血漿銅藍蛋白
| 血浆铜蓝蛋白(ferroxidase) | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
 PDB rendering based on 1kcw. | |||||||||||||
| |||||||||||||
| 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編號 | 1.16.3.1 | ||||||||||||
| |||||||||||||
| 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] | |||||||||||
血漿銅藍蛋白（英語：Ceruloplasmin）又称銅藍血漿蛋白、铜蓝蛋白，由肝臟細胞製造，重約151千道爾頓(kDa)，包含六個銅離子。在血液中，血漿銅藍蛋白攜帶了90%的銅離子，另外10%由白蛋白攜帶。血漿銅藍蛋白的主要作用是進行依賴銅離子的氧化反應，反應時將二價銅離子還原成一價，而把鐵離子由二價氧化成三價，成為可以與運鐵蛋白結合的型態。 因為血漿銅藍蛋白是由肝臟製造，所以當有肝臟疾病時其含量就會下降。或是因為基因缺陷而無法製造，如威爾森氏症、原血漿銅藍蛋白缺乏症等。在懷孕、淋巴瘤、慢性發炎、類風濕性關節炎的情況下血漿銅藍蛋白在血液中的含量則會上升。
多数（80～95%）肝豆狀核變性患者血漿銅藍蛋白下降。
延伸閱讀
[编辑]註釋
[编辑]參考文獻
[编辑]- Gropper, Smith, Groff. Advanced Nutrition And Human Metabolism 5th ed.
延伸閱讀
[编辑]- 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.
