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In Vivo Study of Anti-Influenza Effect of Silver Nanoparticles in a Mouse Model
Published in Devarajan Thangadurai, Saher Islam, Charles Oluwaseun Adetunji, Viral and Antiviral Nanomaterials, 2022
Ludmila Puchkova, Mohammad Al Farroukh, Ekaterina Ilyechova, Irina Kiseleva
There is enough information to distinguish the links between the copper balance supported system, in which Ag(+) nanoparticles are involved (Figure 11.2). So, in the same way with copper ions, the absorbed Ag(+) is transported through the bloodstream to hepatocytes using alpha-2-macroglobulin (Skomorokhova et al. 2020). Ag(+) is captured by the extracellular CTR1 copper-binding sites and transported via its cuprophilic pore to the cytosolic copper-binding domain (Sankova et al. 2017). Copper chaperon superoxide dismutase (CCS) and ATOX1 (copper chaperon ATP7A/B) but not copper chaperon for CCO (COX17), accept Ag(+) from the cytosolic domain of CTR1 (Puchkova et al. 2019). However, CCS does not transfer Ag(+) to the SOD1 active center, thence AgNP treatment in mice does not cause a loss of SOD1 and CCO enzymatic activity (Zatulovskiy et al. 2012; Ilyechova et al. 2014; Orlov et al. 2016). ATOX1 delivers Ag(+) to ATP7A/B, which, in turn, transfers Ag(+) to the Golgi apparatus lumen, where they are incorporated into the active centers of Cp during its maturation and folding (Orlov et al. 2016; Skomorokhova et al. 2020). The Cp molecule can bind up to four silver atoms. This leads to unfolding and loss of enzymatic activity (Ilyechova et al. 2014). At the same time, AgNP do not affect the expression of the Cp gene at the level of transcription, translation, secretion, and T½ Ag-Cp life span in the bloodstream (Orlov et al. 2016). Ag(+) are formed from AgNP are excreted mainly through bile, which is partially associated with Cp (Skomorokhova et al. 2020).
Copper uptake in adult rainbow trout irradiated during early life stages and in non-irradiated bystander trout which swam with the irradiated fish
Published in International Journal of Radiation Biology, 2022
Richard Smith, Sunita Nadella, Richard Moccia, Colin Seymour, Carmel Mothersill
Aside from compromising ion and water balance (as previously outlined in the Introduction) the pathological action of copper extends to tumorigenesis and cancer progression. Cancer cells contain higher levels of copper than nonmalignant cells (Ebadi and Swanson 1988; Nasulewicz et al. 2004; Lowndes and Harris 2005) and the copper chaperone/transcription factor Atox1 is instrumental in cancer cell migration (Blockhuys and Wittung-Stafshede 2017). Consequently lowering cellular copper (i.e. the opposite of the increases reported here) may therefore have potential as an anti-cancer treatment (reviewed by Brewer 2014). However, in cancer cells, copper has also been shown to exert a specific anti-proliferative action (Koňarikova et al. 2016) and promote the pro-oxidant cytotoxicity of flavonoids (Arif et al 2018). Consequently copper induced oxidative stress (e.g. Valko et al. 2005) offers a possibility for cancer treatment (Gupte and Mumper 2009). Additionally copper enhances the action of anti-cancer chemotherapeutics, such as curcumin (Lee et al. 2016), oleuropein (Capo et al. 2017), cisplatin (Liu et al. 2016) and disulfiram (Wang et al. 2018).
Metal-metal interaction and metal toxicity: a comparison between mammalian and D. melanogaster
Published in Xenobiotica, 2021
Xiaoyu Yu, Xianhan Tian, Yiwen Wang, Chunfeng Zhu
Although DMT1 can absorb Cu2+, copper transporter 1 (Ctr1) is the main absorption mechanism in mammals. Three high-affinity homologs, Ctr1A, Ctr1B, and Ctr1C have been identified in the fruit fly (Zhou et al.2003, Petris 2004). Ceruloplasmin in blood transports Cu2+ to the reductase on the surface of the cell membrane and reduces it to Cu+, which is then transferred by Ctr1 on the membrane (Espinoza et al.2012). Cu entering cells can bind to Cu-specific chaperones such as COX17, CCS, and ATOX1, which can be further transported to cytochrome c oxidase in mitochondria (Banci et al.2008)(copper chaperones for superoxide dismutase) SOD1 (Schmidt et al.2000) and ATP7A. ATP7A also transports Pb out of cells. However, at present, there is only one Cu P-type ATPase transporter called ATP7 in D. melanogaster, which is expressed widely (Norgate et al.2006). Its function is similar to ATP7A and can transfer Cu to the secretory pathway or to the circulatory system through intestinal cells (Burke et al.2008).
Impaired copper transport in schizophrenia results in a copper-deficient brain state: A new side to the dysbindin story
Published in The World Journal of Biological Psychiatry, 2020
Kirsten E. Schoonover, Stacy L. Queern, Suzanne E. Lapi, Rosalinda C. Roberts
The present study is the first to investigate dysbindin-1 and copper transporters as a combined pathology in schizophrenia. The substantia nigra (SN) exhibits one of the highest levels of copper within the brain and the highest level of the copper chaperone Atox1 (Davies et al. 2013), indicating the SN has a high demand for cellular copper. Therefore, we measured (1) dysbindin-1 isoforms 1A and 1B/C, encoded by risk factor gene DTNBP1; (2) copper transporter CTR1, responsible for copper transport across the BBB; (3) copper-transporting P-type ATPase, ATP7A, which works in conjunction with CTR1 for intracellular copper transport; (4) ATP7A homologue ATP7B, responsible for transfer of copper to the secretory pathway; and (5) SN tissue copper content. We also conducted a preliminary analysis of medication status, as there are biological correlates to medication status. Our hypothesis is illustrated in Figure 1(A). We hypothesise schizophrenia patients exhibit deficits in copper transport in a copper-rich brain region potentially in relation to dysbindin-1 alterations (Figure 1(B)), which will in turn result in a cellular copper deficit within the SN. This work has been presented in preliminary form (Schoonover and Roberts 2016).