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Interaction of L-lysine and soluble elastin with the semicarbazide-sensitive amine oxidase in the context of its vascular-adhesion and tissue maturation functions.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 2010 Apr; Vol. 1804 (4), pp. 941-7. Date of Electronic Publication: 2010 Jan 15. - Publication Year :
- 2010
-
Abstract
- The copper-containing quinoenzyme semicarbazide-sensitive amine oxidase (EC 1.4.3.21; SSAO) is a multifunctional protein. In some tissues, such as the endothelium, it also acts as vascular-adhesion protein 1 (VAP-1), which is involved in inflammatory responses and in the chemotaxis of leukocytes. Earlier work had suggested that lysine might function as a recognition molecule for SSAO/VAP-1. The present work reports the kinetics of the interaction of L-lysine and some of its derivatives with SSAO. Binding was shown to be saturable, time-dependent but reversible and to cause uncompetitive inhibition with respect to the amine substrate. It was also specific, since D-lysine, L-lysine ethyl ester and epsilon-acetyl-L-lysine, for example, did not bind to the enzyme. The lysine-rich protein soluble elastin bound to the enzyme relatively tightly, which may have relevance to the reported roles of SSAO in maintaining the extracellular matrix (ECM) and in the maturation of elastin. Our data show that lysyl residues are not oxidized by SSAO, but they bind tightly to the enzyme in the presence of hydrogen peroxide. This suggests that binding in vivo of SSAO to lysyl residues in physiological targets might be regulated in the presence of H(2)O(2), formed during the oxidation of a physiological SSAO substrate, yet to be identified.<br /> (Copyright 2010 Elsevier B.V. All rights reserved.)
- Subjects :
- Amine Oxidase (Copper-Containing) antagonists & inhibitors
Animals
Blood Vessels metabolism
Cattle
Cell Adhesion physiology
Endothelial Cells cytology
Endothelial Cells metabolism
Enzyme Inhibitors metabolism
Enzyme Inhibitors pharmacology
Extracellular Matrix metabolism
Hydrogen Peroxide metabolism
In Vitro Techniques
Kinetics
Lysine analogs & derivatives
Lysine pharmacology
Solubility
Amine Oxidase (Copper-Containing) metabolism
Cell Adhesion Molecules metabolism
Elastin metabolism
Lysine metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1804
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 20079884
- Full Text :
- https://doi.org/10.1016/j.bbapap.2010.01.003