Academic literature on the topic 'Metal transporters, ZIPs'
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Journal articles on the topic "Metal transporters, ZIPs"
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Bin, Bum-Ho, Juyeon Seo, and Sung Tae Kim. "Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells." Journal of Immunology Research 2018 (October 2, 2018): 1–9. http://dx.doi.org/10.1155/2018/9365747.
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Zinc is an important trace metal in immune systems, and zinc transporters are involved in many immune responses. Recent advances have revealed the structural and biochemical bases for zinc transport across the cell membrane, with clinical implications for the regulation of zinc homeostasis in immune cells like dendritic cells, T cells, B cells, and mast cells. In this review, we discuss the function, structure, and transport aspects of two major mammalian zinc transporter types, importers and exporters. First, Zrt-/Irt-like proteins (ZIPs) mediate the zinc influx from the extracellular or luminal side into the cytoplasm. There are 14 ZIP family members in humans. They form a homo- or heterodimer with 8 transmembrane domains and extra-/intracellular domains of various lengths. Several ZIP members show specific extracellular domains composed of two subdomains, a helix-rich domain and proline-alanine-leucine (PAL) motif-containing domain. Second, ZnT (zinc transporter) was initially identified in early studies of zinc biology; it mediates zinc efflux as a counterpart of ZIPs in zinc homeostasis. Ten family members have been identified. They show a unique architecture characterized by a Y-shaped conformation and a large cytoplasmic domain. A precise, comprehensive understanding of the structures and transport mechanisms of ZIP and ZnT in combination with mice experiments would provide promising drug targets as well as a basis for identifying other transporters with therapeutic potential.
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Satarug, Soisungwan, Scott H. Garrett, Seema Somji, Mary Ann Sens, and Donald A. Sens. "Aberrant Expression of ZIP and ZnT Zinc Transporters in UROtsa Cells Transformed to Malignant Cells by Cadmium." Stresses 1, no. 2 (April 22, 2021): 78–89. http://dx.doi.org/10.3390/stresses1020007.
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Maintenance of zinc homeostasis is pivotal to the regulation of cell growth, differentiation, apoptosis, and defense mechanisms. In mammalian cells, control of cellular zinc homeostasis is through zinc uptake, zinc secretion, and zinc compartmentalization, mediated by metal transporters of the Zrt-/Irt-like protein (ZIP) family and the Cation Diffusion Facilitators (CDF) or ZnT family. We quantified transcript levels of ZIP and ZnT zinc transporters expressed by non-tumorigenic UROtsa cells and compared with those expressed by UROtsa clones that were experimentally transformed to cancer cells by prolonged exposure to cadmium (Cd). Although expression of the ZIP8 gene in parent UROtsa cells was lower than ZIP14 (0.1 vs. 83 transcripts per 1000 β-actin transcripts), an increased expression of ZIP8 concurrent with a reduction in expression of one or two zinc influx transporters, namely ZIP1, ZIP2, and ZIP3, were seen in six out of seven transformed UROtsa clones. Aberrant expression of the Golgi zinc transporters ZIP7, ZnT5, ZnT6, and ZnT7 were also observed. One transformed clone showed distinctively increased expression of ZIP6, ZIP10, ZIP14, and ZnT1, with a diminished ZIP8 expression. These data suggest intracellular zinc dysregulation and aberrant zinc homeostasis both in the cytosol and in the Golgi in the transformed UROtsa clones. These results provide evidence for zinc dysregulation in transformed UROtsa cells that may contribute in part to their malignancy and/or muscle invasiveness.
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Becares, Eva Ramos, Per Amstrup Pedersen, Pontus Gourdon, and Kamil Gotfryd. "Overproduction of Human Zip (SLC39) Zinc Transporters in Saccharomyces cerevisiae for Biophysical Characterization." Cells 10, no. 2 (January 21, 2021): 213. http://dx.doi.org/10.3390/cells10020213.
