The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a.
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SYSTEMATIC NAME
IUBMB Comments
Fe(II):oxygen oxidoreductase
The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a.
incubation of C6 glioma cells with the copper chelator bathocuproine disulfonate prevents expression of ceruloplasmin on the cell surface and leads to a decrease in cellular ceruloplasmin. Incubation of cells with bathocuproine disulfonate also reduces the ability of cells to lower their ferritin levels
mouse embryonal carcinoma cell line, addition of enzyme to culture medium induces aggregation within 24 h, with half-maximal effect at 0.05 mM. No association with apoptosis, necrosis or changes in secretory function. aggregation is less pronounce in aging neurons, K+ channels seem not to be involved
transfection of C6 glioma cells with RNAi oligonucleotide pools specific for cell suface GPI-ceruloplasmin leads to decreased levels of GPI-ceruloplasmin but does not affect accumulation of ferritin, when cells are incubated with iron. In the absence of ceruloplasmin, the transporter protein ferroportin is rapidly internalized and degraded. Depeltion of extra-cellular Fe(II) can maintain cell surface ferroportin in the absence of ceruloplasmin