L-lysine As a Recognition Molecule for the VAP-1 Function of SSAO

Overview

Journal J Neural Transm (Vienna)

Specialties Neurology
Physiology

Date 2007 Mar 30

PMID 17393063

Citations 3

Authors

A Olivieri

K Tipton

J OSullivan

Affiliations

Soon will be listed here.

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.

Citing Articles

Effects of an anti-inflammatory VAP-1/SSAO inhibitor, PXS-4728A, on pulmonary neutrophil migration.

Schilter H, Collison A, Russo R, Foot J, Yow T, Vieira A Respir Res. 2015; 16:42.

PMID: 25889951 PMC: 4389443. DOI: 10.1186/s12931-015-0200-z.

Implication for functions of the ectopic adipocyte copper amine oxidase (AOC3) from purified enzyme and cell-based kinetic studies.

Shen S, Wertz D, Klinman J PLoS One. 2012; 7(1):e29270.

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From caffeine to fish waste: amine compounds present in food and drugs and their interactions with primary amine oxidase.

Olivieri A, Rico D, Khiari Z, Henehan G, OSullivan J, Tipton K J Neural Transm (Vienna). 2011; 118(7):1079-89.

PMID: 21373760 DOI: 10.1007/s00702-011-0611-z.

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