Figure 1.
Structures of ibuprofen, flurbiprofen and the metabolites investigated in the present study.
Figure 2.
Inhibition of the activities of ovine COX-1 (towards arachidonic acid) and human recombinant COX-2 (towards either arachidonic acid or 2-AG) by ibuprofen and its 2′- and 3′-hydroxy metabolites.
The substrates used (10 µM) are shown in the figure, as are the concentrations (in µM) of the test compounds. “F30” refers to 30 µM flurbiprofen, used as a positive control. Values are means ± s.e.m. (unless enclosed by the symbols), n = 3, of the change in oxygen utilisation following addition of enzyme to the oxygen electrode chamber.
Figure 3.
Inhibition of the activities of ovine COX-1 (towards arachidonic acid) and human recombinant COX-2 (towards either arachidonic acid or 2-AG) by flurbiprofen and its 4′-hydroxy metabolite.
The substrates used (10 µM) are shown in the figure, as are the concentrations (in µM) of the test compounds. Values are means ± s.e.m. (unless enclosed by the symbols), n = 3, of the change in oxygen utilisation following addition of enzyme to the oxygen electrode chamber.
Table 1.
Comparison of the effects of the NSAIDs and their metabolites upon the initial activity of COX-1.
Table 2.
Comparison of the effects of the NSAIDs and their metabolites upon the initial activity of COX-2.
Figure 4.
Inhibition of FAAH activity in rat brain homogenates by ibuprofen and its 1′-OH, 2′-OH, 3′-OH and carboxy metabolites.
The AEA assay concentration was 0.5 µM. Values are means ± s.e.m. (unless enclosed by the symbols), n = 3.
Figure 5.
Inhibition of FAAH activity in rat brain homogenates by A, flurbiprofen and its 4′-hydroxy metabolite.
The AEA assay concentration was 0.5 µM. Values are means ± s.e.m. (unless enclosed by the symbols), n = 3.
Table 3.
pI50 and IC50 values for ibuprofen, flurbiprofen and their metabolites towards the inhibition of 0.5 µM [3H]AEA hydrolysis by rat brain FAAH.