ceruloplasmin

The molecular weight of human ceruloplasmin is reported to be 151kDa.

The α2 region is mostly haptoglobin, α2-macroglobulin, α2-antiplasmin and ceruloplasmin.

The disease is caused by mutations in the ceruloplasmin gene.

The liver also releases copper into the bloodstream that is not bound to ceruloplasmin.

Serum copper and ceruloplasmin concentrations were within normal limits.

In the bloodstream, copper is carried throughout the body by albumin, ceruloplasmin, and other proteins.

The majority of blood copper (or serum copper) is bound to ceruloplasmin.

Greater-than-normal ceruloplasmin levels may indicate or be noticed in:

If a family history of liver disease is present, serum copper and ceruloplasmin levels can rule out Wilson's disease.

Copper transport here involves the protein ceruloplasmin, which carries the majority of copper in blood.

Fortunately, copper deficiency can be confirmed by very low serum metal and ceruloplasmin concentrations in the blood.

This may be to furnish more copper for ceruloplasmin synthesis or to release free copper.

It is the main site for the synthesis of lipoproteins, ceruloplasmin, transferrin, complement, and glycoproteins.

Lower-than-normal ceruloplasmin levels may indicate the following:

Another iron transporting enzyme is ceruloplasmin.

Most of the copper (70 - 95%) excreted by the liver is incorporated into ceruloplasmin, the main copper carrier in blood.

Ceruloplasmin carries about 70% of the total copper in human plasma while albumin carries about 15%.

Low ceruloplasmin is also found in Menkes disease and aceruloplasminemia, which are related to, but much rarer than Wilson's disease.

Included here are also related binding proteins, like ferritin and transferrin for iron, and ceruloplasmin for copper.

Hephaestin presents homology with ceruloplasmin, a serum dehydrogenase protein involved in copper detoxification and storage.

Another protein, hephaestin, is noted for its homology to ceruloplasmin, and also participates in iron and probably copper metabolism.

Albumin may be confused at times to have a greater importance as a copper carrier because it binds copper less tightly than ceruloplasmin.

Copper is transported to extra-hepatic tissues by ceruloplasmin, albumin and amino acids, or excreted into the bile.

Autosomal recessive disorder characterized by low serum ceruloplasmin and increased hepatic copper content on liver biopsy.

Ashwell's goal as a researcher was to devise a labeling serum glycoproteins in order to study the role of ceruloplasmin in Wilson disease.