Ceruloplasmin

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Ceruloplasmin (ferroxidase)
PDB rendering based on 1kcw.
Identifiers
Symbol(s) CP; CP-2
External IDs OMIM: 117700 MGI: 88476 Homologene: 75
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 1356 12870
Ensembl ENSG00000047457 ENSMUSG00000003617
Uniprot P00450 Q2F3J4
Refseq NM_000096 (mRNA)
NP_000087 (protein) 		NM_001042611 (mRNA)
NP_001036076 (protein)
Location Chr 3: 150.37 - 150.42 Mb Chr 3: 20.15 - 20.2 Mb
Pubmed search [1] [2]

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Ceruloplasmin (or caeruloplasmin) is officially known as ferroxidase or iron(II):oxygen oxidoreductase.

Function

It is an enzyme (EC 1.16.3.1) synthesized in the liver containing 6 atoms of copper in its structure. Ceruloplasmin carries 90% of the copper in our plasma. The other 10% is carried by albumin, albumin may be confused at times to have a greater importance as a copper carrier because it binds copper less tightly than ceruloplasmin. Ceruloplasmin exhibits a copper-dependent oxidase activity, which is associated with possible oxidation of Fe2+ (ferrous iron) into Fe3+ (ferric iron), therefore assisting in its transport in the plasma in association with transferrin, which can only carry iron in the ferric state.

Pathology

Like any other plasma protein, levels drop in patients with hepatic disease due to reduced synthesizing capabilities.

Mutations in the ceruloplasmin gene can lead to the rare genetic human disease aceruloplasminemia, characterized by iron overload in the brain, liver, pancreas, and retina.

Interpretation

Decreased levels

Lower-than-normal ceruloplasmin levels may indicate:

Elevated levels

Greater-than-normal ceruloplasmin levels may indicate:

