Abstract
γ-Glutamyl transpeptidase (γ-GT) plays an important role in the turnover of glutathione and protein biosynthesis. Because in inflammation both catabolic and anabolic steps are activated together with migration of cells, an alteration in γ-GT activity was postulated to occur at the site of inflammation with the development of the inflammatory process. We discovered that γ-GT activity was increased markedly at sites of inflammation produced in several ways in rats. A significant increase in enzyme activity appeared soon after the induction of inflammation. In carrageenin-induced acute inflammation, the paw tissue attained a 3- to 4-fold increase in enzyme activity within 4 hr; in established adjuvant arthritis, a 20- to 24-fold increase over its basal activity occured in the rat paw tissue. The specific enzyme activity was 20–22 nmoles/min/mg protein in the cellular sediment of carrageenin-induced pleural exudate. In cotton granulomatous tissue it was 5- to 6-fold higher compared to the enzyme activity of the skeletal muscles. The in vivo in γ-GT activity was prevented from occuring in proportion to the anti-inflammatory potencies of the test drugs given orally. The prevention of enzyme activity was observed with indomethacin in carrageenin-induced edematous paw tissue and with phenylbutazone in both adjuvant arthritis and carrageenin-induced pleural exudate. Prednisolone was observed to be the most potent drug against cotton granuloma. Nonsteroidal anti-inflammatory drugs (NSAIDs) were not found to affect enzyme activity in vitro when incubated with cellular infiltrate from a cotton pellet granuloma. Differences in certain physico-chemical characteristics, viz. stability at 50°, pH dependency and effects of solvents, were not discernible in between the enzyme activities of the untreated and edematous paw tissues. The studies thus suggest that measurement of γ-GT in inflammation may prove to be a valuable biochemical marker for the assessment of anti-inflammatory activity of drugs in vivo.
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