Characterization, mapping, and expression of the human ceruloplasmin gene.

Abstract

Ceruloplasmin (CP) is a copper-binding protein in vertebrate plasma. It is the product of an intragenic triplication and is composed of three homologous domains. Oligonucleotide probes constructed according to published amino acid sequences were used to identify cDNA clones encoding human CP. Two clones, CP-1 and CP-2, differed from each other by the presence or absence, respectively, of a deduced sequence of four amino acids. The two clones provided 81% of the sequence encoding CP. Comparison of the nucleotides of the three domains of the CP coding sequence revealed internal domain homology with identity of sequences ranging from 50.1% to 56%. The nucleotide sequence of CP-2 cDNA was compared to that of a homologous human protein, clotting factor VIII, and was found to be 48% identical overall. The CP gene was mapped to human chromosome 3 by somatic-cellhybrid analysis and to 3q25 by in situ hybridization; however, sites of hybridization to DNA on other chromosomal sites suggested additional CP-like DNA sequences in the human genome. A DNA polymorphism was detected with CP cDNA after endonuclease digestion of human DNA by Pst I. CP mRNA was detected in human liver, macrophages, and lymphocytes by in situ histohybridization.

Ceruloplasmin expression by human peripheral blood lymphocytes: A new link between immunity and iron metabolism

“…The sequence of the amplified fragments was analyzed by DNA sequencing and compared to the nucleotide sequence for CP cDNA previously reported [31,37,38]. The identification of sCP and GPI-CP fragments was confirmed, showing that huPBL express the transcripts for sCP and GPI-CP ( Figs.…”

“…Human peripheral blood monocyte (huPBMn) cDNA samples were also prepared as positive controls for CD33 PCR assay. HepG2 cDNA sample was used as a positive control for specific amplification of sCP [31] and GPI-CP [36].…”

“…In particular, a membrane-bound glycosylphosphatidylinositol (GPI)-anchored form of CP (GPI-CP) localized at the surface of mammalian astrocytes [28], rat leptomeningeal cells [29], and Sertoli cells [30] was reported. However, despite the detection of CP mRNA in immune cells [31,32], the characterization of the specific molecular isoform (s) expressed by huPBL has never been attempted.…”

Exon 12 Ceruloplasmin Gene New Nonsense Mutation Causing Aceruloplasminemia in an Italian Patient

“…CP is expressed in the central nervous system as well as in visceral organs and it plays an important role in the brain iron transport and storage and it is essential for neuron survival in CNS [2].…”

Application of Acute Phase Proteins for Monitoring Inflammatory States in Cattle

“…Dooley et al (1981) were the first to characterized bovine Cp. It is the product of an intragenic triplication and is comprised of three homologous domains (Yang et al, 1986). In humans, Cp is a single polypeptide chain of 1,046 amino acids (Endo et al, 1982), whereas bovine Cp is comprised of 1,063 amino acids (Zimin et al, 2009).…”