References

Further reading

  • Gitlin JD (1998). "Aceruloplasminemia.". Pediatr. Res. 44 (3): 271-6. doi:10.1203/00006450-199809000-00001. PMID 9727700.
  • Hellman NE, Gitlin JD (2002). "Ceruloplasmin metabolism and function.". Annu. Rev. Nutr. 22: 439-58. doi:10.1146/annurev.nutr.22.012502.114457. PMID 12055353.
  • Mazumder B, Seshadri V, Fox PL (2003). "Translational control by the 3'-UTR: the ends specify the means.". Trends Biochem. Sci. 28 (2): 91-8. doi:10.1016/S0968-0004(03)00002-1. PMID 12575997.
  • Giurgea N, Constantinescu MI, Stanciu R, et al. (2005). "Ceruloplasmin - acute-phase reactant or endogenous antioxidant? The case of cardiovascular disease.". Med. Sci. Monit. 11 (2): RA48-51. PMID 15668644.
  • Kingston IB, Kingston BL, Putnam FW (1978). "Chemical evidence that proteolytic cleavage causes the heterogeneity present in human ceruloplasmin preparations.". Proc. Natl. Acad. Sci. U.S.A. 74 (12): 5377-81. PMID 146197.
  • Polosatov MV, Klimov PK, Masevich CG, et al. (1979). "Interaction of synthetic human big gastrin with blood proteins of man and animals.". Acta hepato-gastroenterologica 26 (2): 154-9. PMID 463490.
  • Schilsky ML, Stockert RJ, Pollard JW (1993). "Caeruloplasmin biosynthesis by the human uterus.". Biochem. J. 288 ( Pt 2): 657-61. PMID 1463466.
  • Walker FJ, Fay PJ (1990). "Characterization of an interaction between protein C and ceruloplasmin.". J. Biol. Chem. 265 (4): 1834-6. PMID 2105310.
  • Fleming RE, Gitlin JD (1990). "Primary structure of rat ceruloplasmin and analysis of tissue-specific gene expression during development.". J. Biol. Chem. 265 (13): 7701-7. PMID 2332446.
  • Yang FM, Friedrichs WE, Cupples RL, et al. (1990). "Human ceruloplasmin. Tissue-specific expression of transcripts produced by alternative splicing.". J. Biol. Chem. 265 (18): 10780-5. PMID 2355023.
  • Koschinsky ML, Funk WD, van Oost BA, MacGillivray RT (1986). "Complete cDNA sequence of human preceruloplasmin.". Proc. Natl. Acad. Sci. U.S.A. 83 (14): 5086-90. doi:10.1073/pnas.83.14.5086. PMID 2873574.
  • Royle NJ, Irwin DM, Koschinsky ML, et al. (1987). "Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively.". Somat. Cell Mol. Genet. 13 (3): 285-92. doi:10.1007/BF01535211. PMID 3474786.
  • Yang F, Naylor SL, Lum JB, et al. (1986). "Characterization, mapping, and expression of the human ceruloplasmin gene.". Proc. Natl. Acad. Sci. U.S.A. 83 (10): 3257-61. doi:10.1073/pnas.83.10.3257. PMID 3486416.
  • Mercer JF, Grimes A (1986). "Isolation of a human ceruloplasmin cDNA clone that includes the N-terminal leader sequence.". FEBS Lett. 203 (2): 185-90. doi:10.1016/0014-5793(86)80739-6. PMID 3755405.
  • Rask L, Valtersson C, Anundi H, et al. (1983). "Subcellular localization in normal and vitamin A-deficient rat liver of vitamin A serum transport proteins, albumin, ceruloplasmin and class I major histocompatibility antigens.". Exp. Cell Res. 143 (1): 91-102. doi:10.1016/0014-4827(83)90112-X. PMID 6337857.
  • Kressner MS, Stockert RJ, Morell AG, Sternlieb I (1984). "Origins of biliary copper.". Hepatology 4 (5): 867-70. PMID 6479854.
  • Takahashi N, Bauman RA, Ortel TL, et al. (1983). "Internal triplication in the structure of human ceruloplasmin.". Proc. Natl. Acad. Sci. U.S.A. 80 (1): 115-9. doi:10.1073/pnas.80.1.115. PMID 6571985.
  • Takahashi N, Ortel TL, Putnam FW (1984). "Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule.". Proc. Natl. Acad. Sci. U.S.A. 81 (2): 390-4. doi:10.1073/pnas.81.2.390. PMID 6582496.
  • Dwulet FE, Putnam FW (1981). "Complete amino acid sequence of a 50,000-dalton fragment of human ceruloplasmin.". Proc. Natl. Acad. Sci. U.S.A. 78 (2): 790-4. doi:10.1073/pnas.78.2.790. PMID 6940148.
  • Kingston IB, Kingston BL, Putnam FW (1980). "Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides.". J. Biol. Chem. 255 (7): 2878-85. PMID 6987229.
v • d • e
Other oxidoreductases (EC 1.15-1.18)
1.15 - Acting on superoxide as acceptorSuperoxide dismutase
1.16 - Oxidizing metal ionsCeruloplasmin
1.17 - Acting on CH or CH2 groupsXanthine oxidase - Ribonucleotide reductase
1.18 - Acting on iron-sulfur proteins as donorsNitrogenase
v • d • e
Proteins: carrier proteins
HormoneFollistatin - Growth hormone binding protein - Insulin-like growth factor binding protein - Neurophysins (Neurophysin I, II)
Sex hormone binding globulin/Androgen binding protein - Transcortin - Thyroxine-binding globulin - Transthyretin
Metal/elementcalcium (Calcium-binding protein, Calmodulin-binding proteins) - copper (Ceruloplasmin) - iron (Iron-binding proteins, Transferrin receptor)
VitaminRetinol binding protein (4) - Transcobalamin
OtherAcyl carrier protein - Adaptor protein - Cholesterylester transfer protein - F-box protein - GTP-binding protein - Latent TGF-beta binding protein - Light-harvesting complex - Membrane transport protein
v • d • e
Globulins: alpha globulins
Alpha 1-antichymotrypsin - Alpha 1-antitrypsin - Alpha 2-macroglobulin - Alpha 2-antiplasmin - Antithrombin - Ceruloplasmin - Haptoglobin - Heparin cofactor II - Orosomucoid - Retinol binding protein - Transcortin
v • d • e
Acute phase proteins
Alpha 1-antichymotrypsin - Alpha 1-antitrypsin - Alpha 2-macroglobulin - C-reactive protein - Ceruloplasmin - C3 - Fibrin - Haptoglobin - Haemopexin - Orosomucoid - Serum albumin (negative) - Amyloid (P, A) - Transferrin
de:Caeruloplasmin

fr:Ferroxidase hu:Cöruloplazmin nl:Ceruloplasmine ja:セルロプラスミン

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Acknowledgement and Attribution Regarding Sources of Content

Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .

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