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Zinc constitutes the second most abundant transition metal in the human body, and it is implicated in numerous cellular processes, including cell division, DNA and protein synthesis as well as for the catalytic activity of many enzymes. Two major membrane protein families facilitate zinc homeostasis in the animal kingdom, i.e., Zrt/Irt-like proteins (ZIPs aka solute carrier 39, SLC39, family) and Zn transporters (ZnTs), essentially conducting zinc flux in the opposite directions. Human ZIPs (hZIPs) regulate import of extracellular zinc to the cytosol, being critical in preventing overaccumulation of this potentially toxic metal, and crucial for diverse physiological and pathological processes, including development of neurodegenerative disorders and several cancers. To date, our understanding of structure–function relationships governing hZIP-mediated zinc transport mechanism is scarce, mainly due to the notorious difficulty in overproduction of these proteins for biophysical characterization. Here we describe employment of a Saccharomyces cerevisiae-based platform for heterologous expression of hZIPs. We demonstrate that yeast is able to produce four full-length hZIP members belonging to three different subfamilies. One target (hZIP1) is purified in the high quantity and homogeneity required for the downstream biochemical analysis. Our work demonstrates the potential of the described production system for future structural and functional studies of hZIP transporters.
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Kambe, Taiho, Jim Geiser, Brett Lahner, David E. Salt, and Glen K. Andrews. "Slc39a1 to 3 (subfamily II) Zip genes in mice have unique cell-specific functions during adaptation to zinc deficiency." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 294, no. 5 (May 2008): R1474—R1481. http://dx.doi.org/10.1152/ajpregu.00130.2008.
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Subfamily II of the solute carrier (Slc)39a family contains three highly conserved members (ZIPs 1–3) that share a 12-amino acid signature sequence present in the putative fourth transmembrane domain and function as zinc transporters in transfected cells. The physiological significance of this genetic redundancy is unknown. Here we report that the complete elimination of all three of these Zip genes, by targeted mutagenesis and crossbreeding mice, causes no overt phenotypic effect. When mice were fed a zinc-adequate diet, several indicators of zinc status were indistinguishable between wild-type and triple-knockout mice, including embryonic morphogenesis and growth, alkaline phosphatase activity in the embryo, ZIP4 protein in the visceral yolk sac, and initial rates (30 min) of accumulation/retention of 67Zn in liver and pancreas. When mice were fed a zinc-deficient diet, embryonic membrane-bound alkaline phosphatase activity was reduced to a much greater extent, and 80% of the embryos of the triple-knockout mice developed abnormally compared with 12% of the embryos of wild-type mice. During zinc deficiency, the accumulation/retention (3 h) of 67Zn in the liver and pancreas of weanlings was significantly impaired in the triple-knockout mice compared with wild-type mice. Thus none of these three mammalian Zip genes apparently plays a critical role in zinc homeostasis when zinc is replete, but they play important, noncompensatory roles when this metal is deficient.
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Figueira, Antonio, Ederson Akio Kido, and Raul Santin Almeida. "Identifying sugarcane expressed sequences associated with nutrient transporters and peptide metal chelators." Genetics and Molecular Biology 24, no. 1-4 (December 2001): 207–20. http://dx.doi.org/10.1590/s1415-47572001000100028.
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Plant nutrient uptake is an active process, requiring energy to accumulate essential elements at higher levels in plant tissues than in the soil solution, while the presence of toxic metals or excess of nutrients requires mechanisms to modulate the accumulation of ions. Genes encoding ion transporters isolated from plants and yeast were used to identify sugarcane putative homologues in the sugarcane expressed sequence tag (SUCEST) database. Five cluster consensi with sequence homology to plant high-affinity phosphate transporter genes were identified. One cluster consensus allowed the prediction of a full-length protein containing 541 amino acids, with 81% amino acid identity to the Nicotiana tabacum NtPT1 gene, consisting of 12 membrane-spanning domains divided by a large hydrophilic charged region. Putative homologues to Arabidopsis thaliana micronutrient transporter genes were also detected in some of the SUCEST libraries. Iron uptake in grasses involves the release of the phytosiderophore mugeneic acid (MA) which chelate Fe3+ which is then absorbed by a specific transporter. Sugarcane expressed sequence tag (EST) homologous to genes coding for three enzymes of the mugeneic acid biosynthetic pathway [nicotianamine synthase; nicotianamine transferase; and putative mugeneic acid synthetase (ids3)] and a putative Fe3+-phytosiderophore transporter were detected. Seven sugarcane sequence clusters were identified with strong homology to members of the ZIP gene family (ZIP1, ZIP3, ZIP4, IRT1 and ZNT1), while four clusters homologous to ZIP2 and three to ZAT were found. Homologues to members of another gene family, Nramp, which code for broad-specificity transition metal transporters were also detected with constitutive expression. Partial transcripts homologous to genes encoding gamma-glutamylcysteine synthetase, glutathione synthetase, and phytochelatin synthase (responsible for biosynthesis of the metal chelator phytochelatin) and all four types of the major plant metal-chelator peptide metallothionein (MT) were identified: Type I MT being the most abundant (>1% of seed-library reads), followed by Type II which had a similar pattern of expression as that described for Arabidopsis MT. Identifying and understanding the expression of genes associated with nutrient uptake and metal tolerance could lead to the development of more nutrient-efficient sugarcane cultivars, or might allow the use of sugarcane as a hyper-accumulator plant for the restoration of contaminated areas in phytoremediation programs.
