Amine oxidases are widely distributed from microorganisms to vertebrates and produce hydrogen peroxide plus aldehyde when catabolizing endogenous or xenobiotic amines. Novel roles have been attributed to several members of the amine oxidase families, which cannot be more considered as simple amine scavengers. Semicarbazide-sensitive amine oxidase (SSAO) is abundantly expressed in mammalian endothelial, smooth muscle, and fat cells, and plays a role in lymphocyte adhesion to vascular wall, arterial fiber elastic maturation, and glucose transport, respectively. This latter role is detailed and the perspectives opened by the insulin-like actions of amine oxidase substrates are discussed in the present review. Independent studies have demonstrated that SSAO substrates and monoamine oxidase substrates mimic diverse insulin effects in adipocytes: glucose transport activation, lipogenesis stimulation and lipolysis inhibition. These substrates also stimulate in vitro adipogenesis. Acute in vivo administration of amine oxidase substrates improves glucose tolerance in rats, mice and rabbits, while chronic treatments with benzylamine plus vanadate exert an antihyperglycaemic effect in diabetic rats. Dietary supplementations with methylamine, benzylamine or tyramine have been evidenced to influence metabolic control in rodents by increasing glucose tolerance or decreasing lipid mobilisation, without noticeable changes in the plasma markers of lipid peroxidation or protein glycation, despite adverse effects on vasculature. Thus, the ingested amines are not totally degraded at the intestinal barreer and can act on adipose and vascular tissues. In regard with this influence on metabolic control, more attention must be paid to the composition or supplementation in amines in foods and nutraceutics.

Amine oxidase substrates for impaired glucose tolerance correction / C., Carpene; S., Bour; V., Visentin; Pellati, Federica; Benvenuti, Stefania; M. C., Iglesias Osma; M. J., Garcia Barrado; P., Valet. - In: JOURNAL OF PHYSIOLOGY AND BIOCHEMISTRY. - ISSN 1138-7548. - STAMPA. - 61:(2005), pp. 405-419. [10.1007/BF03167058]

Amine oxidase substrates for impaired glucose tolerance correction

PELLATI, Federica;BENVENUTI, Stefania;
2005

Abstract

Amine oxidases are widely distributed from microorganisms to vertebrates and produce hydrogen peroxide plus aldehyde when catabolizing endogenous or xenobiotic amines. Novel roles have been attributed to several members of the amine oxidase families, which cannot be more considered as simple amine scavengers. Semicarbazide-sensitive amine oxidase (SSAO) is abundantly expressed in mammalian endothelial, smooth muscle, and fat cells, and plays a role in lymphocyte adhesion to vascular wall, arterial fiber elastic maturation, and glucose transport, respectively. This latter role is detailed and the perspectives opened by the insulin-like actions of amine oxidase substrates are discussed in the present review. Independent studies have demonstrated that SSAO substrates and monoamine oxidase substrates mimic diverse insulin effects in adipocytes: glucose transport activation, lipogenesis stimulation and lipolysis inhibition. These substrates also stimulate in vitro adipogenesis. Acute in vivo administration of amine oxidase substrates improves glucose tolerance in rats, mice and rabbits, while chronic treatments with benzylamine plus vanadate exert an antihyperglycaemic effect in diabetic rats. Dietary supplementations with methylamine, benzylamine or tyramine have been evidenced to influence metabolic control in rodents by increasing glucose tolerance or decreasing lipid mobilisation, without noticeable changes in the plasma markers of lipid peroxidation or protein glycation, despite adverse effects on vasculature. Thus, the ingested amines are not totally degraded at the intestinal barreer and can act on adipose and vascular tissues. In regard with this influence on metabolic control, more attention must be paid to the composition or supplementation in amines in foods and nutraceutics.
2005
61
405
419
Amine oxidase substrates for impaired glucose tolerance correction / C., Carpene; S., Bour; V., Visentin; Pellati, Federica; Benvenuti, Stefania; M. C., Iglesias Osma; M. J., Garcia Barrado; P., Valet. - In: JOURNAL OF PHYSIOLOGY AND BIOCHEMISTRY. - ISSN 1138-7548. - STAMPA. - 61:(2005), pp. 405-419. [10.1007/BF03167058]
C., Carpene; S., Bour; V., Visentin; Pellati, Federica; Benvenuti, Stefania; M. C., Iglesias Osma; M. J., Garcia Barrado; P., Valet
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/310635
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