Effect of NADH on the Ceruloplasmin Catalyzed Oxidation of Dopamine and Noradrenaline.

Løvstad, Rolf A.; Odham, Göran; Pettersson, Bente; Svensson, Sigfrid; Koskikallio, J.; Kachi, Sukeji

doi:10.3891/acta.chem.scand.25-3144

Cited by 16 publications

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“…However, the oxidation of synthetic substrates 23 as well as physiologically important substrates such as DA, NE and E are all catalyzed by CP. [25][26][27] Neurons do not express CP, but instead, we recently found, depend on amyloid precursor protein (APP) for iron-export ferroxidase activity. 28 APP is a transmembrane protein expressed in most tissues.…”

Section: Introductionmentioning

confidence: 99%

Amine oxidase activity of β-amyloid precursor protein modulates systemic and local catecholamine levels

et al. 2012

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The catecholamines dopamine (DA), norepinephrine (NE) and epinephrine (E) are neurotransmitters and hormones that mediate stress responses in tissues and plasma. The expression of β-amyloid precursor protein (APP) is responsive to stress and is high in tissues rich in catecholamines. We recently reported that APP is a ferroxidase, subsuming, in neurons and other cells, the iron-export activity that ceruloplasmin mediates in glia. Here we report that, like ceruloplasmin, APP also oxidizes synthetic amines and catecholamines catalytically (K(m) NE=0.27 mM), through a site encompassing its ferroxidase motif and selectively inhibited by zinc. Accordingly, APP knockout mice have significantly higher levels of DA, NE and E in brain, plasma and select tissues. Consistent with this, these animals have increased resting heart rate and systolic blood pressure as well as suppressed prolactin and lymphocyte levels. These findings support a role for APP in extracellular catecholaminergic clearance.

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Section: Introductionmentioning

confidence: 99%

Amine oxidase activity of β-amyloid precursor protein modulates systemic and local catecholamine levels

et al. 2012

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“…The formation of adrenochrome, as a result of lactoperoxidase action on adrenaline, was monitored spectrophotometrically at 485 nm. A molar absorption coefficient of 4020 M −1 cm −1 , determined according to a method described in a previous publication (Løvstad 1971), was used for calculating the enzyme activity. The rate of lactoperoxidase dependent urate oxidation was determined from the decrease of the 295 nm absorption band, characterizing the compound (ε = 11 000 M −1 cm −1 ).…”

Section: Methodsmentioning

confidence: 99%

Effect of urate on the lactoperoxidase catalyzed oxidation of adrenaline

Løvstad

2004

Biometals

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Lactoperoxidase is an iron containing enzyme, which is an essential component of the defense system of mammalian secretary fluids. The enzyme readily oxidizes adrenaline and other catecholamines to coloured aminochrome products. A Km-value of 1.21 mM and a catalytic constant (k = Vmax/[Enz]) of 15.5 x 10(3) min(-1) characterized the reaction between lactoperoxidase and adrenaline at pH 7.4. Urate was found to activate the enzyme catalyzed oxidation of adrenaline in a competitive manner, the effect decreasing with increasing adrenaline concentration. Lactoperoxidase was able to catalyze the oxidation of urate. However, urate was a much poorer substrate than adrenaline, and it seems unlikely that urate activates by functioning as a free, redox cycling intermediate between enzyme and adrenaline. The activation mechanism probably involves an urate-lactoperoxidase complex.

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“…Aminochrome compounds absorb light in the visible region. Rate of aminochrome formation from catecholamines was determined spectrophotometrically as described by Osaki (1963) and Lsvstad (1971).…”

Section: Methodsmentioning

confidence: 99%

Catecholamine Stimulation of Copper Dependent Haemolysis: Protective Action of Superoxide Dismutase, Catalase, Hydroxyl Radical Scavengers and Serum Proteins (Ceruloplasmin, Albumin and Apotransferrin)

Løvstad

1984

Acta Pharmacologica et Toxicologica

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Abstracl:Copper induced lysis of washed rat erythrocytes was stimulated by catecholamines, the order of effectiveness being: adrenaline > noradrenaline 1 dopamine > L-DOPA. The degree of effectiveness is related to the rate of copper ion dependent oxidation of catecholamine, adrenaline being more rapidly oxidized than the other catecholamines investigated. Superoxide dismutase, catalase and different hydroxyl radical scavengers (mannitol, tris, formate and ethanol) markedly reduced the haemolytic effect of copper and catecholamine, suggesting the possibility that superoxide radicals and hydrogen peroxide, formed in the reaction system, cooperate in producing hydroxyl radicals, which are directly involved in the haemolytic action. The plasma proteins, ceruloplasmin, albumin and apotransferrin, also reduced the copper-catecholamine induced haemolysis. The protective action is probably not related to the copper binding ability of thesc proteins.

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Effect of NADH on the Ceruloplasmin Catalyzed Oxidation of Dopamine and Noradrenaline.

Cited by 16 publications

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Amine oxidase activity of β-amyloid precursor protein modulates systemic and local catecholamine levels

Amine oxidase activity of β-amyloid precursor protein modulates systemic and local catecholamine levels

Effect of urate on the lactoperoxidase catalyzed oxidation of adrenaline

Catecholamine Stimulation of Copper Dependent Haemolysis: Protective Action of Superoxide Dismutase, Catalase, Hydroxyl Radical Scavengers and Serum Proteins (Ceruloplasmin, Albumin and Apotransferrin)

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