ceruloplasmin; ferroxidase (CP)
Jump to navigation
Jump to search
Function
- oxidizes Fe+2 to Fe+3 without releasing oxygen radicals
- essential for transferrin binding of iron
- binds copper (6-7 atoms per molecule)
- but not a transport protein for copper
- involved in iron transport across the cell membrane
4 Fe+2 + 4 H+ + O2 = 4 Fe+3 + 2 H2O
Cofactor: binds 6 copper ions per monomer
Structure
- glycoprotein
- belongs to the multicopper oxidase family
- contains 3 F5/8 type A domains
- contains 6 plastocyanin-like domains
Compartment
Expression
Pathology
- defects in CP are the cause of aceruloplasminemia
- ceruloplasmin levels are decreased in Wilson's disease
- copper cannot be incorporated into ceruloplasmin in liver due to a defect in copper transporting ATPase-2
Notes
- blue protein
More general terms
Additional terms
References
- ↑ Tietz Fundamentals of Clinical Chemistry 3rd ed, WB Saunders, 1987 pg 331
- ↑ Principles of Biochemistry 6th ed., White, Handler, Smith, Hill, & Lehman (eds.) McGraw-Hill, NY 1978, pg 408 (MW)
- ↑ UniProt http://www.uniprot.org/uniprot/P00450.html
- ↑ GeneReviews http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/CP
- ↑ Wikipedia; Note: ceruloplasmin entry http://en.wikipedia.org/wiki/ceruloplasmin