The physiopathological significance of ceruloplasmin

Floris, Giovanni; Medda, Rosaria; Padiglia, Alessandra; Musci, Giovanni

doi:10.1016/s0006-2952(00)00399-3

Cited by 90 publications

(46 citation statements)

References 79 publications

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“…This situation is reminiscent of mammalian systems, in which ceruloplasmin, in addition to its ferrooxidase activity, is thought to oxidize catecholamines such as 6-hydroxydopamine and thereby prevent the formation of reactive oxygen species (9). For example, copper accelerated the autooxidation of 6-hydroxydopamine 61-fold (5).…”

Section: Discussionmentioning

confidence: 99%

Linkage between Catecholate Siderophores and the Multicopper Oxidase CueO in Escherichia coli

et al. 2004

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The multicopper oxidase CueO had previously been demonstrated to exhibit phenoloxidase activity and was implicated in intrinsic copper resistance in Escherichia coli. Catecholates can potentially reduce Cu(II) to the prooxidant Cu(I). In this report we provide evidence that CueO protects E. coli cells by oxidizing enterobactin, the catechol iron siderophore of E. coli, in the presence of copper. In vitro, a mixture of enterobactin and copper was toxic for E. coli cells, but the addition of purified CueO led to their survival. Deletion of fur resulted in copper hypersensitivity that was alleviated by additional deletion of entC, preventing synthesis of enterobactin. In addition, copper added together with 2,3-dihydroxybenzoic acid or enterobactin was able to induce a ⌽(cueO-lacZ) operon fusion more efficiently than copper alone. The reaction product of the 2,3-dihydroxybenzoic acid oxidation by CueO that can complex Cu(II) ions was determined by gas chromatography-mass spectroscopy and identified as 2-carboxymuconate.

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Section: Discussionmentioning

confidence: 99%

Linkage between Catecholate Siderophores and the Multicopper Oxidase CueO in Escherichia coli

et al. 2004

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“…Ceruloplasmin is a multifunctional protein both storing and transporting copper within the body. Ceruloplasmin donates copper in a regulatory fashion with evidence of CP receptors on the membranes of numerous different cell types, supporting CP's role as a cell signalling multifunctional enzyme within many different metabolic pathways (Floris et al, 2000). Ceruloplasmin is an antioxidant protein, scavenging reactive oxygen species and preventing their formation through its involvement in iron homeostasis.…”

Section: Ceruloplasminmentioning

confidence: 93%

Acute phase proteins: a review of their function, behaviour and measurement in chickens

O'Reilly

Eckersall

2014

World's Poultry Science Journal

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This review brings together and consolidates the large amount of research on acute phase proteins (APPs) that has been undertaken in chickens. Acute phase proteins are secreted from the liver as a result of inflammation or infection that can be measured in plasma. They have been well-characterised in other farm animal species and have been measured in a wide variety of poultry research areas. The acceleration in chicken APP research is in response to increased interest in ways the immune responses of the chicken can be measured and compared during infection or environmental or nutritional changes. All APPs that have been identified and characterised in chickens are described in the following review and their responses during infection discussed. The APPs are tabulated with basal values and classification to provide a comparative and useful reference. The ways APPs can be measured in chickens and the assays available are also described. This review will detail the functions of the positive APPs in chickens and their behaviour during an APR.

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“…In the blood, Fe 2ϩ is oxidized to Fe 3ϩ by ceruloplasmin or hephaestin so that it can be coupled with transferrin, which is the predominant serum iron carrier protein. 52,54,55 However, iron circulating in this form in the blood outside of the CNS can not directly cross the blood brain barrier (BBB). There are several pathways that can transfer iron across the BBB.…”

Section: Iron Transportmentioning

confidence: 99%

“…61 Finally, after the brain uses the iron it has stored, the iron must leave the cell, and the copper-associated protein ceruloplasmin may facilitate cellular release of iron. 52,54 Iron leaves the body via bleeding or through the shedding of skin and other cells. 55 …”

Section: Iron Transportmentioning

confidence: 99%

Iron in Chronic Brain Disorders: Imaging and Neurotherapeutic Implications

et al. 2007

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Summary:Iron is important for brain oxygen transport, electron transfer, neurotransmitter synthesis, and myelin production. Though iron deposition has been observed in the brain with normal aging, increased iron has also been shown in many chronic neurological disorders including Alzheimer's disease, Parkinson's disease, and multiple sclerosis. In vitro studies have demonstrated that excessive iron can lead to free radical production, which can promote neurotoxicity. However, the link between observed iron deposition and pathological processes underlying various diseases of the brain is not well understood. It is not known whether excessive in vivo iron directly contributes to tissue damage or is solely an epiphenomenon. In this article, we focus on the imaging of brain iron and the underlying physiology and metabolism relating to iron deposition. We conclude with a discussion of the potential implications of iron-related toxicity to neurotherapeutic development.

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The physiopathological significance of ceruloplasmin

Cited by 90 publications

References 79 publications

Linkage between Catecholate Siderophores and the Multicopper Oxidase CueO in Escherichia coli

Linkage between Catecholate Siderophores and the Multicopper Oxidase CueO in Escherichia coli

Acute phase proteins: a review of their function, behaviour and measurement in chickens

Iron in Chronic Brain Disorders: Imaging and Neurotherapeutic Implications

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