When the initial segment after 3-day EDL was treated with 40% > 10-kDa oRTF, GGT catalytic activity returned to the sham control value (Fig. 3B). However, treatment with < 10-kDa oRTF did not recover the decreased GGT catalytic activity (Fig. 3B). GGT catalytic activity in the initial segment after 3-day EDL returned to sham control values after treatment with 20% rRTF (Fig. 3C).

GGT Protein Level Recovered by RTF

Western blot analyses showed that GGT protein levels decreased after 3-day EDL (Fig. 4), but oRTF treatment (10%) brought the decreased GGT protein level back to sham control levels (Fig. 4A). Similar results were obtained with treatments of 10% no-ABP oRTF or charcoal oRTF (Fig. 4B). When tissues were treated with 40% > 10-kDa oRTF, GGT protein level returned to the sham control level (Fig. 4C). However, < 10-kDa oRTF did not recover the loss of GGT protein caused by 3-day EDL (Fig. 4C). As shown in Figure 4D, rRTF treatment (20%) recovered the decreased GGT protein level in the initial segment caused by 3-day EDL. buy asthma inhaler
Fig4Regulation of gamma-glutamyl
FIG. 4. GGT protein level in the EDL 3 D initial segment recovered by RTF preparations. Initial segments from sham 3 D-operated or EDL 3 Doperated rats were treated with A) 10% sRTF or oRTF, B) 10% sRTF, no-ABP oRTF, or charcoal oRTF, C) 40% sRTF, > Ю-kDa oRTF, or < 10-kDa oRTF, or D) 20% sRTF or rRTF at 35°C for 6 h. The homogenates of the treated initial segments were subjected to Western blot analyses. Fifty micrograms of the homogenate was separated by 12% SDS-PAGE and transferred to nitrocellulose membranes. The membranes were then

GGT Catalytic Activity and GGT Protein Level Recovered by bFGF and TP A after 3-Day EDL

As shown in Figure 5, bFGF but not EGF recovered the decreased GGT catalytic activity caused by 3-day EDL, and the recovery of GGT catalytic activity by bFGF was prevented in the presence of cycloheximide, a protein synthesis inhibitor. Western blot analyses showed that the GGT protein level returned to the sham control level in the 3-day-EDL initial segment following incubation with recombinant bFGF but not with EGF (Fig. 6).
Fig5Regulation of gamma-glutamyl
FIG. 5. The recovery of the decreased GGT catalytic activity in EDL 3 D initial segments by bFGF. Initial segments from EDL 3 D-operated rats were incubated with or without various concentrations of bovine bFGF, 20.1 ng/ml bFGF in combination with 10 jxg/ml cycloheximide (Cyclo.), or 20 ng/ml human EGF at 35°C for 6 h. The sham-treated initial segment was used as a control. GGT catalytic activity was determined in the homogenates of the treated tissues and expressed as a percentage of GGT catalytic activity in the sham-treated initial segment in each experiment. Data shown represent mean percentage ± SEM from four to six individual experiments in each group. Mean percentages for GGT catalytic activity with different letters were significantly different (p < 0.05).

Fig6Regulation of gamma-glutamyl
FIG. 6. The recovery of decreased GGT protein level in EDL 3 D initial segments by bFGF. Initial segments from EDL 3 D-operated rats were incubated with or without different concentrations of bovine bFGF or human EGF at 35°C for 6 h. The sham-treated initial segment was used as a control. The homogenates of the treated initial segments were subjected to Western blot analyses. Fifty micrograms of homogenate was separated by 12% SDS-PAGE and transferred to a nitrocellulose membrane. The membrane was then probed with rabbit anti-GGT antibody (1: 500) for 3 h at room temperature. Molecular masses, kDa, of detected GGT proteins are indicated on the left.