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Literature summary for 1.16.3.1 extracted from

  • De Domenico, I.; Ward, D.M.; di Patti, M.C.; Jeong, S.Y.; David, S.; Musci, G.; Kaplan, J.
    Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin (2007), EMBO J., 26, 2823-2831.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine the requirement for a ferroxidase to maintain iron transport activity may explain brain iron overload in patients with aceruloplasminemia Mus musculus

Cloned(Commentary)

Cloned (Comment) Organism
expressed in C6 glioma cells Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information 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 Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
Bathocuproine disulfonate 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 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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