Similarly, CdCl2 did not cause a change in GST-α levels ( Fig. 4A). CAT activity measurements

HER2 inhibitor showed that treatment with CdTe-QDs caused a significant decrease (1.4-fold, p < 0.001) in this enzyme activity, compared to the control ( Fig. 4B). Treatment of CdCl2 also resulted in a similar reduction in CAT activity ( Fig. 4B). As a preliminary screen for apoptosis, caspase-3 activity, level of cleaved PARP and annexin V binding to externalized phosphatydylserine were examined. CdTe-QDs induced cleavage of pro caspase-3 to its active form. A 1.6-fold (p < 0.001) increase in active form of caspase-3 was observed in CdTe-QD treated cells. CdCl2 and STS treatments also increased caspase-3 activity ( Fig. 5A). Measurement of cleaved PARP levels in test cells showed that CdTe-QDs caused a significant increase (13.2-fold, p < 0.001). While STS treatments also resulted in dramatic increase in PARP cleavage, CdCl2 treatment caused only a moderate elevation (3.8-fold, p < 0.001) ( Fig. 5B). Cells were treated with conjugated annexin V and the binding of the protein to externalized phosphatidylserine in apoptotic cells was detected by fluorescence. The results show that while the control cultures had background levels of annexin V staining (Fig. 6A), CdTe-QD treatment resulted in a significant

increase in annexin V positive cells Palbociclib order (Fig. 6B). Both CdCl2 and STS treatments also generated a high number of apoptotic cells that appeared intensely stained with annexin V (Fig. 6C and D). Since Fas-mediated cell death has been suggested to be related to extrinsic apoptosis, the effect of CdTe-QDs on

Fas level was examined to reveal details about the apoptotic pathways induced by CdTe-QDs. Treatment of CdTe-QDs induced a marginal increase in Fas level (1.15-fold, p < 0.05), compared to the control ( Fig. 7A). While a similar effect was observed with CdCl2 treatment, there was no change in Fas level caused by STS ( Fig. 7A). Caspase-8 is a marker for extrinsic apoptosis and its activity was examined Montelukast Sodium in HepG2 cells during CdTe-QD exposure. CdTe-QD treatment resulted in increased caspase-8 activity (1.5-fold, p < 0.001), compared to the control ( Fig. 7B). While CdCl2 treatment also caused increased caspase-8 activity (1.2-fold, p < 0.001), STS treatment caused no change in the activity of this protein ( Fig. 7B). Since Bcl2 is recognized as a potent inhibitor of apoptotic cell death and involved in intrinsic apoptotic pathway, the effect of CdTe-QDs on this protein level in HepG2 was examined. Exposure resulted in a significant decrease in Bcl2 level (1.8-fold, p < 0.001) ( Fig. 8A). Similar cell treatments with CdCl2 and STS also led to reduced Bcl2 levels albeit ∼10% (p < 0.05) less than that caused by CdTe-QDs ( Fig. 8A). Bax is also an important indicator of intrinsic apoptosis.