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维基百科

血漿銅藍蛋白

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英语Aceruloplasminemia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。

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
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]

多数(80~95%)肝豆狀核變性患者血漿銅藍蛋白下降。

延伸閱讀

註釋

參考文獻

  • Gropper, Smith, Groff. Advanced Nutrition And Human Metabolism 5th ed. 

延伸閱讀

  • 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. 

外部連結

  • 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

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, 包含六個銅離子, 在血液中, 攜帶了90, 的銅離子, 另外10, 由白蛋白攜帶, 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, 原缺乏症, 英语, aceruloplasminemia, 在懷孕, 淋巴. 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 英语 Aceruloplasminemia 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 血浆铜蓝蛋白 ferroxidase PDB rendering based on 1kcw 有效结构PDB 直系同源检索 PDBe RCSBPDB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 GeneEC編號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 transportSources Amigo QuickGORNA表达模式更多表达数据直系同源体物种人类小鼠Entrez135612870EnsemblENSG00000047457ENSMUSG00000003617UniProtP00450Q61147mRNA序列NM 000096NM 001042611蛋白序列NP 000087NP 001036076基因位置Chr 3 148 88 148 94 MbChr 3 19 96 20 01 MbPubMed查询 1 2 查论编多数 80 95 肝豆狀核變性患者血漿銅藍蛋白下降 目录 1 延伸閱讀 2 註釋 3 參考文獻 4 延伸閱讀 5 外部連結延伸閱讀 编辑人类铁代谢註釋 编辑參考文獻 编辑Gropper Smith Groff Advanced Nutrition And Human Metabolism 5th ed 引文格式1维护 冗余文本 link 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 Wunsch 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 外部連結 编辑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 分子与细胞生物学主题 取自 https zh wikipedia org w index php title 血漿銅藍蛋白 amp oldid 72794266, 维基百科,wiki,书籍,书籍,图书馆,

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