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Copper chaperone

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https://www.readbyqxmd.com/read/28078344/kinetic-analysis-of-copper-transfer-from-a-chaperone-to-its-target-protein-mediated-by-complex-formation
#1
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
#2
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
#3
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...
December 24, 2016: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27942658/defining-the-human-copper-proteome-and-analysis-of-its-expression-variation-in-cancers
#4
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
#5
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
#6
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...
November 27, 2016: International Journal of Biological Macromolecules
https://www.readbyqxmd.com/read/27896900/molecular-features-of-copper-binding-proteins-involved-in-copper-homeostasis
#7
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
#8
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
https://www.readbyqxmd.com/read/27753272/streptococcus-mutans-copper-chaperone-copz-is-critical-for-biofilm-formation-and-competitiveness
#9
S S Garcia, Q Du, H Wu
The oral cavity is a dynamic environment characterized by hundreds of bacterial species, saliva, and an influx of nutrients and metal ions such as copper. Although there is a physiologic level of copper in the saliva, the oral cavity is often challenged with an influx of copper ions. At high concentrations copper is toxic and must therefore be strictly regulated by pathogens for them to persist and cause disease. The cariogenic pathogen Streptococcus mutans manages excess copper using the copYAZ operon that encodes a negative DNA-binding repressor (CopY), the P1-ATPase copper exporter (CopA), and the copper chaperone (CopZ)...
December 2016: Molecular Oral Microbiology
https://www.readbyqxmd.com/read/27744583/disease-causing-point-mutations-in-metal-binding-domains-of-wilson-disease-protein-decrease-stability-and-increase-structural-dynamics
#10
Ranjeet Kumar, Candan Ariöz, Yaozong Li, Niklas Bosaeus, Sandra Rocha, Pernilla Wittung-Stafshede
After cellular uptake, Copper (Cu) ions are transferred from the chaperone Atox1 to the Wilson disease protein (ATP7B) for incorporation into Cu-dependent enzymes in the secretory pathway. Human ATP7B is a large multi-domain membrane-spanning protein which, in contrast to homologues in other organisms, has six similar cytoplasmic metal-binding domains (MBDs). The reason for multiple MBDs is proposed to be indirect modulation of enzymatic activity and it is thus intriguing that point mutations in MBDs can promote Wilson disease...
October 15, 2016: Biometals: An International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
https://www.readbyqxmd.com/read/27666810/endothelial-antioxidant-1-a-key-mediator-of-copper-dependent-wound-healing-in-vivo
#11
Archita Das, Varadarajan Sudhahar, Gin-Fu Chen, Ha Won Kim, Seock-Won Youn, Lydia Finney, Stefan Vogt, Jay Yang, Junghun Kweon, Bayasgalan Surenkhuu, Masuko Ushio-Fukai, Tohru Fukai
Copper (Cu), an essential nutrient, promotes wound healing, however, target of Cu action and underlying mechanisms remain elusive. Cu chaperone Antioxidant-1 (Atox1) in the cytosol supplies Cu to the secretory enzymes such as lysyl oxidase (LOX), while Atox1 in the nucleus functions as a Cu-dependent transcription factor. Using mouse cutaneous wound healing model, here we show that Cu content (by X-ray Fluorescence Microscopy) and nuclear Atox1 are increased after wounding, and that wound healing with and without Cu treatment is impaired in Atox1(-/-) mice...
September 26, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27633855/effect-of-chaperones-on-prion-protein-prp23-98-aggregation-in-vitro
#12
Noriyuki Shiraishi, Yoshiaki Hirano
Recent studies have indicated that PrP23-98, an N-terminal portion of PrP, polymerizes into amyloid-like and proteinase K (PK)-resistant aggregates in the presence of NADPH with copper ions [19], and then that CRT suppressed aggregation of PrP23-98 and also promoted solubilization of the aggregates [18]. As it is interesting to find out whether other chaperones can inhibit aggregation of PrP23-98 in vitro similar to CRT, this study was conducted to determine whether BiP, Grp94, PDI Grp58 and heat shock cognate protein70 (Hsc70) can inhibit aggregation of PrP23-98 in vitro...
2016: Protein and Peptide Letters
https://www.readbyqxmd.com/read/27581939/copper-transporters-and-chaperones-their-function-on-angiogenesis-and-cellular-signalling
#13
S R Bharathi Devi, Aloysius Dhivya M, K N Sulochana
Copper, although known as a micronutrient, has a pivotal role in modulating the cellular metabolism. Many studies have reported the role of copper in angiogenesis. Copper chaperones are intracellular proteins that mediate copper trafficking to various cell organelles. However, the role and function of copper chaperones in relation to angiogenesis has to be further explored. The intracellular copper levels when in excess are deleterious and certain mutations of copper chaperones have been shown to induce cell death and influence various cellular metabolisms...
September 2016: Journal of Biosciences
https://www.readbyqxmd.com/read/27539433/identification-of-binding-sites-of-cisplatin-to-human-copper-chaperone-protein-cox17-by-high-resolution-ft-icr-ms
#14
Lijie Li, Wei Guo, Kui Wu, Yao Zhao, Qun Luo, Qingwu Zhang, Jianan Liu, Shaoxiang Xiong, Fuyi Wang
RATIONALE: Cox17 is a key copper chaperone protein responsible for delivery of cuprous ions to mitochondria and has been demonstrated to be involved in the anticancer action of cisplatin. However, the binding sites of the drug to the protein have not yet been directly identified. METHODS: The recombinant protein apo-Cox172s-s , the functional state of Cox17 transferring Cu(I), was reacted with an excess of cisplatin to produce platinated Cox17 adducts, of which the platination sites were identified by high-resolution Fourier transform ion cyclotron tandem mass spectrometry (FT-ICR-MS/MS) through electron capture dissociation (ECD)...
