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. Author manuscript; available in PMC: 2010 Jul 2.
Published in final edited form as: Gastroenterology. 2009 Feb 6;136(5):1772–1782. doi: 10.1053/j.gastro.2009.01.070

Figure 6.

Figure 6

Effect of chelating intracellular calcium and cathepsin B inhibition on caspase 3 activation induced by inhibition of HSP70 expression. Inhibition of HSP70 expression by (A) quercetin, (B) triptolide, and (C and D) HSP70 siRNA induces caspase 3 activation in both MiaPaCa-2 and Panc-1 pancreatic cancer cell lines. Chelation of cytosolic calcium by BAPTA protects against caspase 3 activation induced by the down-regulation of HSP70 by (A) quercetin, (B) triptolide, and (C and D) HSP70 siRNA. Similarly, the inhibition of cathepsin B by CA074me reduces caspase 3 activation induced by (A) quercetin, (B) triptolide, and (C and D) HSP70 siRNA. Pretreatment with both BAPTA and CA074me provided significantly more protection against caspase activation than that conferred by BAPTA and CA074me alone. Caspase 3 activity (mean ± SEM) is expressed as a percentage of control. *p ≤ .05 (t test) as compared with inhibited HSP70 expression alone. #p ≤ .05 (t test) as compared with pretreatment with BAPTA or CA074me alone.