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Satarug, Soisungwan, David A. Vesey, and Glenda C. Gobe. "The Evolving Role for Zinc and Zinc Transporters in Cadmium Tolerance and Urothelial Cancer." Stresses 1, no. 2 (May 19, 2021): 105–18. http://dx.doi.org/10.3390/stresses1020009.
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Cadmium (Cd) is an environmental toxicant with serious public health consequences due to its persistence within arable soils, and the ease with which it enters food chains and then, accumulates in human tissues to induce a broad range of adverse health effects. The present review focuses on the role of zinc (Zn), a nutritionally essential metal, to protect against the cytotoxicity and carcinogenicity of Cd in urinary bladder epithelial cells. The stress responses and defense mechanisms involving the low-molecular-weight metal binding protein, metallothionein (MT), are highlighted. The efflux and influx transporters of the ZnT and Zrt-/Irt-like protein (ZIP) gene families are discussed with respect to their putative role in retaining cellular Zn homeostasis. Among fourteen ZIP family members, ZIP8 and ZIP14 mediate Cd uptake by cells, while ZnT1 is among ten ZnT family members solely responsible for efflux of Zn (Cd), representing cellular defense against toxicity from excessively high Zn (Cd) intake. In theory, upregulation of the efflux transporter ZnT1 concomitant with the downregulation of influx transporters such as ZIP8 and ZIP14 can prevent Cd accumulation by cells, thereby increasing tolerance to Cd toxicity. To link the perturbation of Zn homeostasis, reflected by the aberrant expression of ZnT1, ZIP1, ZIP6, and ZIP10, with malignancy, tolerance to Cd toxicity acquired during Cd-induced transformation of a cell model of human urothelium, UROtsa, is discussed as a particular example.
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Cousins, Robert J. "Gastrointestinal Factors Influencing Zinc Absorption and Homeostasis." International Journal for Vitamin and Nutrition Research 80, no. 45 (October 1, 2010): 243–48. http://dx.doi.org/10.1024/0300-9831/a000030.
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Diet-derived luminal factors have a major influence on zinc available for uptake across the apical membrane of enterocytes. Malabsorption and possibly intestinal microbiota limit this zinc availability. The transporter ZIP4 is expressed along the entire gastrointestinal tract and acts as a major processor of dietary zinc for loading into enterocytes from the apical membrane. Zip4 and other Zip family genes expressed in the gastrointestinal tract are up-regulated in periods of dietary zinc restriction. This provides for powerful homeostatic control. The transporter ZIP14 is up-regulated along the entire gastrointestinal tract by proinflammatory conditions. Intracellular transporters such as ZnT7, influence the transcellular movement of zinc across the enterocyte. Metallothionein, an intracellular metal buffer, and the transporter ZnT1 at the basolateral membrane, regulate the amount of zinc released to the portal circulation for systemic distribution. Pancreatic release of zinc by acinar cells is through the secretory process and apical membrane and involves transporters ZnT2 and ZnT1, respectively. Expression of both transporters is zinc-responsive. Enterocytes and acinar cells constitutively express Zip5 at the basolateral membrane, where it may serve as a monitor of zinc status.
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Chen, Shu-Wei, Kun Wu, Wu-Hong Lv, Fang Chen, Chang-Chun Song, and Zhi Luo. "Functional Analysis of Two Zinc (Zn) Transporters (ZIP3 and ZIP8) Promoters and Their Distinct Response to MTF1 and RREB1 in the Regulation of Zn Metabolism." International Journal of Molecular Sciences 21, no. 17 (August 26, 2020): 6135. http://dx.doi.org/10.3390/ijms21176135.
