acid-phosphatase and butibufen

Here we report the results of a study on the influence of butibufen (50 and 250 mg/kg) on enzyme activity and lysosomal membrane stabilization. The influence of hydrocortisone acetate (25 and 75 mg/kg) and acetylsalicylic acid (ASA) (50 mg/kg) was comparatively studied. We determined beta-glucuronidase and acid phosphatase free and total activity and the ratio between both types of activity (a ratio which indicates lysosomal membrane stability). This determination was carried out using hepatic homogenates from Sprague-Dawley rats. The drugs were administered orally 18 and 3 h before sacrifice. The results show that none of the drugs used in this study modify free or total beta-glucuronidase activity. The ratio between free and total activity of this enzyme was not modified by the drugs when compared to controls. On the contrary, the figures for acid phosphatase were modified by all the drugs employed, showing statistical significance (p < 0.001 for 250 mg/kg butibufen and 75 mg/kg hydrocortisone and p < 0.001 for 50 mg/kg ASA). The ratio of free/total activity was modified only by hydrocortisone (75 mg/kg) (p < 0.001). Thus our results indicated that the antiinflammatory drugs employed in this study can reduce acid phosphatase activity and only hydrocortisone seems to be able to stabilize the lysosomal membrane. Acid phosphatase enzyme inhibition might partially contribute to the antiinflammatory action of these drugs.

Topics: Acid Phosphatase; Analysis of Variance; Animals; Anti-Inflammatory Agents; Anti-Inflammatory Agents, Non-Steroidal; Aspirin; Glucuronidase; Hydrocortisone; Liver; Lysosomes; Male; Phenylbutyrates; Rats; Rats, Sprague-Dawley