Properties and functions of tissue-bound semicarbazide-sensitive amine oxidases in isolated cell preparations and cell cultures

Lyles, Geoffrey A.; Pino, Ricardo Canavate del

doi:10.1007/978-3-7091-6499-0_23

MAO — The Mother of All Amine Oxidases

1998

DOI: 10.1007/978-3-7091-6499-0_23

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Properties and functions of tissue-bound semicarbazide-sensitive amine oxidases in isolated cell preparations and cell cultures

Geoffrey A. Lyles

Ricardo Canavate del Pino

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2009

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Cited by 6 publications

(13 citation statements)

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“…12 It has been suggested that vascular SSAO could mediate toxicological effects. 11 Taken together, these numerous studies illustrate that the functional diversity of SSAO partly depends on the nature of the cell type in which the enzyme is expressed.…”

mentioning

confidence: 97%

“…4 SSAO is also abundantly found in vascular smooth muscle cells (VSMCs) and non-VSMCs. 1,11 The high activity of SSAO in the aorta has been ascribed to its strong expression in the tunica media, which mainly contains smooth muscle cells. 11,12 The knowledge of SSAO physiology continues to progress, and putative functions of the enzyme appear pleiotropic according to the nature of the cell type.…”

mentioning

confidence: 99%

“…1,11 The high activity of SSAO in the aorta has been ascribed to its strong expression in the tunica media, which mainly contains smooth muscle cells. 11,12 The knowledge of SSAO physiology continues to progress, and putative functions of the enzyme appear pleiotropic according to the nature of the cell type. Thus, in high endothelial venules of peripheral lymphatic tissues, SSAO/ VAP-1 mediates lymphocyte binding to endothelial cells.…”

mentioning

confidence: 99%

“…11 Cultures of VSMCs derived from the media of the aorta have been used by a limited number of laboratories to characterize SSAO expression and to study the possible toxicological effects mediated by the enzyme. 15,16 However, the SSAO activities mentioned in these studies were often much lower than those reported in aortic homogenates or freshly isolated VSMCs, 16 thus suggesting that culture conditions may not be optimal for SSAO expression.…”

mentioning

confidence: 99%

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Semicarbazide-Sensitive Amine Oxidase in Vascular Smooth Muscle Cells

Hadri

Moldes

Mercier

et al. 2002

ATVB

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Abstract-Cultured vascular smooth muscle cells (VSMCs) derived from rat aortic media were used to examine semicarbazide-sensitive amine oxidase (SSAO) expression during their differentiation process. In a defined serum-free medium permissive for in vitro VSMC differentiation, there was a large increase in SSAO mRNA and protein levels and in the related enzyme activity during the course of cell culture. This pattern of expression was concomitant with that of some smooth muscle-specific mRNA markers of differentiation. mRNAs in differentiated cultured VSMCs were comparable to those detected in total aorta and media. Pharmacological properties of SSAO present in VSMCs were similar to enzyme activities previously described in the aortic wall. In this model, we also demonstrated that methylamine, a physiological substrate of SSAO, activated 2-deoxyglucose transport in a time-and dose-dependent manner. This methylamine effect was reproduced by other SSAO substrates and was prevented by the SSAO inhibitor semicarbazide. It was antagonized in the presence of catalase, suggesting that SSAO-activated glucose transport was mediated through H 2 O 2 production. In addition, methylamine promoted glucose transporter 1 accumulation at the cell surface. Thus, we demonstrate for the first time the differentiation-dependent expression of SSAO in VSMCs and its role in the regulation of VSMC glucose uptake.