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ZIP (zinc-regulated transporters, iron-regulated transporter-like protein) family plays an important role in organism Zn balance. This research identified the promoter regions of ZIP3 and ZIP8, two members of ZIP family, from a freshwater teleost yellow catfish Pelteobagrus fulvidraco, characterized the binding sequences of the metal-responsive transcription factor-1 (MTF-1) and Ras responsive element binding protein 1 (RREB1) on their promoter regions. The present study cloned and obtained the 2027 bp of ZIP3 promoter and 1664 bp of ZIP8 promoter, and predicted several key elements on their promoters, such as the binding sites of CREB (cAMP-response element binding protein), KLF4 (Kruppel like factor 4), MTF-1 and RREB1. The sequence deletion from −361 bp to −895 bp down-regulated the luciferase activity of ZIP3 promoter, and the deletion from −897 bp to −1664 bp down-regulated the luciferase activity of ZIP8 promoter. Within different deletion plasmids, the relative luciferase activities of ZIP3 and ZIP8 promoters changes to Zn incubation in a Zn concentration-dependent manner. The site mutagenesis and EMSA (electrophoretic mobility shift assay) found that the −1327 bp/−1343 bp MTF-1 binding site and the −248 bp/−267 bp RREB1 binding site on the ZIP3 promoter, and the −1543 bp/−1557 bp MTF-1 binding site on the ZIP8 promoter are functional sites. Low Zn increased the binding capability between MTF-1 and its responsive site on the ZIP3 promoter, and high Zn increased the transcriptional activation ZIP3 by RREB1; Zn also promoted the binding ability between MTF-1 and its responsive element on the ZIP8 promoter. This study provides the first direct evidence for the response elements of MTF-1 and RREB1 on ZIP3 and MTF-1 on ZIP8 to Zn, which are very important for the evaluation of Zn nutrition and toxicity in vertebrates.
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Kim, Juyoung, Jaekwon Lee, and Moon-Suhn Ryu. "Zinc and the Zinc Transporter SLC39A10/ZIP10 Are Required for Heme Synthesis in Developing Erythroid Progenitors." Current Developments in Nutrition 5, Supplement_2 (June 2021): 1320. http://dx.doi.org/10.1093/cdn/nzab059_021.
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Abstract Objectives Zinc is an essential nutrient for diverse biological processes in the body. Cellular zinc homeostasis is established through differential expressions of the transmembrane zinc transporter proteins, ZnTs and ZIPs. The aims of the current studies were to elucidate the roles of cellular zinc in erythrocyte maturation, and to determine the zinc transporters essential to erythroid zinc homeostasis. Methods G1E-ER4 mouse cells were employed as an in vitro study model of terminal erythroid differentiation. A cell-impermeable zinc chelator, diethylenetriamine pentaacetate (DTPA), was used to limit extracellular zinc availability. For gene silencing, gene-specific siRNAs were introduced to cells via Nucleofection. Functional impacts of zinc and gene deficiency were assessed via ICP-MS-based metal quantitation, heme assays, and gene expression assays using RNA-seq, qPCR, and western analyses. Results G1E-ER4 cells featured a 1.7-fold increase in total cellular zinc contents after 48 h of differentiation. Restriction of zinc import by 50 µM of DTPA led to less red coloration and lower increases in mean corpuscular hemoglobin contents by development. The heme deficiency by DTPA was fully restored by the addition of equimolar zinc, and was not due to changes in cellular iron contents. Zinc-deficient G1E-ER4 cells differentiated with normal Alas2 and Hbb-b1 transcript responses, but less Alad and alpha-globin expressions. Among the 24 zinc transporter genes, Zip10 produced the most prominent response to zinc restriction in differentiating erythroid cells. ZIP10-deficient G1E-ER4 cells were less efficient than control cells in hemoglobin production under zinc restriction. ZIP10 deficiency alone had no effects on the molecular indices of red cell hemoglobinization. Conclusions Our studies characterize zinc as a nutrient essential to normal erythroid maturation and heme synthesis. Moreover, we have identified a compensatory role of ZIP10 for erythroid zinc homeostasis during zinc restriction. Thus, poor zinc status and ZIP10 mutations might serve as potential risk factors and thus new therapeutic targets for anemia and other erythrocyte-related disorders. Funding Sources Supported by CFANS Graduate Fellowship to JK, and the Allen Foundation, Inc. and USDA NIFA Hatch Funds to M-SR.
