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Copper chaperone

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https://www.readbyqxmd.com/read/29121854/monitoring-interactions-inside-cells-by-advanced-spectroscopies-overview-of-copper-transporters-and-cisplatin
#1
Alessia Lasorsa, Giovanni Natile, Antonio Rosato, Francesco Tadini-Buoninsegni, Fabio Arnesano
BACKGROUND: Resistance, either at the onset of the treatment or developed after an initial positive response, is a major limitation of antitumor therapy. In the case of platinum-based drugs, copper transporters have been found to interfere with drug trafficking by facilitating the import or favoring the platinum export and inactivation. METHODS: The use of powerful spectroscopic, spectrometric and computational methods have allowed a deep structural insight into the mode of interaction of platinum drugs with the metal-binding domains of the transporter proteins...
November 10, 2017: Current Medicinal Chemistry
https://www.readbyqxmd.com/read/29101230/glutathione-limits-aquacopper-i-to-sub-femtomolar-concentrations-through-cooperative-assembly-of-a-tetranuclear-cluster
#2
M Thomas Morgan, Lily Anh H Nguyen, Haylie L Hancock, Christoph J Fahrni
The tripeptide glutathione (GSH) is a crucial intracellular reductant and radical scavenger, but may also coordinate the soft Cu(I) cation and thereby yield pro-oxidant species. The GSH-Cu(I) interaction is thus a key consideration for both redox and copper homeostasis in cells. However, even after nearly four decades of investigation, the nature and stability of the GSH-Cu complexes formed under biologically relevant conditions remain controversial. Here, we revealed the unexpected predominance of a tetranuclear [Cu4(GS)6] cluster that is sufficiently stable to limit the effective free aquocopper(I) concentration to the subfemtomolar regime...
November 3, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29062896/copper-chaperone-cupa-and-zinc-control-copy-regulation-of-the-pneumococcal-cop-operon
#3
Miranda J Neubert, Elizabeth A Dahlmann, Andrew Ambrose, Michael D L Johnson
Any metal in excess can be toxic; therefore, metal homeostasis is critical to bacterial survival. Bacteria have developed specialized metal import and export systems for this purpose. For broadly toxic metals such as copper, bacteria have evolved only export systems. The copper export system (cop operon) usually consists of the operon repressor, the copper chaperone, and the copper exporter. In Streptococcus pneumoniae, the causative agent of pneumonia, otitis media, sepsis, and meningitis, little is known about operon regulation...
September 2017: MSphere
https://www.readbyqxmd.com/read/28965584/identification-of-eight-copper-cu-uptake-related-genes-from-yellow-catfish-pelteobagrus-fulvidraco-and-their-tissue-expression-and-transcriptional-responses-to-dietborne-cu-exposure
#4
Jie Cheng, Zhi Luo, Guang-Hui Chen, Chuan-Chuan Wei, Mei-Qin Zhuo
The present working hypothesis is that absorption of dietary Cu is related to mRNA expressions of genes involved in Cu uptake and transport of the intestine in fish. To this end, the full-length cDNA sequences of eight Cu uptake related genes, including two isoforms of copper transporter genes (ctr1 and ctr2), three copper chaperone genes (atox1, ccs and cox17), two Cu-ATPase genes (atp7a and atp7b) and divalent metal ion transporter 1 (dmt1), were cloned and characterized in yellow catfish P. fulvidraco, respectively...
December 2017: Journal of Trace Elements in Medicine and Biology
https://www.readbyqxmd.com/read/28959342/enhancement-of-solubility-and-specific-activity-of-a-cu-zn-superoxide-dismutase-by-co-expression-with-a-copper-chaperone-in-escherichia-coli
#5
Warawan Eiamphungporn, Sakda Yainoy, Virapong Prachayasittikul
BACKGROUND: Human Cu/Zn superoxide dismutase (hSOD1) is an antioxidant enzyme with potential as a therapeutic agent. However, heterologous expression of hSOD1 has remained an issue due to Cu(2+) insufficiency at protein active site, leading to low solubility and enzymatic activity. OBJECTIVES: The effect of co-expressed human copper chaperone (hCCS) to enhance the solubility and enzymatic activity of hSOD1 in E. coli was investigated in the presence and absence of Cu(2+)...
