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Copper chaperone

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https://www.readbyqxmd.com/read/28549213/binding-of-copper-and-cisplatin-to-atox1-is-mediated-by-glutathione-through-the-formation-of-metal-sulfur-clusters
#1
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 9, 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
#2
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...
May 20, 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
#3
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
Metallo-chaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for Sod1 (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...
May 22, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28466911/stepwise-copper-i-binding-to-metallothionein-a-mixed-cooperative-and-non-cooperative-mechanism-for-all-20-copper-ions
#4
Judith S Scheller, Gordon W Irvine, Daisy L Wong, Andrea Hartwig, Martin J Stillman
Copper is a ubiquitous trace metal of vital importance in that it serves as a cofactor in many metalloenzymes. Excess copper becomes harmful if not sequestered appropriately in the cell. As a metal ion chaperone, metallothionein (MT) has been proposed as a key player in zinc and copper homeostasis within the cell. The underlying mechanisms by which MT sequesters and transfers copper ions, and subsequently achieves its proposed biological function remain unknown. Using a combination of electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD), and emission spectroscopy, we report that the Cu(i) to human apo-MT1a binding mechanism is highly pH-dependent...
May 24, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28433108/genetic-and-environmental-modifiers-of-wilson-disease
#5
Valentina Medici, Karl-Heinz Weiss
Wilson disease (WD) is characterized by remarkable variety in its phenotypic presentation. Patients with WD can present with hepatic, neurologic, and psychiatric symptoms combined in different and unpredictable ways. Importantly, no convincing phenotype-genotype correlation has ever been identified, opening the possibility that other genes, aside from ATPase copper-transporting beta (ATP7B), are involved in the pathogenesis of this condition. In addition, modifier genes, or genes that can affect the expression of other genes, may be involved...
2017: Handbook of Clinical Neurology
https://www.readbyqxmd.com/read/28428045/sco2-deficient-mice-develop-increased-adiposity-and-insulin-resistance
#6
Shauna Hill, Sathyaseelan S Deepa, Kavithalakshmi Sataranatarajan, Pavithra Premkumar, Daniel Pulliam, Yuhong Liu, Vanessa Y Soto, Kathleen E Fischer, Holly Van Remmen
Cytochrome c oxidase (COX) is an essential transmembrane protein complex (Complex IV) in the mitochondrial respiratory electron chain. Mutations in genes responsible for the assembly of COX are associated with Leigh syndrome, cardiomyopathy, spinal muscular atrophy and other fatal metabolic disorders in humans. Previous studies have shown that mice lacking the COX assembly protein Surf1 (Surf1(-/-) mice) paradoxically show a number of beneficial metabolic phenotypes including increased insulin sensitivity, upregulation of mitochondrial biogenesis, induction of stress response pathways and increased lifespan...
April 18, 2017: Molecular and Cellular Endocrinology
https://www.readbyqxmd.com/read/28294521/thiol-based-copper-handling-by-the-copper-chaperone-atox1
#7
REVIEW
Yuta Hatori, Sachiye Inouye, Reiko Akagi
Human antioxidant protein 1 (Atox1) plays a crucial role in cellular copper homeostasis. Atox1 captures cytosolic copper for subsequent transfer to copper pumps in trans Golgi network, thereby facilitating copper supply to various copper-dependent oxidereductases matured within the secretory vesicles. Atox1 and other copper chaperones handle cytosolic copper using Cys thiols which are ideal ligands for coordinating Cu(I). Recent studies demonstrated reversible oxidation of these Cys residues in copper chaperones, linking cellular redox state to copper homeostasis...
