Human Vascular Adhesion Protein-1 in Smooth Muscle Cells

Jaakkola, Kimmo; Kaunismäki, Katja; Tohka, Sami; Yegutkin, Gennady G.; Vänttinen, E; Havia, T; Pelliniemi, Lauri J.; Virolainen, Martti; Jalkanen, Sirpa; Salmi, Marko

doi:10.1016/s0002-9440(10)65514-9

Cited by 74 publications

(60 citation statements)

References 38 publications

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“…It is therefore conceivable that in addition to soluble primary amines, Lox and SSAO may act on amino acids included in matrix proteins. In addition, considering our methodological approach and the size of arterial samples, it is not possible to establish the relationship between SSAO tissue expression and activity, but this has previously investigated in the work of Jaakkola et al (1999) and Andres et al (2001). In this context, further morphological, biochemical, and molecular investigations will be required to determine this relationship and the exact nature of the SSAO substrate(s) in the blood vessels.…”

Section: Discussionmentioning

confidence: 99%

Semicarbazide-sensitive Amine Oxidase in Annulo-aortic Ectasia Disease: Relation to Elastic Lamellae-associated Proteins

Sibon

Larrieu

Hadri³

et al. 2004

J Histochem Cytochem.

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Inserm U441 (IS,DL,DD,JB,J-MDL), Pessac, France, and CNRS UMR 7079 (KEH,NM,BF) and Inserm EMI U01-07 (CL,PL), Paris, France S U M M A R Y Lysyl oxidases (Lox), which are members of the amine oxidase family, are involved in the maturation of elastic lamellae and collagen fibers. Modifications of amine oxidases in idiopathic annulo-aortic ectasia disease (IAAED) have never been investigated. Our aim was to examine the expression of several proteins that might interfere with elastic fiber organization in control ( n ϭ 10) and IAAED ( n ϭ 18) aortic tissues obtained at surgery. Expression of amine oxidases and semicarbazide-sensitive amine oxidase (SSAO), and cellular phenotypic markers were examined by immunohistopathology and confocal microscopy. The expression of these proteins was assessed in relation to clinical and histomorphological features of the arterial wall. In control aorta, SSAO staining was expressed along elastic lamellae, whereas in aneurysmal areas of IAAED, SSAO was markedly decreased, in association with severe disorganization of elastic lamellae. Smooth muscle myosin heavy chain was also decreased in IAAED compared with controls, indicating smooth muscle cell dedifferentiation. Multiple regression analysis showed that elastic lamellar thickness (ELT) was correlated positively with the SSAO:elastin ratio and negatively with the Lox:elastin ratio, and that the clinical features of IAAED (aneurysm, thoracic aorta diameter, and aortic insufficiency) were positively correlated with ELT but not with SSAO. The relationship between SSAO expression and ELT suggests that this amine oxidase may be involved in elastic fiber organization. However, in advanced IAAED, the deficit in SSAO expression could be secondary to the decrease and fragmentation of elastic fibers and/or to vascular smooth muscle cell dedifferentiation. (J Histochem

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Section: Discussionmentioning

confidence: 99%

Semicarbazide-sensitive Amine Oxidase in Annulo-aortic Ectasia Disease: Relation to Elastic Lamellae-associated Proteins

Sibon

Larrieu

Hadri³

et al. 2004

J Histochem Cytochem.

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“…VAP-1, an adhesion protein with the same primary structure as tissue-bound SSAO, has been located in the endothelial wall of the high endothelial venules (Bono et al 1999). Expressed in inflammatory conditions, it binds to lymphocytes and helps them to migrate between endothelial cells into lymphoid organs (Jaakkola et al 1999). The presence of SSAO IR in lymphatic vessels and brain microvessels (Castillo et al 1998), but not in endothelial cells of large blood vessels, might reflect its duality as an enzyme and an adhesion protein.…”

Section: Discussionmentioning

confidence: 99%

“…A vascular adhesion protein, VAP-1, with identical sequence to the tissue-bound SSAO has recently been described Bono et al 1998). Because VAP-1 is involved in lymphocyte migration to lymphoid organs, a new physiological role for SSAO in cellular trafficking has been suggested Jaakkola et al 1999).…”

mentioning

confidence: 99%

Tissue Activity and Cellular Localization of Human Semicarbazide-sensitive Amine Oxidase

Andrés

Lizcano

Rodrı́guez

et al. 2001

J Histochem Cytochem.

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S U M M A R Y Semicarbazide-sensitive amine oxidase (SSAO), widely distributed in highly vascularized mammalian tissues, metabolizes endogenous and xenobiotic aromatic and aliphatic monoamines. To assess whether its physiological role in humans is restricted to oxidation, we used an immunohistochemical approach to examine the cellular localization of SSAO in human peripheral tissues (adrenal gland, duodenum, heart, kidney, lung, liver, pancreas, spleen, thyroid gland, and blood vessels) and also analyzed its subcellular localization. The results are in agreement with the specific activities also determined in the same samples and are discussed with reference to the tissue distribution of monoamine oxidase A and B. Together with the oxidative deamination of monoamines, SSAO cellular localization indicates that, in most human peripheral tissues, it might participate in the regulation of physiological processes via H 2 O 2 generation.

