<I>Mechanism of tuftsin inactivation by polymorphonuclear neutrophils</I>

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The subcellular localization of the tuftsin-inactivating activity was studied using guinea pig polymorphonuclear neutrophils (PMNs) and the following results were obtained. Tuftsin-inactivating activity was present in the membrane fraction. When PMNs wer modified chemically by a poorly permeant reagent, diazotized sulfanilic acid (DSA), to inhibit ecto-enzymes selectively, PMNs lost the tuftsin-inactivating activity, suggesting that the tuftsin-inactivatingyactivity is localized on the cell surface as an ecto-enzyme. When PMNs were modified by DSA at different concentrations, the degree of inhibitionby DSA of the tuftsin-inactivating activity was proportional to the degree of inhibition of the activity of leucine aminopeptidase (LAP), an ecto-enzyme. These results suggest the possibility that LAP may be identical with the tuftsin-inactivating enzyme or at least may act as one of the tuftsin-inactivating enzymes.
日本炎症・再生医学会の論文