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- Niemi, MEK, et al.
(författare)
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- 2021
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swepub:Mat__t
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| 5. |
- Das, Umi, et al.
(författare)
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Computational characterization and expression profile of MTP1 gene associated with zinc homeostasis across dicot plant species
- 2021
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Ingår i: Gene Reports. - : Elsevier. - 2452-0144. ; 23, s. 1-13
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Tidskriftsartikel (refereegranskat)abstract
- This study characterizes different MTP1 (metal tolerance protein)/ZAT (zinc transporter) homologs involved in zinc (Zn) homeostasis in plants. BLAST analysis of AtMTP1 protein against 15 plant species showed 21 MTP1 homologs. These MTP1 protein homologs generally contain ~400 residues, six transmembrane helices and cation transmembrane transporter activity (GO:0008324), which can be utilized in predicting Zn uptake and tolerance mechanisms. These MTP1 genes having 1 exon are located on chromosomes 2, 7, and 14. Motifs contain conserved sequences of 41–50 residues belonging to the cation efflux family, which may help target binding sites and transcription factors. Further, AtMTP1 shows close similarities with Glycine max and Medicago trunculata. Interactome analysis suggests the association of AtMTP1 with cadmium/zinc-transporting ATPase and ZIP metal ion transporter. The AtMTP1 network is predominantly connected to cadmium/zinc-transporting ATPase (heavy metal ATPase 2, HMA2; heavy metal ATPase 3, HMA3; heavy metal ATPase 4, HMA4), cation efflux protein (MTP11), and metal tolerance protein C3 (AT4G58060). The Genevestigator predicts the high expression potential of AtMTP1 in the apical root during senescence, seedling, and bolting stages in an association with 11 co-expressed genes, mainly linked to estradiol toxicity and heat stress. Besides, AtMTP1 protein homologs possess conserved N-glyco motifs and physicochemical properties. The similarity and interactions of AtMTP1 gene with other genes suggest that Zn homeostasis in plants is associated with the regulation of different genes. These findings may advance our understanding to further develop plants capable of maintaining Zn homeostasis under adverse conditions. © 2021 Elsevier Inc.
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| 6. |
- Rahman, Md Aminur, et al.
(författare)
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Arsenic
- 2023
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Ingår i: Inorganic Contaminants and Radionuclides. - : Elsevier. ; , s. 13-40
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Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
- Arsenic (As) is a poisonous metalloid and recognized as a Group I human carcinogen by the International Agency for Research on Cancer (IARC). Arsenic often exists in groundwater and surface water, oceanic and inland deposits, rocks, soils, and biota at variable concentrations. Over the last few decades, As contamination has been augmented noticeably due to both natural and anthropogenic sources. Arsenic contamination in groundwater is currently a major global environmental catastrophe, which affects over 200 million people in 107 countries and causes various health complications including cancer. Therefore, updated information regarding the sources, chemical form, bioavailability, extent and severity, food safety and regulation, remediation, and management of As is essential. In this chapter, we accumulated the detailed sources of As, including point and diffuse sources, various inorganic and organic As species, and their toxicity in the environment. Moreover, the fate of As in the environment, economic implications of As-contaminated food and food products, and the bioavailability and bio-accessibility of As in environmental media are also briefly summarized. Remediation technologies for As-contaminated soil with the latest case study and regulatory limits of As in soil are also presented in this chapter. Overall, this chapter incorporates the past and contemporary knowledge of As, which will be useful for better management of As in the near future.
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| 8. |
- Woolcott, Orison O, et al.
(författare)
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Arachidonic acid is a physiological activator of the ryanodine receptor in pancreatic beta-cells.
- 2006
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Ingår i: Cell Calcium. - : Elsevier BV. - 0143-4160 .- 1532-1991. ; 39:6, s. 529-37
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Tidskriftsartikel (refereegranskat)abstract
- Pancreatic beta-cells have ryanodine receptors but little is known about their physiological regulation. Previous studies have shown that arachidonic acid releases Ca(2+) from intracellular stores in beta-cells but the identity of the channels involved in the Ca(2+) release has not been elucidated. We studied the mechanism by which arachidonic acid induces Ca(2+) concentration changes in pancreatic beta-cells. Cytosolic free Ca(2+) concentration was measured in fura-2-loaded INS-1E cells and in primary beta-cells from Wistar rats. The increase of cytosolic Ca(2+) concentration induced by arachidonic acid (150microM) was due to both Ca(2+) release from intracellular stores and influx of Ca(2+) from extracellular medium. 5,8,11,14-Eicosatetraynoic acid, a non-metabolizable analogue of arachidonic acid, mimicked the effect of arachidonic acid, indicating that arachidonic acid itself mediated Ca(2+) increase. The Ca(2+) release induced by arachidonic acid was from the endoplasmic reticulum since it was blocked by thapsigargin. 2-Aminoethyl diphenylborinate (50microM), which is known to inhibit 1,4,5-inositol-triphosphate-receptors, did not block Ca(2+) release by arachidonic acid. However, ryanodine (100microM), a blocker of ryanodine receptors, abolished the effect of arachidonic acid on Ca(2+) release in both types of cells. These observations indicate that arachidonic acid is a physiological activator of ryanodine receptors in beta-cells.
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