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Gebeyew, Kefyalew, Chunyu Jiang, Qinghua Gao, Liping Zhang, Hanhua Zhu, Yushi Tian, Qi Wang, Yuqing Wei, Zhiliang Tan, and Xuefeng Han. "Cadmium Accumulation in the Goat Liver and Kidney Is Partially Promoted by the Upregulation of Metal Transporter Genes." Animals 12, no. 11 (May 30, 2022): 1408. http://dx.doi.org/10.3390/ani12111408.
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Metal transporters, including divalent metal-ion transporter-1 (DMT1), Zrt-/Irt-like protein 8 and 14 (ZIP8 and ZIP14), and ferroportin-1 (FPN1), reportedly participate in cellular cadmium (Cd) uptake, but those in farm animals remain unclarified. This study aimed to examine the growth, plasma biochemical indices, Cd accumulation, and expression of metal transporter genes in the liver, kidney, and muscle of goats exposed to rice paddies contaminated with different levels of Cd. Twenty-four goats were randomly assigned across three dietary treatments: 0.23, 0.63, and 1.07 mg of Cd/kg of dry matter (DM) for 60 days. The results showed that dietary Cd exposure increased (p < 0.05) both Cd accumulation and the mRNA expressions of metal transporter genes (DMT1, ZIP, and FPN1) in the liver and kidney but not in the muscle, suggesting dietary Cd exhibited different deposition rates between goat liver, kidney, and muscle. These outcomes suggest that high levels of dietary Cd stimulated the expression of metal transporter genes and thereby enhanced the uptake and accumulation of Cd in the goat liver and kidney. As such, higher Cd concentrations in the liver and kidney observed with Cd diets could be partly explained by upregulation of metal transport genes expression.
Dissertations / Theses on the topic "Metal transporters, ZIPs"
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REED, JODIE MICHELLE. "CHARACTERIZATION OF THE 8-TRANSMEMBRANE ZIP8 TRANSPORTER: EVIDENCE OF INTRACELLULAR TRAFFICKING IN RESPONSE TO EXTRACELLULAR METAL CONCENTRATIONS." University of Cincinnati / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1187007206.
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Reed, Jodie Michelle. "Characterization of the 8-Transmembrane ZIP8 transporter evidence of intracellular trafficking in response to extracellular metal concentrations /." Cincinnati, Ohio : University of Cincinnati, 2007. http://www.ohiolink.edu/etd/view.cgi?acc%5Fnum=ucin1187007206.
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Thesis (M.S.)--University of Cincinnati, 2007.Advisor: Dr. Timothy P Dalton Title from electronic thesis title page (viewed Dec.6, 2007). Includes abstract. Keywords: Health Sciences, Toxicology Includes bibliographical references.
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Flavio, Martini. "Functional analysis of AtZIP4, AtZIP6 and AtZIP9 metal transporters of Arabidopsis thaliana and Expression of Saccharomyces cerevisiae ZRC1 in different plant species." Doctoral thesis, 2019. http://hdl.handle.net/11562/994556.
