Abstract
Semicarbazide-sensitive amine oxidase (EC 1.4.3.6) acts as a vascular-adhesion protein (VAP-1), mediating the adhesion of lymphocytes to vascular endothelial cells under inflammatory conditions. The relationship between the adhesive and the enzymatic functions of SSAO have not yet been fully defined. Previous studies from this laboratory showed aminohexoses, which were neither substrates nor direct inhibitors of SSAO, bound to the enzyme as reversible inhibitors in the presence of H(2)O(2) generated during substrate oxidation. The possibility that surface L-lysine could act similarly has been investigated in the present study. The presence of L-lysine during the oxidation of benzylamine resulted in time- and dose-dependent inhibition of SSAO activity, in a process that was dependent on the H(2)O(2) formed during benzylamine oxidation. The possible implications of this in terms of the therapeutic uses of lysine are discussed.
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