Substrate specificity of caeruloplasmin. Phenylalkylamine substrates

Barrass, B. C.; Coult, D.B.; Rich, PR; Tutt, K. J.

doi:10.1016/0006-2952(74)90312-8

Cited by 18 publications

(3 citation statements)

References 12 publications

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“…That was the first indication of CP's involvement in neurodegenerative processes. Oxidation of brain catecholamines by CP was revealed in early works [24][25][26][27], but only recently was it demonstrated that, under physiological conditions, some anions increase the activity of CP with non-iron substrates by two orders, whereas Fe 2+ oxidation remains unaffected [28]. Oxidation of brain catecholamines by CP was revealed in early works [24][25][26][27], but only recently was it demonstrated that, under physiological conditions, some anions increase the activity of CP with non-iron substrates by two orders, whereas Fe 2+ oxidation remains unaffected [28].…”

Section: Some Physiological Functions Of Cpmentioning

confidence: 99%

Interactions of caeruloplasmin with other proteins participating in inflammation

Vasilyev

2010

Biochemical Society Transactions

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The first detailed report of a specific interaction of CP (caeruloplasmin) with another protein described its complex with LF (lactoferrin) in 2000. Since then, several protein-protein interactions involving CP have been reported, mostly concerning iron-containing proteins. The CP-LF complex was studied thoroughly, and evidence of reciprocal effects of CP and LF was obtained. Another specific interaction investigated in detail occurs between CP and MPO (myeloperoxidase). CP-LF, CP-MPO and CP-LF-MPO complexes were found in sera of patients with inflammation. Modelling in vitro allowed understanding of which structural peculiarities of CP and partners allow the modification of their functions in a complex. The present paper reviews the latest data on complexes of CP with LF and MPO, and advances some suggestions about their role in health and disease.

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Section: Some Physiological Functions Of Cpmentioning

confidence: 99%

Interactions of caeruloplasmin with other proteins participating in inflammation

Vasilyev

2010

Biochemical Society Transactions

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“…However, it has been suspected that o-dianisidine might be attacked by ceruloplasmin. This pathway, running through free radical formation [22][23][24][25], differed from oxidative deamination and no liberation of HzO 2 occurred. Therefore, if o-dianisidine represents a substrate for ceruloplasmin it should be oxidized without peroxidase as well.…”

Section: (1) Direct Oxidation Of O-dianisidine By Ceruloplasmlnmentioning

confidence: 99%

Determination of histaminase (diamine oxidase) activity byo-dianisidine test: Interference of ceruloplasmin

1977

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Until now o-dianisidine was used as an indicator substance in a test system for the determination of diamine oxidase. More recently, however, this substance was also used to measure ceruloplasmin activity. A study of the test principles revealed that o-dianisidine was the one denominator for both enzymes. As it was found for diamine oxidase the indicator was oxidized via peroxidase mediated H2O2 cleavage. Ceruloplasmin, however, oxidized o-dianisidine directly with resulting free radical formation. An addition of histamine dihydrochloride or putrescine dihydrochloride to an incubation mixture, containing ceruloplasmin as enzyme and o-dianisidine or p-phenylene-diamine as substrates, produced an activation of the enzyme, being more than 10-fold in the presence of 1 X 10(-2) M putrescine at pH 7.0. It was assumed that an allosteric effect of the dihydrochloride component might be responsible for this activation. When the activity of purified diamine oxidase was determined by the o-dianisidine test and by the isotope assay, a very good correlation between both methods was found. But, in a mixture of diamine oxidase and ceruloplasmin, no differentiation between the two enzymic activities by the o-dianisidine test was possible. This observation demonstrated an interference of ceruloplasmin when the o-dianisidine method was used for the determination of diamine oxidase activity. To apply our findings also in vivo the amine oxidase activity increasing in guinea-pig plasma during inflammation, was determined by the o-dianisidine test and by specific methods for some amine oxidase. Despite an enhanced oxidation of the o-dianisidine observed, only an increase of ceruloplasmin activity was found. It was concluded that ceruloplasmin had no 'histaminase activity' as has been assumed by other authors using the o-dianisidine test.

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“…Where excess albumin catabolism occurs, as for example in an inflamed tissue where both tissue destruction and tissue repair may be considerably in excess of normal, some of this extra copper could be 'off-loaded' causing either copper-mediated tissue suppression or copper-incited tissue irritation or even both simultaneously. Caeruloplasmin may have a protective role by virtue of its ability to oxidise certain amines [6].…”

Section: Association Of Copper With Inflammatory Diseasementioning

confidence: 99%

Ambivalent role of copper in inflammatory disorders

Whitehouse

1976

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Soluble copper (Cu) preparations are both acute/chronic irritants and effective anti-inflammatory agents in rats. Copper is a prevalent component in several folk remedies for arthritis. Patients with rheumatoid arthritis and ankylosing spondylitis are reported to have higher-than-normal levels of serum copper, mainly associated with albumin. The anti-arthritis drug, D-penicillamine (Pn), efficiently strips Cu from some of its (pharmacologically inert) storage forms, e.g. Cu-albumin, Cu-polynucleotides yielding low M.W. Cu-Pn complexes, which show anti-inflammatory activity (ca. 5 X phenylbutazone) in rats irritated with carrageenan, oleyl alcohol, sodium urate and adjuvants. Under certain conditions Pn also blocks the amine-oxidase activity of caeruloplasmin, a circulating copper protein which is elevated in inflamed animals (an 'acute phase reactant'). Drugs, nutritional factors and the disease process may all possibly affect the movement of copper in vivo between inert reversible pharmacoactive reversible toxic forms.

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Substrate specificity of caeruloplasmin. Phenylalkylamine substrates

Cited by 18 publications

References 12 publications

Interactions of caeruloplasmin with other proteins participating in inflammation

Interactions of caeruloplasmin with other proteins participating in inflammation

Determination of histaminase (diamine oxidase) activity byo-dianisidine test: Interference of ceruloplasmin

Ambivalent role of copper in inflammatory disorders

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