Semicarbazide-sensitive amine oxidase activity exerts insulin-like effects on glucose metabolism and insulin-signaling pathways in adipose cells

Zorzano, António; Abella, Annie; Marti, Luc; Carpéné, Christian; Palacı́n, Manuel; Testar, Xavier

doi:10.1016/s1570-9639(03)00039-6

Cited by 70 publications

(61 citation statements)

References 62 publications

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“…In general, the end-products of the reaction at high concentrations are highly cytotoxic and implicated in playing a role in various processes resulting in cellular damage, like atherosclerosis and vascular complications in diabetes [1][2][3]. In addition, SSAO activity has been shown to be involved in glucose transport [4][5][6], adipocyte differentiation [7], and structural organization of vascular smooth muscle [8,9]. The physiological substrates for the SSAOs are still poorly known, but it is hypothesized that the soluble amines methylamine and/or aminoacetone could be among the naturally occurring substrates for the SSAOs [10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase

Kaitaniemi

Elovaara

Grön

et al. 2009

Cell. Mol. Life Sci.

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Semicarbazide-sensitive amine oxidases (SSAOs) catalyze oxidative deamination of primary amines, but the true physiological function of these enzymes is still poorly understood. Here, we have studied the functional and structural characteristics of a human cell-surface SSAO, AOC2, which is homologous to the better characterized family member, AOC3. The preferred in vitro substrates of AOC2 were found to be 2-phenylethylamine, tryptamine and p-tyramine instead of methylamine and benzylamine, the favored substrates of AOC3. Molecular modeling suggested structural differences between AOC2 and AOC3, which provide AOC2 with the capability to use the larger monoamines as substrates. Even though AOC2 mRNA was expressed in many tissues, the only tissues with detectable AOC2-like enzyme activity were found in the eye. Characterization of AOC2 will help in evaluating the contribution of this enzyme to the pathological processes attributed to the SSAO activity and in designing specific inhibitors for the individual members of the SSAO family.

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Section: Introductionmentioning

confidence: 99%

The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase

Kaitaniemi

Elovaara

Grön

et al. 2009

Cell. Mol. Life Sci.

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“…These insulinlike effects result from an increased tyrosine phosphorylation of intracellular proteins that is, in turn, mediated by the inhibition of protein tyrosine phosphatases via the oxidation of a unique cysteine residue of their active site [23]. We have already shown that a hydrogen peroxide-dependent mechanism is involved in the insulin-mimicking effects of an SSAO substrate of reference, benzylamine, which, in rat adipocytes and especially in the presence of vanadate, is able to increase insulin receptor substrate phosphorylation, phosphoinositide 3-kinase activity and glucose transporter translocation [24].…”

Section: Introductionmentioning

confidence: 99%

Short- and long-term insulin-like effects of monoamine oxidases and semicarbazide-sensitive amine oxidase substrates in cultured adipocytes

Carpéné¹,

Daviaud²,

Boucher³

et al. 2006

Metabolism

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“…It remains to be established whether the binding capacity of SSAO, acting as VAP-1, is modulated by the presence of substrate oxidation, during the inflammatory process. H 2 O 2 formed during substrate oxidation is known to be involved in mediating some other functions of SSAO, including the promotion of glucose transport [see 1,8,29]. In that case it has been proposed that methylamine, formed by the intracellular metabolism of adrenaline by monoamine oxidase, may be the physiological substrate [30].…”

Section: Discussionmentioning

confidence: 99%

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

Olivieri

O'Sullivan

Fortuny

et al. 2010

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Interaction of l-lysine and soluble elastin with the semicarbazide-sensitive amine oxidase in the context of its vascularadhesion and tissue maturation functions, BBA -Proteins and Proteomics (2010), doi: 10.1016/j.bbapap.2010 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Corresponding author: Aldo Olivieri, oliviera@tcd.ie A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT 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 ε-acetyl-L-lysine, for example, did not bind to the enzyme. The lysinerich protein soluble elastin bound to the enzyme relatively tightly, which may have relevance to the reported roles of SSAO in maintaining the extra-cellular 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.

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Semicarbazide-sensitive amine oxidase activity exerts insulin-like effects on glucose metabolism and insulin-signaling pathways in adipose cells

Cited by 70 publications

References 62 publications

The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase

The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase

Short- and long-term insulin-like effects of monoamine oxidases and semicarbazide-sensitive amine oxidase substrates in cultured adipocytes

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

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