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  • 1
    Online Resource
    Online Resource
    Berlin, Heidelberg :Springer Berlin / Heidelberg,
    Keywords: Plants -- Effect of metals on. ; Electronic books.
    Description / Table of Contents: How do metals enter plants? Where do the signals come from and what are the processes involved in remediation of metals in plants? Ths book discusses studies on signaling and remediation processes with recent technological advancement including "omic" studies.
    Type of Medium: Online Resource
    Pages: 1 online resource (267 pages)
    Edition: 1st ed.
    ISBN: 9783642220814
    Language: English
    Note: Intro -- Metal Toxicity in Plants: Perception, Signaling and Remediation -- Preface -- Reference -- Contents -- Heavy Metal Bindings and Their Interactions with Thiol Peptides and Other Biological Ligands in Plant Cells -- 1 Introduction -- 2 Biological Ligands for Heavy Metal Conjugation and Detoxification in Plant Cells -- 2.1 Phytochelatins -- 2.2 Organic Acids, Nicotianamine, Amino Acids, and Phytates -- 2.3 Soluble Phenolics -- 3 Heavy Metal Localization and Distribution -- 3.1 Localization of Heavy Metals in Cells and Tissues of Different Plant Organs -- 3.2 Distribution of Heavy Metals and Conjugating Ligands in Root -- 3.3 Distribution of Heavy Metals and Conjugating Ligands in Shoots -- 4 Conclusion -- References -- Heavy Metal Perception in a Microscale Environment: A Model System Using High Doses of Pollutants -- 1 Introduction -- 2 Microscale Versus Macroscale Analysis: Time Resolved Responses -- 3 ROS Signaling and Antioxidant Responses -- 4 Phytohormone Signaling Pathways -- 5 Conclusion -- References -- Genetic and Molecular Aspects of Metal Tolerance and Hyperaccumulation -- 1 Introduction -- 1.1 Metals as Toxicants -- 1.2 Metals as Stressors -- 1.3 Defining Metal Tolerance -- 1.4 Defining Metal Accumulation -- 2 Genetic Aspects of Tolerance and Accumulation -- 2.1 Evidence from Classical Mendelian Genetics and Mutants -- 2.2 Evidence from Quantitative Genetics and Mapping -- 2.3 Evidence from Reverse Genetics and Genetic Engineering -- 2.4 Evidence from Natural Populations Variability -- 3 Molecular Aspects of Tolerance and Accumulation -- 3.1 Evidence from Physiology and Biochemistry -- 3.2 Evidence from Gene Cloning -- 3.2.1 Gene Copy Number -- 3.2.2 Gene Expression -- 3.2.3 Sequence Variants -- 3.2.4 Structural Information -- 3.3 Evidence from Transcriptomic Analysis -- 4 Conclusion -- References. , Cadmium and Copper Stress Induce a Cellular Oxidative Challenge Leading to Damage Versus Signalling -- 1 Introduction -- 1.1 Cadmium and Copper Uptake and Homeostasis -- 1.1.1 Uptake of Excess Cu and Cd by the Plant Is Unavoidable -- 1.1.2 Chelation and Sequestration of Excess Metals -- 1.2 The Perception of Cd and Cu Stress and the Generation of Excess Reactive Oxygen Species -- 1.2.1 Direct and Indirect Mechanisms of ROS Generation -- 1.2.2 Enzymatic ROS Generation -- 1.2.3 Cd and Cu Disturb Redox Homeostasis in Plant Organelles -- 1.2.4 Perception of the Stress Signal -- 2 The Oxidative Stress Signature Consists of Altered Redox-Related Gene Expression, Enzyme Activities and Metabolites, and Is Informative for the Oxidative Challenge Induced by Metals -- 2.1 Superoxide Scavenging by Superoxide Dismutases -- 2.2 H2O2 Scavenging: Catalases and Ascorbate Peroxidases -- 2.3 Detoxification of ROS Via the Ascorbate-Glutathione Cycle -- 2.4 Antioxidant Metabolites -- 2.5 Description of the Oxidative Stress Signature -- 3 The Oxidative Challenge Can Cause Damage and Trigger Signalling Pathways Leading to Acclimation Responses -- 3.1 Metal-Induced Oxidative Damage -- 3.2 The Cd- and Cu-Induced Oxidative Challenge Activates and Interferes with Signalling Pathways -- 3.3 Retrograde Signalling by Cellular Organelles -- 4 Conclusion -- References -- Insights into Cadmium Toxicity: Reactive Oxygen and Nitrogen Species Function -- 1 Introduction -- 2 Cadmium Toxicity in Plants -- 3 Plant Mechanisms to Cope with Cadmium -- 4 Transcriptomic and Proteomic Analyses Under Cadmium Stress -- 5 ROS Metabolism in Response to Cadmium -- 5.1 ROS Production Under Cd Stress -- 5.2 Antioxidant Systems Under Cd Stress -- 5.2.1 Enzymatic Antioxidants Systems -- 5.2.2 Non-enzymatic Antioxidants Systems -- 6 NO Metabolism in Response to Cadmium. , 6.1 NO Production Under Cd Stress -- 6.2 NO Function and Protection Under Cd Stress -- 7 Organelles Involvement in Cd Stress -- 8 Conclusion -- References -- Exploring the Plant Response to Cadmium Exposure by Transcriptomic, Proteomic and Metabolomic Approaches: Potentiality of High High-Throughput Methods, Promises of Integrative Biology -- 1 Introduction -- 2 Global Response of Plants to Cadmium