4-Hydroxy-2-Nonenal-Modified Glyceraldehyde-3-Phosphate Dehydrogenase Is Degraded by Cathepsin G in Rat Neutrophils
Figure 5
Effects of various cathepsin G inhibitors on the HNE-modified GAPDH-degrading activity of the active fraction. The active fraction separated from the cell extract from neutrophils was incubated with eGAPDH and 100 μM HNE in the presence of DFP or various cathepsin G inhibitors (Z-GLF-CMK: 100 μM; cathepsin G inhibitor I: 10 μM; N-acetyl-eglin C: 1 μM; α 1-antichymotrypsin: 1 μM; DFP: 1 mM) at 37°C for 3 h. The reaction products were separated by SDS-PAGE using 12% polyacrylamide gels and analyzed by Western blotting using an anti-GAPDH mAb. Data are mean ± SE (bars) values from four independent experiments. Significant decreases in GAPDH level compared to control are indicated by asterisks: ***.