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“…However, it is unclear how a SSAO inhibitor would affect the variety of cardiovascular and noncardiovascular pools of SSAO activity, including adipose and gastrointestinal tract smooth muscle, where the function of SSAO also remains undetermined (18). For example, the SSAO protein homolog vascular adhesion protein-1 (VAP-1) expressed in endothelial and vascular smooth muscle cells mediates lymphocyte binding (26,41). Whereas previous studies detect little to no SSAO activity in endothelial cell cultures (50), purified human and bovine brain microvessels possess concentrated SSAO activity with relatively high affinity for MA (11).…”

Section: Implications For Human Health: Pharmacological and Toxicologmentioning

confidence: 99%

Vasoactive effects of methylamine in isolated human blood vessels: role of semicarbazide-sensitive amine oxidase, formaldehyde, and hydrogen peroxide

Conklin¹,

Cowley²,

Wiechmann

et al. 2004

American Journal of Physiology-Heart and Circulatory Physiology

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. Vasoactive effects of methylamine in isolated human blood vessels: role of semicarbazide-sensitive amine oxidase, formaldehyde, and hydrogen peroxide. Am J Physiol Heart Circ Physiol 286: H667-H676, 2004; 10.1152/ajpheart.00690. 2003.-It is hypothesized that methylamine (MA) and semicarbazidesensitive amine oxidase (SSAO) activity are involved in the cardiovascular complications in human diabetics. To test this, we 1) determined the acute vasoactive effects of MA (1-1,000 mol/l) in uncontracted and norepinephrine (NE; 1 mol/l)-precontracted human blood vessels used for coronary artery bypass grafts [left internal mammary artery (LIMA), radial artery (RA), and right saphenous vein (RSV)]; 2) tested whether MA effects in LIMA and RSV were dependent on SSAO activity using the SSAO inhibitor semicarbazide (1 mmol/l, 15 min); 3) determined the effects of MA metabolites formaldehyde and hydrogen peroxide in LIMA and RSV; 4) tested whether the MA response was nitric oxide, prostaglandin, or hyperpolarization dependent; 5) measured the LIMA and RSV cGMP levels after MA exposure; and 6) quantified SSAO activity in LIMA, RA, and RSV. In NE-precontracted vessels, MA stimulated a biphasic response in RA and RSV (rapid contraction followed by prolonged relaxation) and dominant relaxation in LIMA (mean Ϯ SE, %relax-ation: 55.4 Ϯ 3.9, n ϭ 30). The MA-induced relaxation in LIMA was repeatable, nontoxic, and age independent. Semicarbazide significantly blocked MA-induced relaxation (%inhibition: 82.5 Ϯ 4.8, n ϭ 7) and SSAO activity (%inhibition: 98.1 Ϯ 1.3, n ϭ 26) in LIMA. Formaldehyde (%relaxation: 37.3 Ϯ 18.6, n ϭ 3) and H 2O2 (%relax-ation: 55.6 Ϯ 9.0, n ϭ 9) at 1 mmol/l relaxed NE-precontracted LIMA comparable with MA. MA-induced relaxation in LIMA was nitric oxide, prostaglandin, and possibly cGMP independent and blocked by hyperpolarization. We conclude that vascular SSAO activity may convert endogenous amines, like MA, to vasoactive metabolites. amine metabolism; coronary artery bypass grafts; diabetes; H2O2 A CURRENT HYPOTHESIS STATES that chronic methylamine (MA) exposure induces vascular injury and promotes vascular disease, including atherosclerosis, in humans via semicarbazidesensitive amine oxidase-mediated (SSAO) metabolism of MA to injurious metabolites: formaldehyde, H 2 O 2 , and ammonia (NH 3 ) (19, 50-52). Recent clinical and experimental studies support such a relationship. Altered plasma MA levels, MA excretion, and elevated plasma SSAO activity are present in human diseases associated with chronic vascular pathology [e.g., diabetes mellitus and uremia (Refs. 3,5,6,27, and 49; for reviews, see Refs. 19 and 51)]. In the case of Type I diabetes, SSAO plasma levels increase at the onset of disease (6) and plasma SSAO activity positively correlates with the amount of glycosylated hemoglobin, an indicator of the severity of complications in human diabetics (5, 43). Similarly, plasma SSAO activity is elevated within 2 wk after streptozotocin-induced diabetes in rats (22). Thus much circumstantial evidence link...

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Human Vascular Adhesion Protein-1 in Smooth Muscle Cells

Cited by 74 publications

References 38 publications

Semicarbazide-sensitive Amine Oxidase in Annulo-aortic Ectasia Disease: Relation to Elastic Lamellae-associated Proteins

Semicarbazide-sensitive Amine Oxidase in Annulo-aortic Ectasia Disease: Relation to Elastic Lamellae-associated Proteins

Tissue Activity and Cellular Localization of Human Semicarbazide-sensitive Amine Oxidase

Vasoactive effects of methylamine in isolated human blood vessels: role of semicarbazide-sensitive amine oxidase, formaldehyde, and hydrogen peroxide

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