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Plants have developed a variety of adaptive strategies to take up sufficient quantities of essential macro- and micro-nutrients and avoid their excessive accumulation, which could be toxic. Metal transporters play an essential role in this homeostatic network by controlling the metal efflux across cellular membranes and compartments. The ZIP (ZRT IRT1-like Proteins: Zinc-regulated transporter Iron-regulated transporter 1-like protein) family of metal transporter is involved in this complex network. We have focused on three ZIP-family members: AtZIP4, AtZIP6 and AtZIP9, for which very little information is available. These genes have not been yet characterized although a possible role in micronutrients vascular system uploading and root uptake was hypothesized. ZIP6 is not part of the four main groups in the ZIP family and Milner et al., (2013) have highlighted its higher expression in roots than in shoots, whereas no expression modulation at varying Zn and Fe concentrations (Wintz et al., 2003). The transcript level of ZIP6 seems to be constitutively higher in the Zn hyperaccumulator Arabidopsis halleri ssp. halleri than in A. thaliana, independently of the Zn concentration (Becher et al., 2003). ZIP9 is clustered together with ZIP4, sharing c.a. 60% identity and 77% similarity at the amino acid sequence. Wintz et al. (2003) have shown that in A. thaliana both ZIP4 and ZIP9 are up-regulated in roots and shoots in Zn-deficient conditions. In A. halleri roots, ZIP9 is up-regulated upon Zn-deficiency and down-regulated in presence of high Zn concentrations. In A. thaliana shoots, ZIP9 level is detectable only upon excess Zn (Weber et al., 2004). The aim of this project is the functional analysis of AtZIP6 and AtZIP9, to understand their expression pattern and their subcellular localization. AtZIP6 and AtZIP9 knock-out mutant lines were investigated and will be used for testing metal tolerance and accumulation in order to identify which metal(s) are transported by these proteins. The high similarity between ZIP9 and ZIP4 prompted us to add AtZIP4 mutant our analysis to avoid a possible functional complementation. Furthermore, over-expressing A. thaliana lines have also been obtained fusing the 35S constitutive promoter to the AtZIP6 and AtZIP9 coding sequence in order to perform a phenotypic characterization and a metal accumulation analysis in comparison to single zip4, zip6, zip9, double zip6/zip9, zip4/zip9, zip4/zip6 and a triple zip4/zip6/zip9 knock-out mutants and wild-type lines Another part of the project concerns the effect of heterologous yeast genes in A. thaliana, tobacco and poplar plants, analyzing their ability in heavy metal accumulation. ZRC1 gene was selected since it induces Zn/Cd resistance in Saccharomyces cerevisiae. ScZRC1 is a vacuolar transporter that mediates the detoxification of Zn excess storing it into the vacuole (MacDiarmid et al., 2003). ScZRC1 belongs to the CDF transporter family and might have also a putative role in Cd detoxification.
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Ehsani, Sepehr. "The Significance of the Evolutionary Relationship of Prion Proteins and ZIP Transporters in Health and Disease." Thesis, 2012. http://hdl.handle.net/1807/33986.
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The cellular prion protein (PrPC) is unique amongst mammalian proteins in that it not only has the capacity to aggregate (in the form of scrapie PrP; PrPSc) and cause neuronal degeneration, but can also act as an independent vector for the transmission of disease from one individual to another of the same or, in some instances, other species. Since the discovery of PrPC nearly thirty years ago, two salient questions have remained largely unanswered, namely, (i) what is the normal function of the cellular protein in the central nervous system, and (ii) what is/are the factor(s) involved in the misfolding of PrPC into PrPSc? To shed light on aspects of these questions, we undertook a discovery-based interactome investigation of PrPC in mouse neuroblastoma cells (Chapter 2), and among the candidate interactors, identified two members of the ZIP family of zinc transporters (ZIP6 and ZIP10) as possessing a PrP-like domain. Detailed analyses revealed that the LIV-1 subfamily of ZIP transporters (to which ZIPs 6 and 10 belong) are in fact the evolutionary ancestors of prions (Chapter 3). We were further able to demonstrate that PrPC likely emerged from a ZIP ancestor molecule nearly half-a-billion years ago via a retrotransposition event (Chapter 4). Moreover, biochemical investigations on ZIP10, as a model LIV-1 ZIP transporter, demonstrated that the ectodomain shedding of ZIP10 observed in prion-infected mice resembles a cellular response to transition metal starvation and suggested that prion disease in mice might phenocopy a transition metal starvation status (Chapter 5). These studies have opened a new angle to study prion biology in health and disease. Biochemical investigations on other LIV-1 ZIPs and attempts at the structural elucidation of the PrP-like domain of LIV-1 ZIP proteins are ongoing and have not been included in this thesis.
Books on the topic "Metal transporters, ZIPs"
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Hu, Jian. ZIP Metal Ion Transporters. Elsevier Science & Technology, 2023.
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Hu, JianBiochemistry Building. ZIP Metal Ion Transporters. Elsevier Science & Technology Books, 2023.
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Ajeesh Krishna, T. P., T. Maharajan, S. Ignacimuthu, and S. Antony Ceasar. "Functional, Structural, and Transport Aspects of ZIP in Plants." In Plant Metal and Metalloid Transporters, 207–26. Singapore: Springer Nature Singapore, 2022. http://dx.doi.org/10.1007/978-981-19-6103-8_10.
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Dempski, Robert E. "The Cation Selectivity of the ZIP Transporters." In Metal Transporters, 221–45. Elsevier, 2012. http://dx.doi.org/10.1016/b978-0-12-394390-3.00009-4.
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