Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The blue copper protein caeruloplasmin is synthesized mainly by hepatocytes. An alternative transcript for caeruloplasmin produced in certain extrahepatic tissues, CP-1, contains an additional 12 nucleotides encoding 4 amino acids not present in the hepatic transcript, CP-2 [Yang, Friedrichs, Cupples, Bonifacio, S Sanford, Horton & Bowman (1990) J. Biol. Chem. 265, 10780-10785]. We have demonstrated transcription of caeruloplasmin mRNA by a well-differentiated human uterine epithelial adenocarcinoma cell line, Ishikawa, and by human uterine endometrium and purified endometrial glands. Identical CP-2 nucleotide sequences were obtained for partial caeruloplasmin transcripts from human liver and Ishikawa cells, indicating that CP-2 transcripts are produced by uterine epithelial lining cells. The synthesis of caeruloplasmin protein was demonstrated for Ishikawa cells and another uterine adenocarcinoma cell line, ECC1. Peptide-mapping analysis indicated that caeruloplasmin secreted by Ishikawa cells was structurally identical with the protein synthesized by the human hepatoblastoma cell line HepG2. The secretion of a 135,000-M(r) caeruloplasmin by Ishikawa and ECC1 cells, comparable with that of the human hepatoblastoma cell line, HepG2, indicated similar processing of uterine and hepatic caeruloplasmin. Incorporation of 67Cu into caeruloplasmin was demonstrated for Ishikawa and ECC1 cells, suggesting that the human uterus produces a bioactive form of caeruloplasmin and possesses the necessary metal transporters and intracellular machinery for copper incorporation into this protein.
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PMID:Caeruloplasmin biosynthesis by the human uterus. 146 66

Ceruloplasmin (CP) is a plasma glycoprotein that transports copper throughout the body. In previous studies (Yang, F., Naylor, S., Lum, J., Cutshaw, S., McCombs, J., Naberhaus, K., McGill, J., Adrian, G., Moore, C., Barnett, D., and Bowman, B. (1986) Proc. Natl. Acad. Sci. U. S. A. 83, 3277-3261), two CP cDNA clones, CP-1 and CP-2, from a human cDNA library, differed from each other by the presence or absence, respectively, of 12 nucleotide bases encoding a deduced sequence of Gly-Glu-Tyr-Pro near the carboxyl-terminal region of the ceruloplasmin molecule. Examination of genomic DNA demonstrates that the two CP mRNAs are produced from a single gene by alternative spliced patterns. The additional amino acids deduced in CP-1 are products of alternative splicing within an intron of the CP gene at a site 12 nucleotide bases 3' to the commonly used site of CP-2. The CP-1 mRNA transcript encoding four extra amino acids appeared as a minor species accompanying CP-2 mRNA in placenta and chondrocytes. CP-1 mRNA was the predominant CP transcript in a lymphoblastic leukemia cell line, CEM. The mRNA examined from other tissues contained only CP-2 mRNA transcripts. These findings predict that alternative RNA splicing may lead to the differential expression of CP genomic sequences and produce alternate isoforms from a single CP gene in specific tissues.
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PMID:Human ceruloplasmin. Tissue-specific expression of transcripts produced by alternative splicing. 235 23

We showed previously that ceruloplasmin associates with the H chain of rat liver ferritin during iron loading into ferritin such that the iron oxidized by ceruloplasmin was deposited into ferritin [S.-H. Juan et al. (1997) Arch. Biochem. Biophys. 341, 280-286]. Three synthetic decapeptides derived from domains 2, 4, and 6 of ceruloplasmin, referred to CP-2, CP-4, and CP-6, were utilized to identify a possible binding site on ceruloplasmin for ferritin. Two of the peptides, CP-4 and CP-6, were found to inhibit iron loading into the recombinant ferritin H chain homopolymer (rH-Ft) by ceruloplasmin. The extent of inhibition of iron loading into ferritin by ceruloplasmin by CP-6, but not CP-4, varied with pH, whereas the inhibitory effect remained constant in increasing concentrations of NaCl. The addition of rH-Ft quenched the fluorescence emission of CP-4 and CP-6, but not CP-2. The quenching of fluorescence was used to estimate dissociation constants for the peptides. Iron loading into ferritin in Hepes buffer was not affected in the presence of these peptides. In addition, synthetic peptides corresponding to the BC loop of ferritin H and L chains were utilized to localize an interaction site on ferritin for ceruloplasmin. The BC loop of H chain but not L chain of ferritin stimulated the ferroxidase activity of ceruloplasmin. Only the BC loop of ferritin H chain decreased the amount of iron loading into ferritin by ceruloplasmin.
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PMID:Studies on the interaction between ferritin and ceruloplasmin. 964 67