December 2016: Iranian journal of biotechnology
https://www.readbyqxmd.com/read/28943953/six-low-penetrance-snps-for-the-estimation-of-breast-cancer-heritability-a-family-based-study-in-caucasian-italian-patients
#6
Simona De Summa, Francesca Graziano, Brunella Pilato, Rosamaria Pinto, Katia Danza, Rosanna Lacalamita, Simona Serratì, Domenico Sambiasi, Mario Grassi, Stefania Tommasi
Breast cancer is a malignancy with a strong heritable component. Genetic counseling has been principally focused on families carrying high-penetrance breast cancer 1/2, early onset genes. Current modeling suggests that the majority of the unexplained fraction of familial risk is likely to be explained by a polygenic model. The aim of the present study was to estimate the heritability (h(2)) of breast cancer susceptibility through the analysis of 6 single nucleotide polymorphisms (SNPs), nuclear mitotic apparatus protein 1, cyclin D1, cytochrome C oxidase copper chaperone, fibroblast growth factor receptor 2, TOX high mobility group box family member 3 and solute carrier family 4 member 7...
October 2017: Oncology Letters
https://www.readbyqxmd.com/read/28925527/one-gene-two-proteins-coordinated-production-of-a-copper-chaperone-by-differential-transcript-formation-and%C3%A2-translational-frameshifting-in-escherichia-coli
#7
Steffen L Drees, Birgit Klinkert, Stefan Helling, Dominik F Beyer, Katrin Marcus, Franz Narberhaus, Mathias Lübben
Programmed ribosomal frameshifting (PRF) is a translational anomaly causing the ribosome to shift into an alternative reading frame. PRFs are common in viral genomes, using a single nucleotide sequence to code for two proteins in overlapping frames. In bacteria and eukaryota, PRFs are less frequent. We report on a PRF in the copper detoxification system of Escherichia coli where a metallochaperone is generated out of the first 69 amino acids and a C-terminal out-of-frame glycine of the gene copA. copA besides codes for the P1B -ATPase CopA, a membrane-integral protein and principal interaction target of the chaperone...
September 19, 2017: Molecular Microbiology
https://www.readbyqxmd.com/read/28900031/the-metal-chaperone-atox1-regulates-the-activity-of-the-human-copper-transporter-atp7b-by-modulating-domain-dynamics
#8
Corey H Yu, Nan Yang, Jameson Bothe, Marco Tonelli, Sergiy Nokhrin, Natalia V Dolgova, Lelita Braiterman, Svetlana Lutsenko, Oleg Y Dmitriev
The human transporter ATP7B delivers copper to the biosynthetic pathways and maintains copper homeostasis in the liver. Mutations in ATP7B cause the potentially fatal hepatoneurological disorder Wilson disease. The activity and intracellular localization of ATP7B are regulated by copper, but the molecular mechanism of this regulation is largely unknown. We show that the copper chaperone Atox1, which delivers copper to ATP7B, and the group of the first three metal-binding domains (MBD1-3) are central to the activity regulation of ATP7B...
November 3, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28898759/cuprous-oxide-nanoparticles-trigger-er-stress-induced-apoptosis-by-regulating-copper-trafficking-and-overcoming-resistance-to-sunitinib-therapy-in-renal-cancer
#9
Qiwei Yang, Ye Wang, Qing Yang, Yi Gao, Xiaopeng Duan, Qingcheng Fu, Chuanmin Chu, Xiuwu Pan, Xingang Cui, Yinghao Sun
While the current standard first-line treatment for advanced renal cell carcinoma (RCC) is sunitinib, patients inevitably develop resistance to this drug. However, the rapid development of nanotechnology has provided emerging techniques for the treatment of advanced tumours, including RCC. In our previous research, cuprous oxide nanoparticles (CONPs) showed ideal anti-tumour effects and low systemic toxicity. While many inorganic nanomedicines, including CONPs, have similar pharmacological effects, their detailed mechanisms remain unknown...
November 2017: Biomaterials
https://www.readbyqxmd.com/read/28820536/atp7a-and-atp7b-regulate-copper-homeostasis-in-developing-male-germ-cells-in-mice
#10
Mateusz Ogórek, Małgorzata Lenartowicz, Rafał Starzyński, Aneta Jończy, Robert Staroń, Andrzej Doniec, Wojciech Krzeptowski, Aleksandra Bednarz, Olga Pierzchała, Paweł Lipiński, Zenon Rajfur, Zbigniew Baster, Patrycja Gibas-Tybur, Paweł Grzmil
The maintenance of copper homeostasis is critical for all cells. As learned from mice with disturbed copper metabolism, this trace element is also important for spermatogenesis. The experiments conducted in yeasts have demonstrated that appropriate copper level must be preserved to enable meiosis progression; however, increased copper level is toxic for cells. This study aims to analyze the expression profile of Atp7a and Atp7b and other genes encoding copper-related proteins during spermatogenesis in mice...