March 15, 2017: IUBMB Life
https://www.readbyqxmd.com/read/28217917/a-comprehensive-phylogenetic-analysis-of-copper-transporting-p1b-atpases-from-bacteria-of-the-rhizobiales-order-uncovers-multiplicity-diversity-and-novel-taxonomic-subtypes
#8
Ciro Cubillas, Fabiola Miranda-Sánchez, Antonio González-Sánchez, José Pedro Elizalde, Pablo Vinuesa, Susana Brom, Alejandro García-de Los Santos
The ubiquitous cytoplasmic membrane copper transporting P1B-1 and P1B-3 -type ATPases pump out Cu(+) and Cu(2+) , respectively, to prevent cytoplasmic accumulation and avoid toxicity. The presence of five copies of Cu-ATPases in the symbiotic nitrogen-fixing bacteria Sinorhizobium meliloti is remarkable; it is the largest number of Cu(+) -transporters in a bacterial genome reported to date. Since the prevalence of multiple Cu-ATPases in members of the Rhizobiales order is unknown, we performed an in silico analysis to understand the occurrence, diversity and evolution of Cu(+) -ATPases in members of the Rhizobiales order...
February 20, 2017: MicrobiologyOpen
https://www.readbyqxmd.com/read/28212901/the-dissociation-of-the-hsp60-pro-caspase-3-complex-by-bis-pyridyl-oxadiazole-copper-complex-cubipyoxa-leads-to-cell-death-in-nci-h292-cancer-cells
#9
Celeste Caruso Bavisotto, Dragana Nikolic, Antonella Marino Gammazza, Rosario Barone, Filippa Lo Cascio, Emanuele Mocciaro, Giovanni Zummo, Everly Conway de Macario, Alberto Jl Macario, Francesco Cappello, Valentina Giacalone, Andrea Pace, Giampaolo Barone, Antonio Palumbo Piccionello, Claudia Campanella
Cell survival and proliferation are central to carcinogenesis, involving various mechanisms among which those that impede apoptosis are important. In this, the role of the molecular chaperone Hsp60 is unclear since it has been reported that it can be both, pro- or anti-apoptotic. A solution to this riddle is crucial to the development of anti-cancer therapies targeting Hsp60. We addressed this question using a tumor cell line, NCI-H292, and [Cu(3,5-bis(2'-pyridyl)-1,2,4-oxadiazole)2(H2O)2](ClO4)2, CubipyOXA, a copper-containing compound with cytotoxic properties...
May 2017: Journal of Inorganic Biochemistry
https://www.readbyqxmd.com/read/28120938/s-acylation-of-sod1-ccs-and-a-stable-sod1-ccs-heterodimer-in-human-spinal-cords-from-als-and-non-als-subjects
#10
Sarah E Antinone, Ghanashyam D Ghadge, Lyle W Ostrow, Raymond P Roos, William N Green
Previously, we found that human Cu, Zn-superoxide dismutase (SOD1) is S-acylated (palmitoylated) in vitro and in amyotrophic lateral sclerosis (ALS) mouse models, and that S-acylation increased for ALS-causing SOD1 mutants relative to wild type. Here, we use the acyl resin-assisted capture (acyl-RAC) assay to demonstrate S-acylation of SOD1 in human post-mortem spinal cord homogenates from ALS and non-ALS subjects. Acyl-RAC further revealed that endogenous copper chaperone for SOD1 (CCS) is S-acylated in both human and mouse spinal cords, and in vitro in HEK293 cells...
January 25, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28107647/programmed-ribosomal-frameshifting-generates-a-copper-transporter-and-a-copper-chaperone-from-the-same-gene
#11
Sezen Meydan, Dorota Klepacki, Subbulakshmi Karthikeyan, Tõnu Margus, Paul Thomas, John E Jones, Yousuf Khan, Joseph Briggs, Jonathan D Dinman, Nora Vázquez-Laslop, Alexander S Mankin
Metal efflux pumps maintain ion homeostasis in the cell. The functions of the transporters are often supported by chaperone proteins, which scavenge the metal ions from the cytoplasm. Although the copper ion transporter CopA has been known in Escherichia coli, no gene for its chaperone had been identified. We show that the CopA chaperone is expressed in E. coli from the same gene that encodes the transporter. Some ribosomes translating copA undergo programmed frameshifting, terminate translation in the -1 frame, and generate the 70 aa-long polypeptide CopA(Z), which helps cells survive toxic copper concentrations...
