血浆铜蓝蛋白

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血浆铜蓝蛋白（英语：Ceruloplasmin）又称铜蓝血浆蛋白、铜蓝蛋白，由肝脏细胞制造，重约151千道尔顿(kDa)，包含六个铜离子。

血浆铜蓝蛋白(ferroxidase)
PDB rendering based on 1kcw.
有效结构 PDB 直系同源检索：PDBe, RCSB PDB查询代码列表 1KCW, 2J5W, 4EJX, 4ENZ
标识
代号	CP; CP-2
扩展标识	遗传学：117700 鼠基因：88476 同源基因：75 GeneCards: CP Gene
EC编号	1.16.3.1
基因本体论描述 分子功能 · ferroxidase activity · copper ion binding · chaperone binding 细胞成分 · extracellular region · extracellular space 生物过程 · copper ion transport · cellular iron ion homeostasis · transmembrane transport Sources: Amigo / QuickGO
RNA表达模式
更多表达数据
直系同源体
物种	人类	小鼠
Entrez	1356	12870
Ensembl	ENSG00000047457	ENSMUSG00000003617
UniProt	P00450	Q61147
mRNA序列	NM_000096	NM_001042611
蛋白序列	NP_000087	NP_001036076
基因位置	Chr 3: 148.88 – 148.94 Mb	Chr 3: 19.96 – 20.01 Mb
PubMed查询	[1]	[2]
查 论 编

概要

在血液中，血浆铜蓝蛋白携带了90%的铜离子，另外10%由白蛋白携带。血浆铜蓝蛋白的主要作用是进行依赖铜离子的氧化反应，反应时将二价铜离子还原成一价，而把铁离子由二价氧化成三价，成为可以与运铁蛋白结合的型态。

因为血浆铜蓝蛋白是由肝脏制造，所以当有肝脏疾病时其含量就会下降。或是因为基因缺陷而无法制造，如肝豆状核变性（威尔森氏症）、原血浆铜蓝蛋白缺乏症（英语：Aceruloplasminemia）等，多数（80～95%）肝豆状核变性患者血浆铜蓝蛋白呈现下降。在怀孕、淋巴瘤、慢性发炎、类风湿性关节炎的情况下，血浆铜蓝蛋白在血液中的含量则会上升。

延伸阅读

• 人类铁代谢

注释

参考文献

• Gropper, Smith, Groff. Advanced Nutrition And Human Metabolism 5th ed. 引文格式1维护：冗余文本 (link)

延伸阅读

• Hellman NE, Gitlin JD. Ceruloplasmin metabolism and function. Annual Review of Nutrition. 2002, 22: 439–58. PMID 12055353. doi:10.1146/annurev.nutr.22.012502.114457.
• Mazumder B, Seshadri V, Fox PL. Translational control by the 3'-UTR: the ends specify the means. Trends in Biochemical Sciences. Feb 2003, 28 (2): 91–8. PMID 12575997. doi:10.1016/S0968-0004(03)00002-1.
• Giurgea N, Constantinescu MI, Stanciu R, Suciu S, Muresan A. Ceruloplasmin - acute-phase reactant or endogenous antioxidant? The case of cardiovascular disease. Medical Science Monitor. Feb 2005, 11 (2): RA48–51. PMID 15668644.
• Kingston IB, Kingston BL, Putnam FW. Chemical evidence that proteolytic cleavage causes the heterogeneity present in human ceruloplasmin preparations. Proceedings of the National Academy of Sciences of the United States of America. Dec 1977, 74 (12): 5377–81. PMC 431726 . PMID 146197. doi:10.1073/pnas.74.12.5377.
• Polosatov MV, Klimov PK, Masevich CG, Samartsev MA, Wünsch E. Interaction of synthetic human big gastrin with blood proteins of man and animals. Acta Hepato-Gastroenterologica. Apr 1979, 26 (2): 154–9. PMID 463490.
• Schilsky ML, Stockert RJ, Pollard JW. Caeruloplasmin biosynthesis by the human uterus. The Biochemical Journal. Dec 1992, 288 (2): 657–61. PMC 1132061 . PMID 1463466. doi:10.1042/bj2880657.
• Walker FJ, Fay PJ. Characterization of an interaction between protein C and ceruloplasmin. The Journal of Biological Chemistry. Feb 1990, 265 (4): 1834–6. PMID 2105310.
• Fleming RE, Gitlin JD. Primary structure of rat ceruloplasmin and analysis of tissue-specific gene expression during development. The Journal of Biological Chemistry. May 1990, 265 (13): 7701–7. PMID 2332446.
• Yang FM, Friedrichs WE, Cupples RL, Bonifacio MJ, Sanford JA, Horton WA, Bowman BH. Human ceruloplasmin. Tissue-specific expression of transcripts produced by alternative splicing. The Journal of Biological Chemistry. Jun 1990, 265 (18): 10780–5. PMID 2355023.
• Yang F, Naylor SL, Lum JB, Cutshaw S, McCombs JL, Naberhaus KH, McGill JR, Adrian GS, Moore CM, Barnett DR. Characterization, mapping, and expression of the human ceruloplasmin gene. Proceedings of the National Academy of Sciences of the United States of America. May 1986, 83 (10): 3257–61. PMC 323492 . PMID 3486416. doi:10.1073/pnas.83.10.3257.
• Mercer JF, Grimes A. Isolation of a human ceruloplasmin cDNA clone that includes the N-terminal leader sequence. FEBS Letters. Jul 1986, 203 (2): 185–90. PMID 3755405. doi:10.1016/0014-5793(86)80739-6.
• Rask L, Valtersson C, Anundi H, Kvist S, Eriksson U, Dallner G, Peterson PA. Subcellular localization in normal and vitamin A-deficient rat liver of vitamin A serum transport proteins, albumin, ceruloplasmin and class I major histocompatibility antigens. Experimental Cell Research. Jan 1983, 143 (1): 91–102. PMID 6337857. doi:10.1016/0014-4827(83)90112-X.
• Kressner MS, Stockert RJ, Morell AG, Sternlieb I. Origins of biliary copper. Hepatology. 1984, 4 (5): 867–70. PMID 6479854. doi:10.1002/hep.1840040512.
• Takahashi N, Bauman RA, Ortel TL, Dwulet FE, Wang CC, Putnam FW. Internal triplication in the structure of human ceruloplasmin. Proceedings of the National Academy of Sciences of the United States of America. Jan 1983, 80 (1): 115–9. PMC 393320 . PMID 6571985. doi:10.1073/pnas.80.1.115.
• Dwulet FE, Putnam FW. Complete amino acid sequence of a 50,000-dalton fragment of human ceruloplasmin. Proceedings of the National Academy of Sciences of the United States of America. Feb 1981, 78 (2): 790–4. PMC 319888 . PMID 6940148. doi:10.1073/pnas.78.2.790.
• Kingston IB, Kingston BL, Putnam FW. Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides. The Journal of Biological Chemistry. Apr 1980, 255 (7): 2878–85. PMID 6987229.

外部链接

• GeneReviews/NCBI/NIH/UW entry on Aceruloplasminemia （页面存档备份，存于互联网档案馆）
• OMIM entries on Aceruloplasminemia （页面存档备份，存于互联网档案馆）