September 20, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28780408/an-essential-role-of-n-terminal-domain-of-copper-chaperone-in-the-enzymatic-activation-of-cu-zn-superoxide-dismutase
#11
Mami Fukuoka, Eiichi Tokuda, Kenta Nakagome, Zhiliang Wu, Isao Nagano, Yoshiaki Furukawa
Cu/Zn-superoxide dismutase (SOD1) is an enzyme that disproportionates superoxide anion into hydrogen peroxide and molecular oxygen. The enzymatic activity of SOD1 requires the binding of copper and zinc ions and also the formation of a conserved intramolecular disulfide bond. In a eukaryotic cell, a copper chaperone for SOD1 (CCS) has been known to supply a copper ion and also introduce the disulfide bond into SOD1; however, a mechanism controlling the CCS-dependent activation of SOD1 remains obscure. Here, we characterized CCS isolated from a human liver fluke, Clonorchis sinensis, and found that an N-terminal domain of CCS was essential in supplying a copper ion in SOD1...
July 31, 2017: Journal of Inorganic Biochemistry
https://www.readbyqxmd.com/read/28760827/copper-homeostasis-networks-in-the-bacterium-pseudomonas-aeruginosa
#12
Julia Quintana, Lorena Novoa-Aponte, José M Argüello
Bacterial copper (Cu(+)) homeostasis enables both precise metallation of diverse cuproproteins and control of variable metal levels. To this end, protein networks mobilize Cu(+) to cellular targets with remarkable specificity. However, the understanding of these processes is rather fragmented. Here, we use genome-wide transcriptomic analysis by RNA-Seq to characterize the response of Pseudomonas aeruginosa to external 0.5 mm CuSO4, a condition that did not generate pleiotropic effects. Pre-steady-state (5-min) and steady-state (2-h) Cu(+) fluxes resulted in distinct transcriptome landscapes...
September 22, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28711491/copper-chaperone-atox1-regulates-pluripotency-factor-oct4-in-preimplantation-mouse-embryos
#13
Emanuele Celauro, Amisa Mukaj, Juan Carlos Fierro-González, Pernilla Wittung-Stafshede
Despite of the importance of copper (Cu) during pregnancy, the roles of Cu-binding proteins during early embryonic development are unknown. The Cu chaperone ATOX1 was recently suggested to have additional functions related to transcription and cancer. When we analyzed single-cell RNA transcript data from early mouse embryos, Atox1 transcript levels increased dramatically at the 8-cell stage and, at 16- and 32-cell embryo stages, matched those of Oct4 which expresses a transcription factor essential for pluripotency in the inner cell mass...
September 9, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28689066/roles-of-a-mitochondrial-accsco2-gene-from-apis-cerana-cerana-in-oxidative-stress-responses
#14
Haihong Jia, Manli Ma, Na Zhai, Zhenguo Liu, Hongfang Wang, Xingqi Guo, Baohua Xu
In eukaryotes, cytochrome c oxidase (COX) is a multimeric protein complex that is the last enzyme in the respiratory electron transport chain of mitochondria. Syntheses of cytochrome c oxidase (SCO) proteins are copper-donor chaperones involved in metalation of the CuA redox center of COX. However, its other precise actions are not yet understood. Here, we report the characterization of AccSCO2 from Apis cerana cerana (Acc). Our data showed that AccSCO2 expression was induced by cold (4°C), CdCl2, HgCl2, ultraviolet (UV) light, and H2O2 and was inhibited by different pesticide treatments...
July 2, 2017: Journal of Inorganic Biochemistry
https://www.readbyqxmd.com/read/28686251/oxygen-dependent-activation-of-cu-zn-superoxide-dismutase-1
#15
REVIEW
Morgan M Fetherolf, Stefanie D Boyd, Duane D Winkler, Dennis R Winge
Copper zinc superoxide dismutase (Sod1) is a critical enzyme in limiting reactive oxygen species in both the cytosol and the mitochondrial intermembrane space. Sod1 dismutes superoxide anions to hydrogen peroxide and oxygen. The catalytic reaction is dependent on an active site copper ion and a disulfide bonded conformation. The activation of Sod1 is mediated by its chaperone Ccs1. The mechanism of Ccs1-mediated Sod1 activation involves both insertion of the catalytic copper ion and mediating disulfide bond formation...
