Interaction of L-lysine and soluble elastin with the semicarbazide-sensitive amine oxidase in the context of its vascular-adhesion and tissue maturation functions.

Hdl Handle:
http://hdl.handle.net/10147/124292
Title:
Interaction of L-lysine and soluble elastin with the semicarbazide-sensitive amine oxidase in the context of its vascular-adhesion and tissue maturation functions.
Authors:
Olivieri, Aldo; O'Sullivan, Jeff; Fortuny, Luis Raimon Alvarez; Vives, Itziar Larrauri; Tipton, Keith F
Affiliation:
School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland. oliviera@tcd.ie
Citation:
Interaction of L-lysine and soluble elastin with the semicarbazide-sensitive amine oxidase in the context of its vascular-adhesion and tissue maturation functions. 2010, 1804 (4):941-7 Biochim. Biophys. Acta
Journal:
Biochimica et biophysica acta
Issue Date:
Apr-2010
URI:
http://hdl.handle.net/10147/124292
DOI:
10.1016/j.bbapap.2010.01.003
PubMed ID:
20079884
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.
Item Type:
Article
Language:
en
MeSH:
Amine Oxidase (Copper-Containing); Animals; Blood Vessels; Cattle; Cell Adhesion; Cell Adhesion Molecules; Elastin; Endothelial Cells; Enzyme Inhibitors; Extracellular Matrix; Hydrogen Peroxide; Kinetics; Lysine; Solubility
ISSN:
0006-3002

Full metadata record

DC FieldValue Language
dc.contributor.authorOlivieri, Aldoen
dc.contributor.authorO'Sullivan, Jeffen
dc.contributor.authorFortuny, Luis Raimon Alvarezen
dc.contributor.authorVives, Itziar Larraurien
dc.contributor.authorTipton, Keith Fen
dc.date.accessioned2011-03-11T16:44:38Z-
dc.date.available2011-03-11T16:44:38Z-
dc.date.issued2010-04-
dc.identifier.citationInteraction of L-lysine and soluble elastin with the semicarbazide-sensitive amine oxidase in the context of its vascular-adhesion and tissue maturation functions. 2010, 1804 (4):941-7 Biochim. Biophys. Actaen
dc.identifier.issn0006-3002-
dc.identifier.pmid20079884-
dc.identifier.doi10.1016/j.bbapap.2010.01.003-
dc.identifier.urihttp://hdl.handle.net/10147/124292-
dc.description.abstractThe 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.-
dc.language.isoenen
dc.subject.meshAmine Oxidase (Copper-Containing)-
dc.subject.meshAnimals-
dc.subject.meshBlood Vessels-
dc.subject.meshCattle-
dc.subject.meshCell Adhesion-
dc.subject.meshCell Adhesion Molecules-
dc.subject.meshElastin-
dc.subject.meshEndothelial Cells-
dc.subject.meshEnzyme Inhibitors-
dc.subject.meshExtracellular Matrix-
dc.subject.meshHydrogen Peroxide-
dc.subject.meshKinetics-
dc.subject.meshLysine-
dc.subject.meshSolubility-
dc.titleInteraction of L-lysine and soluble elastin with the semicarbazide-sensitive amine oxidase in the context of its vascular-adhesion and tissue maturation functions.en
dc.typeArticleen
dc.contributor.departmentSchool of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland. oliviera@tcd.ieen
dc.identifier.journalBiochimica et biophysica actaen
dc.description.provinceLeinster-

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