August 2016: Rapid Communications in Mass Spectrometry: RCM
https://www.readbyqxmd.com/read/27516958/transcriptome-analysis-of-copper-homeostasis-genes-reveals-coordinated-upregulation-of-slc31a1-sco1-and-cox11-in-colorectal-cancer
#15
Vincenza Barresi, Angela Trovato-Salinaro, Giorgia Spampinato, Nicolò Musso, Sergio Castorina, Enrico Rizzarelli, Daniele Filippo Condorelli
Copper homeostasis and distribution is strictly regulated by a network of transporters and intracellular chaperones encoded by a group of genes collectively known as copper homeostasis genes (CHGs). In this work, analysis of The Cancer Genome Atlas database for somatic point mutations in colorectal cancer revealed that inactivating mutations are absent or extremely rare in CHGs. Using oligonucleotide microarrays, we found a strong increase in mRNA levels of the membrane copper transporter 1 protein [CTR1; encoded by the solute carrier family 31 member 1 gene (SLC31A1 gene)] in our series of colorectal carcinoma samples...
August 2016: FEBS Open Bio
https://www.readbyqxmd.com/read/27502587/copper-induces-hepatocyte-injury-due-to-the-endoplasmic-reticulum-stress-in-cultured-cells-and-patients-with-wilson-disease
#16
Shinji Oe, Koichiro Miyagawa, Yuichi Honma, Masaru Harada
Copper is an essential trace element, however, excess copper is harmful to human health. Excess copper-derived oxidants contribute to the progression of Wilson disease, and oxidative stress induces accumulation of abnormal proteins. It is known that the endoplasmic reticulum (ER) plays an important role in proper protein folding, and that accumulation of misfolded proteins disturbs ER homeostasis resulting in ER stress. However, copper-induced ER homeostasis disturbance has not been fully clarified. We treated human hepatoma cell line (Huh7) and immortalized-human hepatocyte cell line (OUMS29) with copper and chemical chaperones, including 4-phenylbutyrate and ursodeoxycholic acid...
September 10, 2016: Experimental Cell Research
https://www.readbyqxmd.com/read/27499330/non-ceruloplasmin-bound-copper-and-atp7b-gene-variants-in-alzheimer-s-disease
#17
R Squitti, M Siotto, M Arciello, L Rossi
ATP7B, a protein mainly expressed in the hepatocytes, is a copper chaperone that loads the metal into the serum copper-protein ceruloplasmin during its synthesis and also escorts superfluous copper into the bile, by a sophisticated trafficking mechanism. Impaired function of this ATPase is associated with a well-known inborn error of copper metabolism, Wilson's disease (WD). Several mutations of ATP7B are known, involving different regions of the protein, thus resulting in a plethora of phenotypes in WD patients...
September 1, 2016: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/27491367/a-novel-biomarker-for-marine-environmental-pollution-of-hsp90-from-mytilus-coruscus
#18
Huihui Liu, Jiong Wu, Mengshan Xu, Jianyu He
Heat shock protein 90 (HSP90) is a conserved molecular chaperone contributing to cell cycle control, organism development and the proper regulation of cytosolic proteins. The full-length HSP90 cDNA of Mytilus coruscus (McHSP90, KT946644) was 2420bp, including an ORF of 2169bp encoding a polypeptide of 722 amino acids with predicted pI/MW 4.89/83.22kDa. BLASTp analysis and phylogenetic relationship strongly suggested McHSP90 was a member of HSP90 family, and it was highly conserved with other known HSP90, especially in the HSP90 family signatures, ATP/GTP-Binding sites and 'EEVD' motif...
October 15, 2016: Marine Pollution Bulletin
https://www.readbyqxmd.com/read/27476637/the-copper-rush-of-the-nineties
#19
Marc Solioz
The nineties witnessed the discovery of the copper ATPases, enzymes which transport copper across the cytoplasmic membranes of bacteria and eukaryotes. In the same decade, several other key components of copper homeostasis have also been discovered, like copper chaperones and plasma membrane copper transporters. This has finally led to a molecular understanding of two inherited human diseases related to copper: Menkes disease, manifested by systemic copper deficiency, and Wilson disease, caused by defective secretion of excess copper...
September 1, 2016: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/27472369/the-role-of-copper-chaperone-atox1-in-coupling-redox-homeostasis-to-intracellular-copper-distribution
#20
REVIEW
Yuta Hatori, Svetlana Lutsenko
Human antioxidant protein 1 (Atox1) is a small cytosolic protein with an essential role in copper homeostasis. Atox1 functions as a copper carrier facilitating copper transfer to the secretory pathway. This process is required for activation of copper dependent enzymes involved in neurotransmitter biosynthesis, iron efflux, neovascularization, wound healing, and regulation of blood pressure. Recently, new cellular roles for Atox1 have emerged. Changing levels of Atox1 were shown to modulate response to cancer therapies, contribute to inflammatory response, and protect cells against various oxidative stresses...
July 27, 2016: Antioxidants (Basel, Switzerland)
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