RESULTS(1)

Effects of EDL on GGT Catalytic Activity in Various Regions of the Rat Epididymis

GGT catalytic activity was measured in epididymal tissue homogenate from rats that had previously undergone unilateral EDL and a sham operation. For sham-operated rats, the levels of GGT catalytic activity were initial segment > caput > corpus = cauda > testes (Fig. 1). GGT catalytic activity in the initial segment decreased by 3 days and 5 days of EDL, but did not differ significantly from that in controls after 1 day and 14 days of EDL. In the caput and corpus regions, GGT catalytic activity did not decrease following 1 day, 3 days, and 5 days of EDL, but decreased by 14 days of EDL. GGT catalytic activity in cauda and testis remained unchanged after EDL for the experimental time periods. buy asthma inhalers
Fig1Regulation of gamma-glutamyl
FIG. 1. GGT catalytic activity in the rat epididymis and testes. GGT catalytic activity (nmol/min per milligram protein) in homogenate of testis (T), initial segment (IS), caput (Ca), corpus (Co), and cauda (Cau) in sham control and unilateral-EDL rats. Each bar in the sham group represents the mean ± SEM of 20 rats, while each bar in the EDL 1 day (D), EDL 3 D, EDL 5 D, and EDL 14 D groups represents the mean ± SEM of 5 rats. Because of printer limitations, some SEM were too small to be printed. GGT catalytic activity of testes and epididymal regions within sham or EDL groups with different letters is significantly different (p < 0.05). GGT catalytic activity of testes or epididymal regions among sham and EDL groups with different numbers is significantly different (p < 0.05).

Decrease of GGT Protein in the Initial Segments after 3-Day EDL

Western blot analysis showed that two subunits of GGT protein (58 kDa and 28 kDa) were detected by the GGT antibody and that the protein levels of both the 58-kDa and 28-kDa proteins decreased after 3-day EDL as compared to levels in the sham control (Fig. 2).
Fig2Regulation of gamma-glutamyl
FIG. 2. GGT protein level in the initial segment decreases after unilateral EDL 3 D as analyzed by Western blotting. Fifty micrograms of homogenate from the initial segments of sham-operated and EDL-operated rats was separated by 12% SDS-PAGE and transferred to a nitrocellulose membrane. The membrane was 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.

GGT Catalytic Activity in the Initial Segments after 3-Day EDL Recovered by RTF

As shown in Figure ЗА, GGT catalytic activity in the initial segment decreased after 3-day EDL and was recovered by treatment with 10% oRTF. Similar results were obtained by treatments with no-ABP oRTF and charcoal oRTF (Fig. ЗА). However, boiled charcoal oRTF did not recover the decreased GGT catalytic activity caused by 3-day EDL (Fig. ЗА). As determined by RIA, the concentrations of testosterone in oRTF, no-ABP oRTF, charcoal oRTF, and boiled charcoal oRTF were 9.035 ± 0.315, < 0.2, 0.715 ± 0.005, and 0.405 ± 0.015 (mean ± SEM) ng/ml, respectively.
Fig3Regulation of gamma-glutamyl
FIG. 3. Effects of various RTF preparations on GGT catalytic activity in the initial segment after EDL 3 D. A) Initial segments from sham 3 Doperated or EDL 3 D-operated rats were incubated with various 10% oRTF preparations or sRTF at 35°C for 6 h . GGT catalytic activity was determined in the homogenates of the treated tissues and expressed as a percentage of GGT catalytic activity in the sRTF-treated (sham) initial seg-