综述

铜伴侣蛋白CCS介导铜锌-超氧化物歧化酶激活的过程

展开
  • 1.四川农业大学动物营养研究所,雅安625014; 2.鱼类营养与安全生产四川省高校重点实验室,雅安625014; 3.动物抗病营养教育部重点实验室,雅安625014
唐玲(1986—),女,重庆垫江人,硕士研究生,从事水生动物营养研究。E-mail: mmtanglingyy@163.com

网络出版日期: 2011-08-15

基金资助

国家公益性行业(农业)科研专项(201003020)

Activation Process of Copper/Zinc Superoxide Dismutase Mediated by CCS

Expand
  • 1.Institute of Animal Nutrition, Sichuan Agricultural University, Ya’an 625014, China; 2. Fish Nutrition and Safety Production University Key Laboratary of Sichuan Province, Sichuan Agricultural University, Ya’an 625014, China; 3. Key Laboratory for Animal Disease-resistance Nutrition of China
    Ministry of Education, Sichuan Agricultural University, Ya’an 625014, China

Online published: 2011-08-15

摘要

CCS是细胞质中铜锌-超氧化物歧化酶(SOD1)的铜伴侣蛋白。本文综述了CCS介导SOD1激活的过程。CCS与SOD1通过蛋白-蛋白相互作用的方式将铜离子插入到不含铜离子的SOD1(apoSOD1)中,并促进二硫键的形成而激活SOD1。影响CCS活性的因素包括:X连锁的细胞凋亡抑制蛋白(XIAP)、神经接头蛋白X11α和铜代谢中含结构域Murr1蛋白(COMMD1)。

关键词: CCS; ; SOD1

本文引用格式

唐玲,冯琳,刘扬,胡凯,周小秋 . 铜伴侣蛋白CCS介导铜锌-超氧化物歧化酶激活的过程[J]. 动物营养学报, 2011 , 23(08) : 1259 -1263 . DOI: 10.3969/j.issn.1006-267x.2011.08.001

Abstract

CCS is the copper chaperone for copper/zinc-superoxide dismutase 1 (SOD1) in cytoplasm. This review described the activation process of cytosolic SOD1 mediated by CCS. With the protein-protein interaction of CCS and SOD1, CCS can directly insert the copper ion into apoSOD1 and promote the formation of intramolecular disulfide bond in SOD1, then finish the activation of SOD1. The activity of CCS can be affected by X-linked inhibitor of apoptosis protein (XIAP), neuronal adaptor protein X11α and copper metabolism (Murr1) domain containing 1 (COMMD1).[Chinese Journal of Animal Nutrition, 2011, 23(8):1259 -1263]

Key words: CCS; copper; SOD1

参考文献

[1]KIM B E, TRACY N, THIELE D J, et al. Mechanisms for copper acquisition, distribution and regulation[J]. Nature Chemical Biology, 2008, 4(3):176-185.

[2]VALENTINE S J, GRALLA E B. Delivering copper inside yeast and human cells[J]. Science, 1997, 278(5339):817-818.

[3]KLOMP L W, LIN S J, YUAN D, et al. Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis[J]. The Journal of Biological Chemistry, 1997, 272(14):9221-9226.

[4]GLERUM D M, SHTANKO A, TZAGOLOFF A. Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase[J]. The Journal of Biological Chemistry, 1996, 271(24):14504-14509.

[5]CULOTTA V C, KLOMP L W. The copper chaperone for superoxide dismutase[J]. The Journal of Biological Chemistry, 1997, 272(38):23469-23472.

[6]CASARENO R L, DARREL W, GITLIN J D, et al. The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase[J]. The Journal of Biological Chemistry, 1998, 273(37):23625-23628.

[7]SCHMIDT P J, RAE T D, PUFAHL R A, et al. Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase[J]. The Journal of Biological Chemistry, 1999, 274(34):23719-23725.

[8]SCHMIDT P J, KUNST C, CCLOTTA V C, et al. Copper activation of superoxide dismutase 1 (SOD1) in vivo[J]. The Journal of Biological Chemistry, 2000, 275(43):33771-33776.

[9]BROWN N M, TORRES A S, DOAN P E, et al. Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase[J]. Proceedings of the National Academy of Sciences, 2004, 101(15):5518-5523.

[10]FURUKAWA Y, TORRES A S, OHALLORAN T V, et al. Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS[J]. The EMBO Journal, 2004, 23(14):2872-2881.

[11]BRADY G F, GALBAN S, LIU X W , et al. Regulation of the copper chaperone CCS by XIAP-mediated ubiquitination[J]. Molecular and Cellular Biology, 2010, 30(8):1923-1936.

[12]FALCONI M, IOVINO M, DESIDERI A, et al. A model for the incorporation of metal from the copper chaperone CCS into Cu,Zn superoxide dismutase[J]. Structure, 1999, 7(8):903-908.

[14]LAMB A L, TORRES A S, O'HALLORAN T V, et al. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone[J]. Nature, 2001, 8(9):751-755.

[15]FURUKAWA Y, THOMASV O. Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis[J]. Antioxidants & Redox Signaling, 2006, 8(5):847-867.

[16]BARTNIKAS T B, GITLIN J D. Mechanisms of biosynthesis of mammalian copper/zinc superoxide dismutase[J]. The Journal of Biological Chemistry, 2003, 278(35):33602-33608

[17]RAE T D, SCHMIDT P J, PUFAHL R A, et al. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase[J]. Science, 1999, 284(805):805-808.

[18]AMY L C, BARTNIKAS T B, GITLIN J D, et al. Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase[J]. The Journal of Biological Chemistry, 2006, 281(19):13581-13587.

[19]BANCI L, BERTINI I, BAFFONI S C, et al. Affinity gradients drive copper to cellular destinations[J]. Nature, 2010, 10(465):1-4.

[20]ENDO T, FUJII T, SATO K, et al. A pivotal role of Zn-binding residues in the function of the copper chaperone for SOD1[J]. Biochemical and Biophysical Research Communications, 2000, 276(3):999-1004.

[21]HWANGA I K, EUMB W S, YOO K Y, et al. Copper chaperone for Cu,Zn-SOD supplement potentiates the Cu,Zn-SOD function of neuroprotective effects against ischemic neuronal damage in the gerbil hippocampus[J]. Free Radical Biology & Medicine, 2005, 39(3):392-402.

[22]TORRES A S, PETRI V, RAE T D, et al. Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase[J]. The Journal of Biological Chemistry, 2001, 276(42):38410-38416.

[23]KACHUR A V, KOCH C J, BIAGLOW J E. Mechanism of copper-catalyzed autoxidation of cysteine[J]. Free Radical Research, 1999, 31(1):23-34.

[24]BERTINATO J, LABBE M R. Copper modulates the degradation of copper chaperone for Cu,Zn superoxide dismutase by the 26 S proteosome[J]. The Journal of Biological Chemistry, 2003, 278(37):35071-35078.

[25]MCLOUGHLIN D M, STANDEN C L, LAU K F, et al. The neuronal adaptor protein X11α interacts with the copper chaperone for SOD1 and regulates SOD1 activity[J]. The Journal of Biological Chemistry, 2001, 276(12):9303-9307.

[26]WILLIANNE I M, WIJMENGA C, BERGER R, et al. Cu,Zn superoxide dismutase maturation and activity are regulated by COMMD1[J]. The Journal of Biological Chemistry, 2010, 285(37):28991-29000.
文章导航

/