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https://www.readbyqxmd.com/read/28900031/the-metal-chaperone-atox1-regulates-the-activity-of-the-human-copper-transporter-atp7b-by-modulating-domain-dynamics
#1
Corey H Yu, Nan Yang, Jameson Bothe, Marco Tonelli, Sergiy Nokhrin, Natalia V Dolgova, Lelita T 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 hepato-neurological 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...
September 12, 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
#2
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...
September 5, 2017: Biomaterials
https://www.readbyqxmd.com/read/28820536/atp7a-and-atp7b-regulate-copper-homeostasis-in-developing-male-germ-cells-in-mice
#3
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...
August 18, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28759062/copper-finger-protein-of-sp1-the-molecular-basis-of-copper-sensing
#4
Siming Yuan, Siming Chen, Zhaoyong Xi, Yangzhong Liu
The cellular copper level is strictly regulated since excessive copper is harmful to cells. It has been proposed that the expression of copper transport protein hCtr1 is transcriptionally regulated by specificity protein 1 (Sp1) in response to the cellular copper level. However, it is not known how Sp1, a zinc-finger-protein (ZFP), can sense copper ions in cells. Here we found that Sp1 demonstrates high binding affinity to cuprous ions, even stronger than Cu-Atox1 binding. Cu(i) can displace Zn(ii) in Sp1, resulting in a well-folded 'Copper-Finger-Protein' (CFP)...
August 16, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28711491/copper-chaperone-atox1-regulates-pluripotency-factor-oct4-in-preimplantation-mouse-embryos
#5
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/28653724/probing-functional-roles-of-wilson-disease-protein-atp7b-copper-binding-domains-in-yeast
#6
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
#7
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
#8
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/28433108/genetic-and-environmental-modifiers-of-wilson-disease
#9
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/28383086/platinum-transfer-from-hctr1-to-atox1-is-dependent-on-the-type-of-platinum-complex
#10
Xuelei Wu, Siming Yuan, Erqiong Wang, Yang Tong, Guolin Ma, Kaiju Wei, Yangzhong Liu
In spite of their wide application, the cellular uptake of platinum based anticancer drugs is still unclear. The copper transport protein, hCTR1, is proposed to facilitate the cellular uptake of cisplatin, whereas organic cation transport (OCT) is more important for oxaliplatin. It has been reported that both N-terminal and C-terminal metal binding motifs of hCTR1 are highly reactive to cisplatin, which is the initial step of protein assisted cellular uptake of cisplatin. It is still unknown how the platinum drugs in hCTR1 transfer to cytoplasmic media, and whether various platinum complexes possess different activities in this process...
May 24, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28294521/thiol-based-copper-handling-by-the-copper-chaperone-atox1
#11
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...
April 2017: IUBMB Life
https://www.readbyqxmd.com/read/28293195/comparative-investigation-of-copper-tolerance-and-identification-of-putative-tolerance-related-genes-in-tardigrades
#12
Thomas L Hygum, Dannie Fobian, Maria Kamilari, Aslak Jørgensen, Morten Schiøtt, Martin Grosell, Nadja Møbjerg
Tardigrades are microscopic aquatic animals renowned for their tolerance toward extreme environmental conditions. The current study is the first to investigate their tolerance toward heavy metals and we present a novel tardigrade toxicant tolerance assay based on activity assessments as a measure of survival. Specifically, we compare tolerance toward copper in four species representing different evolutionary lineages, habitats and adaptation strategies, i.e., a marine heterotardigrade, Echiniscoides sigismundi, a limno-terrestrial heterotardigrade, Echiniscus testudo, a limno-terrestrial eutardigrade, Ramazzottius oberhaeuseri, and a marine eutardigrade, Halobiotus crispae...
2017: Frontiers in Physiology
https://www.readbyqxmd.com/read/28027931/copper-chaperone-atox1-plays-role-in-breast-cancer-cell-migration
#13
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
#14
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/27934216/ctr1-intracellular-loop-is-involved-in-the-copper-transfer-mechanism-to-the-atox1-metallochaperone
#15
Ariel R Levy, Matan Nissim, Netanel Mendelman, Jordan Chill, Sharon Ruthstein
Understanding the human copper cycle is essential to understand the role of metals in promoting neurological diseases and disorders. One of the cycles controlling the cellular concentration and distribution of copper involves the copper transporter, Ctr1; the metallochaperone, Atox1; and the ATP7B transporter. It has been shown that the C-terminus of Ctr1, specifically the last three amino acids, HCH, is involved in both copper coordination and the transfer mechanism to Atox1. In contrast, the role of the intracellular loop of Ctr1, which is an additional intracellular segment of Ctr1, in facilitating the copper transfer mechanism has not been investigated yet...
December 8, 2016: Journal of Physical Chemistry. B
https://www.readbyqxmd.com/read/27744583/disease-causing-point-mutations-in-metal-binding-domains-of-wilson-disease-protein-decrease-stability-and-increase-structural-dynamics
#16
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...
February 2017: 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
#17
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/27472369/the-role-of-copper-chaperone-atox1-in-coupling-redox-homeostasis-to-intracellular-copper-distribution
#18
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)
https://www.readbyqxmd.com/read/27401861/transcriptomic-response-of-yeast-cells-to-atx1-deletion-under-different-copper-levels
#19
Ayca Cankorur-Cetinkaya, Serpil Eraslan, Betul Kirdar
BACKGROUND: Iron and copper homeostatic pathways are tightly linked since copper is required as a cofactor for high affinity iron transport. Atx1p plays an important role in the intracellular copper transport as a copper chaperone transferring copper from the transporters to Ccc2p for its subsequent insertion into Fet3p, which is required for high affinity iron transport. RESULTS: In this study, genome-wide transcriptional landscape of ATX1 deletants grown in media either lacking copper or having excess copper was investigated...
July 11, 2016: BMC Genomics
https://www.readbyqxmd.com/read/27379771/evidence-for-a-role-for-the-putative-drosophila-hgrx1-orthologue-in-copper-homeostasis
#20
Stephen W Mercer, Richard Burke
Glutaredoxins are a family of small molecular weight proteins that have a central role in cellular redox regulation. Human GRX1 (hGRX1) has also been shown to play an integral role in copper homeostasis by regulating the redox activity of the metalated sites of copper chaperones such as ATOX1 and SOD1, and the copper efflux proteins ATP7A and ATP7B. To further elucidate the role of hGRX1 in copper homeostasis, we examined the impact of RNA interference-mediated knockdown of CG6852, a putative Drosophila orthologue of hGRX1...
August 2016: Biometals: An International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
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