August 16, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28685789/orchestration-of-dynamic-copper-navigation-new-and-missing-pieces
#16
REVIEW
Helena Öhrvik, Jan Aaseth, Nina Horn
A general principle in all cells in the body is that an essential metal - here copper - is taken up at the plasma membrane, directed through cellular compartments for use in specific enzymes and pathways, stored in specific scavenging molecules if in surplus, and finally expelled from the cells. Here we attempt to provide a critical view on key concepts involved in copper transfer across membranes and through compartments in the human body. The focus of this review is on the influence of bioinorganic and thermodynamic rules on the flow in cellular copper networks...
September 20, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28653724/probing-functional-roles-of-wilson-disease-protein-atp7b-copper-binding-domains-in-yeast
#17
Kumaravel Ponnandai Shanmugavel, Dina Petranovic, Pernilla Wittung-Stafshede
After Ctr1-mediated uptake into human cells, copper (Cu) ions are transported by the cytoplasmic Cu chaperone Atox1 to the Wilson disease protein (ATP7B) in the Golgi network. Cu transfer occurs via direct protein-protein interactions and leads to incorporation of Cu into Cu-dependent enzymes. ATP7B is a large multi-domain membrane-spanning protein which, in contrast to homologs, has six cytoplasmic metal-binding domains (MBDs). The reason for multiple MBDs is proposed to be indirect modulation of activity but mechanistic studies of full-length ATP7B are limited...
July 19, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28549213/binding-of-copper-and-cisplatin-to-atox1-is-mediated-by-glutathione-through-the-formation-of-metal-sulfur-clusters
#18
Natalia V Dolgova, Corey Yu, John P Cvitkovic, Miroslav Hodak, Kurt H Nienaber, Kelly L Summers, Julien J H Cotelesage, Jerzy Bernholc, George A Kaminski, Ingrid J Pickering, Graham N George, Oleg Y Dmitriev
Copper is an essential nutrient required for many biological processes involved in primary metabolism, but free copper is toxic due to its ability to catalyze formation of free radicals. To prevent toxic effects, in the cell copper is bound to proteins and low molecular weight compounds, such as glutathione, at all times. The widely used chemotherapy agent cisplatin is known to bind to copper-transporting proteins, including copper chaperone Atox1. Cisplatin interactions with Atox1 and other copper transporters are linked to cancer resistance to platinum-based chemotherapy...
June 20, 2017: Biochemistry
https://www.readbyqxmd.com/read/28543811/the-structural-flexibility-of-the-human-copper-chaperone-atox1-insights-from-combined-pulsed-epr-studies-and-computations
#19
Ariel R Levy, Meital Turgeman, Lada Gevorkyan-Aiapetov, Sharon Ruthstein
Metallochaperones are responsible for shuttling metal ions to target proteins. Thus, a metallochaperone's structure must be sufficiently flexible both to hold onto its ion while traversing the cytoplasm and to transfer the ion to or from a partner protein. Here, we sought to shed light on the structure of Atox1, a metallochaperone involved in the human copper regulation system. Atox1 shuttles copper ions from the main copper transporter, Ctr1, to the ATP7b transporter in the Golgi apparatus. Conventional biophysical tools such as X-ray or NMR cannot always target the various conformational states of metallochaperones, owing to a requirement for crystallography or low sensitivity and resolution...
August 2017: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/28533431/copper-zinc-superoxide-dismutase-is-activated-through-a-sulfenic-acid-intermediate-at-a-copper-ion-entry-site
#20
Morgan M Fetherolf, Stefanie D Boyd, Alexander B Taylor, Hee Jong Kim, James A Wohlschlegel, Ninian J Blackburn, P John Hart, Dennis R Winge, Duane D Winkler
Metallochaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering copper and facilitating the oxidation of the Sod1 intramolecular disulfide bond. Here, we present structural, spectroscopic, and cell-based data supporting a novel copper-induced mechanism for Sod1 activation. Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on immature Sod1...
July 21, 2017: Journal of Biological Chemistry
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