January 19, 2017: Molecular Cell
https://www.readbyqxmd.com/read/28107645/a-cu-rious-ribosomal-profiling-pattern-leads-to-the-discovery-of-ribosomal-frameshifting-in-the-synthesis-of-a-copper-chaperone
#12
John F Atkins, Gary Loughran, Pavel V Baranov
In many bacteria, separate genes encode a copper binding chaperone and a copper efflux pump, but in some the chaperone encoding gene has been elusive. In this issue of Molecular Cell, Meydan et al. (2017) report that ribosomes translating the ORF that encodes the copper pump frequently frameshift and terminate to produce the copper chaperone.
January 19, 2017: Molecular Cell
https://www.readbyqxmd.com/read/28078344/kinetic-analysis-of-copper-transfer-from-a-chaperone-to-its-target-protein-mediated-by-complex-formation
#13
Kristine L Kay, Liang Zhou, Leonardo Tenori, Justin M Bradley, Chloe Singleton, Margaret A Kihlken, Simone Ciofi-Baffoni, Nick E Le Brun
Chaperone proteins that traffic copper around the cell minimise its toxicity by maintaining it in a tightly bound form. The transfer of copper from chaperones to target proteins is promoted by complex formation, but the kinetic characteristics of transfer have yet to be demonstrated for any chaperone-target protein pair. Here we report studies of copper transfer between the Atx1-type chaperone CopZ from Bacillus subtilis and the soluble domains of its cognate P-type ATPase transporter, CopAab. Transfer of copper from CopZ to CopAab was found to occur rapidly, with a rate constant at 25 °C of ∼267 s(-1), many orders of magnitude higher than that for Cu(i) dissociation from CopZ in the absence of CopAab...
January 12, 2017: Chemical Communications: Chem Comm
https://www.readbyqxmd.com/read/28072820/p-cymene-promotes-its-catabolism-through-the-p-cymene-and-the-p-cumate-pathways-activates-a-stress-response-and-reduces-the-biofilm-formation-in-burkholderia-xenovorans-lb400
#14
Loreine Agulló, María José Romero-Silva, Mirian Domenech, Michael Seeger
p-Cymene is an aromatic terpene that is present in diverse plant species. The aims of this study were to study the p-cymene metabolism in the model aromatic-degrading bacterium Burkholderia xenovorans LB400, and its response to p-cymene. The catabolic p-cymene (cym) and p-cumate (cmt) genes are clustered on the LB400 major chromosome. B. xenovorans LB400 was able to grow on p-cymene as well as on p-cumate as a sole carbon and energy sources. LB400 growth attained higher cell concentration at stationary phase on p-cumate than on p-cymene...
2017: PloS One
https://www.readbyqxmd.com/read/28027931/copper-chaperone-atox1-plays-role-in-breast-cancer-cell-migration
#15
Stéphanie Blockhuys, Pernilla Wittung-Stafshede
Copper (Cu) is an essential transition metal ion required as cofactor in many key enzymes. After cell uptake of Cu, the metal is transported by the cytoplasmic Cu chaperone Atox1 to P1B-type ATPases in the Golgi network for incorporation into Cu-dependent enzymes in the secretory path. Cu is vital for many steps of cancer progression and Atox1 was recently suggested to have additional functionality as a nuclear transcription factor. We here investigated the expression level, cellular localization and role in cell migration of Atox1 in an aggressive breast cancer cell line upon combining immunostaining, microscopy and a wound healing assay...
