibition of protein synthesis by RG7787 and reduces levels of ribosomal proteins. Forty-eight hours after transfection, A) KB or B) A431/H9 cells were treated with RG7787 for 18 hours and assayed for incorporation of 3H-Leucine to measure the level of protein synthesis. C, D) After DDR1 knockdown, cell lysates were analyzed for the expression of ribosomal proteins by western blot analysis using anti-RPL38, anti-RPL24, anti-RPL10A, and anti-RPL22 antibodies. The relative band intensities were quantified (Multigauge software), normalized to actin levels and represented as percentage of control. E, F) KB or A431/H9 cells were transfected with control siRNA or RPL38 siRNAs or G, H) RPL10A siRNAs for 48 hours then treated with 11ng/ml RG7787 for 18 hours before assaying for protein synthesis by measuring incorporation of 3H-Leucine. I) Knockdown of RPL38 or RPL10A by siRNAs was verified by WB in KB and A431/H9 cells.