Interaction of L-lysine and soluble elastin with the semicarbazide-sensitive amine oxidase in the context of its vascular-adhesion and tissue maturation functions.
Fortuny, Luis Raimon Alvarez
Vives, Itziar Larrauri
Tipton, Keith F
AffiliationSchool of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland. firstname.lastname@example.org
MeSHAmine Oxidase (Copper-Containing)
Cell Adhesion Molecules
MetadataShow full item record
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. Acta
JournalBiochimica et biophysica acta
AbstractThe copper-containing quinoenzyme semicarbazide-sensitive amine oxidase (EC 220.127.116.11; 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.
- L-lysine as a recognition molecule for the VAP-1 function of SSAO.
- Authors: Olivieri A, Tipton K, O'Sullivan J
- Issue date: 2007
- Soluble Vascular Adhesion Protein-1 Mediates Spermine Oxidation as Semicarbazide-Sensitive Amine Oxidase: Possible Role in Proliferative Diabetic Retinopathy.
- Authors: Murata M, Noda K, Kawasaki A, Yoshida S, Dong Y, Saito M, Dong Z, Ando R, Mori S, Saito W, Kanda A, Ishida S
- Issue date: 2017 Dec
- Hydrogen peroxide derived from amine oxidation mediates the interaction between aminosugars and semicarbazide-sensitive amine oxidase.
- Authors: O'Sullivan J, Davey G, O'Sullivan M, Tipton KF
- Issue date: 2007
- Developmental vasculotoxicity associated with inhibition of semicarbazide-sensitive amine oxidase.
- Authors: Langford SD, Trent MB, Balakumaran A, Boor PJ
- Issue date: 1999 Mar 15
- The inhibition of semicarbazide-sensitive amine oxidase by aminohexoses.
- Authors: O'Sullivan J, O'Sullivan M, Tipton KF, Unzeta M, Del Mar Hernandez M, Davey GP
- Issue date: 2003 Apr 11