Studies on Copper Metabolism. Xiv. Copper, Cerulo-Plasmin and Oxidase Activity in Sera of Normal Human Subjects, Pregnant Women, and Patients With Infection, Hepatolenticular Degeneration and the Nephrotic Syndrome 1

Markowitz, Harold; Gubler, C. J.; Mahoney, John P.; Cartwright, G. E.; Wintrobe, M. M.

doi:10.1172/jci103201

Cited by 211 publications

(62 citation statements)

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“…In a series of reports beginning in 1952, Maxwell Wintrobe 3 and co-workers demonstrated that copper deficiency in swine caused a systemic iron deficiency and a deficit in a variety of hematologic parameters. For example, cytochrome c oxidase activity was seen to be lower in these copper-deficient animals, as was the oxidase activity in the plasma toward p-phenylenediamine, an activity that was associated with the level of copperreplete active ceruloplasmin (13)(14)(15). Similar results were obtained in studies on rats and humans, although human swayback has only recently been recognized clinically as a copper deficiency myelopathy (16,17).…”

Section: Introductionmentioning

confidence: 58%

Redox Cycling in Iron Uptake, Efflux, and Trafficking

Kosman

2010

Journal of Biological Chemistry

106

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Aerobic organisms are faced with a dilemma. Environmental iron is found primarily in the relatively inert Fe(III) form, whereas the more metabolically active ferrous form is a strong pro-oxidant. This conundrum is solved by the redox cycling of iron between Fe(III) and Fe(II) at every step in the iron metabolic pathway. As a transition metal ion, iron can be "metabolized" only by this redox cycling, which is catalyzed in aerobes by the coupled activities of ferric iron reductases (ferrireductases) and ferrous iron oxidases (ferroxidases).Following the first crystallization of a protein, jack bean urease, reported by Sumner in 1926 (1), the evolution of protein chemistry remained a slow process, hampered by limitations in techniques for protein resolution and analysis. Not surprisingly, many proteins obtained in relatively pure form were those with prosthetic metal ion groups that imparted a visible absorbance to guide the purification. Some were copper proteins whose Cu(II) spectral properties gave their protein host a greenish blue to bright blue hue. Two of these were from mammalian whole blood: hemocuprein (cupric species from erythrocytes, superoxide dismutase) and ceruloplasmin (cerulean blue species from plasma). Superoxide dismutase was first isolated in 1938 by Mann and Keilin (5); Cp 2 was first isolated in 1948 by Holmberg and Laurell (6). Both proteins play essential roles in aerobic homeostasis. In the case of ceruloplasmin and the other copper proteins that share its substrate specificity, this role is to manage the redox state of iron in the metabolism of this essential yet potentially cytotoxic transition metal ion. These proteins, all of which are members of the MCO family (7-9), and the mechanism by which they provide this function are a focus of this minireview.

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Section: Introductionmentioning

confidence: 58%

Redox Cycling in Iron Uptake, Efflux, and Trafficking

Kosman

2010

Journal of Biological Chemistry

106

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“…However, its function in vivo is still unknown. In previous studies (1,10,11), insufficient data were presented to determine if the oxidase activity per milligram of ceruloplasmin in sera from patients with Wilson's disease differs significantly from normal. Furthermore, these studies were performed on serum, in which inhibitory factors occur in variable amounts (12), and therefore may not accurately compare the oxidase activity per mole of pure ceruloplasmin in Wilson's disease to that of ceruloplasmin in normal individuals.…”

Section: Introductionmentioning

confidence: 99%