January 29, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27942658/defining-the-human-copper-proteome-and-analysis-of-its-expression-variation-in-cancers
#16
S Blockhuys, E Celauro, C Hildesjö, A Feizi, O Stål, J C Fierro-González, P Wittung-Stafshede
Copper (Cu) is essential for living organisms, and acts as a cofactor in many metabolic enzymes. To avoid the toxicity of free Cu, organisms have specific transport systems that 'chaperone' the metal to targets. Cancer progression is associated with increased cellular Cu concentrations, whereby proliferative immortality, angiogenesis and metastasis are cancer hallmarks with defined requirements for Cu. The aim of this study is to gather all known Cu-binding proteins and reveal their putative involvement in cancers using the available database resources of RNA transcript levels...
December 12, 2016: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/27938702/erythrocyte-copper-chaperone-for-superoxide-dismutase-and-superoxide-dismutase-as-biomarkers-for-hepatic-copper-concentrations-in-labrador-retrievers
#17
K Dirksen, Y S Roelen, M E van Wolferen, H S Kruitwagen, L C Penning, I A Burgener, B Spee, H Fieten
Hereditary hepatic copper accumulation in Labrador retrievers leads to hepatitis with fibrosis and eventually cirrhosis. The development of a non-invasive blood-based biomarker for copper status in dogs could be helpful in identifying dogs at risk and to monitor copper concentrations during treatment. In this study, two cellular copper metabolism proteins, Cu/Zn superoxide dismutase (SOD1) and its chaperone (copper chaperone for SOD1, CCS) were measured in erythrocytes and tested for association with hepatic copper concentrations in 15 Labrador retrievers with normal or increased hepatic copper concentrations...
December 2016: Veterinary Journal
https://www.readbyqxmd.com/read/27902937/study-on-the-interaction-between-curcumin-and-copc-by-spectroscopic-and-docking-methods
#18
Zhen Song, Wen Yuan, Ruitao Zhu, Song Wang, Caifeng Zhang, Binsheng Yang
Curcumin is a widely studied polyphenolic compound which has a variety of biological activity as anti-inflammatory and antitumor drugs. Recent research reported that copper chaperone binding with small molecular may relate to the treatment of cancer. In this work, the interaction between curcumin and CopC has been investigated in detail by means of UV-vis absorption, FTIR, CD, fluorescence spectroscopic and molecular docking methods The results showed that the CopC conformation was altered by curcumin with reduction of β-sheet and increase of random coil...
March 2017: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/27896900/molecular-features-of-copper-binding-proteins-involved-in-copper-homeostasis
#19
REVIEW
Giuseppe Inesi
Copper has a wide and important role in biological systems, determining conformation and activity of many metalloproteins and enzymes, such as cytochrome oxidase and superoxide dismutase . Furthermore, due to its possible reactivity with nonspecific proteins and toxic effects, elaborate systems of absorption, concentration buffering, delivery to specific protein sites and elimination, require a complex system including small carriers, chaperones and active transporters. The P-type copper ATPases ATP7A and ATP7B provide an important system for acquisition, active transport, distribution and elimination of copper...
November 28, 2016: IUBMB Life
https://www.readbyqxmd.com/read/27757465/proteomic-responses-to-gold-iii-toxicity-in-the-bacterium-cupriavidus-metallidurans-ch34
#20
Carla M Zammit, Florian Weiland, Joël Brugger, Benjamin Wade, Lyron Juan Winderbaum, Dietrich H Nies, Gordon Southam, Peter Hoffmann, Frank Reith
The metal-resistant β-proteobacterium Cupriavidus metallidurans drives gold (Au) biomineralisation and the (trans)formation of Au nuggets largely via unknown biochemical processes, ultimately leading to the reductive precipitation of mobile, toxic Au(i/iii)-complexes. In this study proteomic responses of C. metallidurans CH34 to mobile, toxic Au(iii)-chloride are investigated. Cells were grown in the presence of 10 and 50 μM Au(iii)-chloride, 50 μM Cu(ii)-chloride and without additional metals. Differentially expressed proteins were detected by difference gel electrophoresis and identified by liquid chromatography coupled mass spectrometry...
October 19, 2016: Metallomics: Integrated Biometal Science
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