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confidence: 97%

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confidence: 99%

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confidence: 99%

mentioning

confidence: 99%

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Semicarbazide-Sensitive Amine Oxidase in Vascular Smooth Muscle Cells

Hadri

Moldes

Mercier

et al. 2002

ATVB

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“…3,4 Another copper-containing amine oxidase, semicarbazidesensitive amine oxidase (SSAO), also called vascular adhesion protein-1, is highly expressed in the plasma membrane of vascular smooth muscle cells of the aortic media. [5][6][7] The exact roles of SSAO in vascular wall function remain unknown. Several previous results support the hypothesis that SSAO may be involved in vascular smooth muscle cell differentiation, organization of the ECM, 8 and regulation of vascular tone.…”

mentioning

confidence: 99%

Modifications of Arterial Phenotype in Response to Amine Oxidase Inhibition by Semicarbazide

Mercier

Hadri²,

Osborne-Pellegrin³

et al. 2007

Hypertension

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Abstract-Semicarbazide-sensitive amine oxidase (SSAO)-deficient mice present no alteration in elastin cross-linking processes and carotid mechanical properties. In contrast, previous studies have shown that SSAO inhibitors induced marked anomalies in arterial structure and function. The aim of the present study was to examine the effect of semicarbazide (SCZ), an efficient SSAO inhibitor, on the arterial phenotype of the carotid artery in relation to modulation of SSAO and lysyl oxidase activities in growing rats. We first show that after 6 weeks of SCZ treatment (100 mg/kg per day), SSAO activity was reduced by 90%, whereas lysyl oxidase activity was only partially inhibited (Ͻ60%) in carotid artery, compared with controls. There was significant growth inhibition and no difference in mean arterial pressure but an increase in pulse pressure with a smaller arterial diameter in SCZ-treated rats. SCZ decreased aortic insoluble elastin without a change in total collagen. In addition, extracellular proteins other than insoluble elastin and collagen were increased in SCZ-treated rats. All of the elastic lamellae presented globular masses along their periphery, and focal disorganization was observed in the ascending aorta. Carotid artery mechanical strength was lower in SCZ-treated rats, and the elastic modulus-wall stress curve was shifted leftward compared with controls, indicating increased stiffness. Thus, SCZ modifies arterial geometry and mechanical properties, alters elastic fiber structure, and reduces the content of cross-linked elastin. Because these abnormalities are essentially absent in SSAO-deficient mice, our results suggest that lysyl oxidase inhibition is responsible for the major part of the vascular phenotype of SCZ-treated rats. Key Words: SSAO Ⅲ carotid artery Ⅲ LOX Ⅲ arterial stiffness Ⅲ elastin T he maturation of elastin and collagen is crucial for the organization of the extracellular matrix (ECM) and to provide functional elasticity and tensile strength of the arterial wall. It is generally considered that the formation of intramolecular and extramolecular cross-links of both elastin and collagen is mediated by lysyl oxidase (LOX). LOX is a carbonyl-dependent copper enzyme, expressed, synthesized, and secreted by vascular smooth muscle cells. 1 Many years ago, Lalich 2 showed that the pharmacological inhibition of LOX with ␤-aminopropionitrile (〉APN) induced aortic ruptures and aneurysms in rat. Mice lacking LOX do not deposit normal elastic fibers and develop aortic aneurysms. 3,4 Another copper-containing amine oxidase, semicarbazidesensitive amine oxidase (SSAO), also called vascular adhesion protein-1, is highly expressed in the plasma membrane of vascular smooth muscle cells of the aortic media. [5][6][7] The exact roles of SSAO in vascular wall function remain unknown. Several previous results support the hypothesis that SSAO may be involved in vascular smooth muscle cell differentiation, organization of the ECM, 8 and regulation of vascular tone. 9 -12 Langford et al 11 have shown that p...

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The role of “semicarbazide-sensitive amine oxidase” in the arterial wall

Mercier¹

2009

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Properties and functions of tissue-bound semicarbazide-sensitive amine oxidases in isolated cell preparations and cell cultures

Cited by 6 publications

References 27 publications

Semicarbazide-Sensitive Amine Oxidase in Vascular Smooth Muscle Cells

Semicarbazide-Sensitive Amine Oxidase in Vascular Smooth Muscle Cells

Modifications of Arterial Phenotype in Response to Amine Oxidase Inhibition by Semicarbazide

The role of “semicarbazide-sensitive amine oxidase” in the arterial wall

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