Exposure -- 2.1 Overview of a Cadmium Exposure in Plants as Evaluated by Transcriptomic, Proteomic and Metabolomic Approaches -- 2.1.1 Primary Metabolism -- 2.1.2 Defence Mechanisms -- 2.2 Transcriptomic Analysis Allow for Large Scale Comparisons Between Species and/or Treatment -- 3 Future Directions -- 3.1 Subcellular-Level Analysis of the Cd Response -- 3.2 Post-translational Modifications: Phosphoproteomic Studies -- 3.3 Systems Biology and Integrated Analysis -- 3.4 Data Mining and Integration: The Bioinformatics Challenge -- 4 Conclusion -- References -- Proteomics as a Toolbox to Study the Metabolic Adjustment of Trees During Exposure to Metal Trace Elements -- 1 Introduction -- 2 Proteomics of Woody Species -- 2.1 Proteomics: General Considerations -- 2.1.1 Protein Extraction and Sample Preparation -- 2.1.2 2D-PAGE -- 2.1.3 Protein Identification -- 2.2 Case Study: Proteome Study of Poplar and Cd Pollution -- 3 Conclusion -- References -- Proteomics of Plant Hyperaccumulators -- 1 Plant Hyperaccumulators -- 2 Methods in Plant Proteomics -- 2.1 Protein Extraction -- 2.2 Protein Separation -- 2.3 Protein Patterns Analysis and Protein Identification -- 3 Proteomic Approaches for Identification of Key Functions in the Hyperaccumulators -- 3.1 Proteins Involved in Plant-Soil Interaction -- 3.2 Root Proteome -- 3.3 Shoot Proteome -- 4 Follow-Up in Proteomic of Hyperaccumulators -- 5 Conclusion -- References. , Heavy Metal Toxicity: Oxidative Stress Parameters and DNA Repair -- 1 Introduction -- 2 Oxidative Stress and Cell Defenses -- 3 DNA Repair Mechanisms: A General Overview -- 3.1 Base Excision Repair (BER) -- 3.2 Nucleotide Excision Repair (NER) -- 3.3 Mismatch Repair (MMR) -- 3.4 Double-Strand Break Repair -- 4 Heavy Metals -- 4.1 Arsenic -- 4.2 Cadmium -- 4.3 Chromium -- 4.4 Copper -- 4.5 Lead -- 4.6 Mercury -- 4.7 Selenium -- 4.8 Zinc -- 5 Heavy Metal Hyperaccumulator Phenotypes in Plants -- 6 Conclusion -- References -- Protein Oxidative Modifications -- 1 Proteins as Molecular Targets of Oxidative Reactions -- 1.1 Protein Oxidative Products -- 2 Metals as Responsible of Protein Oxidation -- 2.1 Metals Ions-Catalyzed Oxidation Systems -- 2.2 Metalloproteins Susceptibility to Oxidative Stress -- 3 Metal Stress in Plants Is Associated to an Increase in Protein Carbonylation -- 3.1 Metals Catalyze Reactive Oxygen Species Generation Inside the Cell -- 4 Metals Can Alter Cell Metabolism by Mediating Protein Carbonylation -- 4.1 Regulation of the Translation of Isoforms: The Catalase -- 5 Carbonylated Protein Degradation -- 5.1 Role of Proteases -- 5.2 Role of 20S Proteasome -- 6 Conclusion -- References -- Zn/Cd/Co/Pb P1b-ATPases in Plants, Physiological Roles and Biological Interest -- 1 Introduction -- 1.1 P-ATPases Subfamily -- 1.2 Structure of the P1B-ATPases -- 2 Physiological Roles and Expression Profiles of Plant P1B-ATPases -- 2.1 HMA1 -- 2.2 HMA6 and HMA8 -- 2.3 HMA5 -- 2.4 HMA7 -- 2.5 HMA2, HMA4 and HMA3 -- 2.5.1 HMA2 and HMA4 -- 2.5.2 HMA3 -- 3 Phylogeny -- 4 Biotechnological Interest -- 4.1 Biofortification -- 4.2 Interest in Phytoremediation -- 5 Conclusion -- References -- Interference of Heavy Metal Toxicity with Auxin Physiology -- 1 Introduction: Auxin as a Growth Regulator -- 2 Auxin: A Mediator Between Growth and Stress Adaptation. , 3 Auxin and Heavy Metal Stress -- 4 Auxin and Essential Metals -- 5 Conclusions -- References -- Index.
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  • 2
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The peroxisomal manganese superoxide dismutase (perMn-SOD; EC 1.15.1.1) was purified to homogeneity for the first time from peroxisomes of pea (Pisum sativum L.) leaves. Peroxisomes were isolated from pea leaves by sucrose density-gradient centrifugation, and then perMn-SOD was purified from these organelles by two purification steps involving anion-exchange and gel-filtration fast protein liquid chromatography. Pure peroxisomal Mn-SOD had a specific activity of 2 880 units per mg protein and was purified 3 000-fold, with a yield of about 7 µg enzyme per kg pea leaves. The relative molecular mass determined for perMn-SOD was 92 000, and it was composed of four equal subunits of 27 kDa. Ultraviolet and visible absorption spectra of the enzyme showed two absorption maxima at 278 and 483 nm, respectively, and two shoulders at 290 and 542 nm. By isoelectric focusing (pH 5-7), an isoelectric point of 5.53 was determined for perMn-SOD. In immunoblot assays, purified Mn-SOD was recognized by a polyclonal antibody against mitochondrial Mn-SOD (mitMn-SOD) from pea leaves. The amino acid sequence of the N-terminal region of the purified peroxisomal enzyme was determined. A 100% identity was found with the mitMn-SOD from pea leaves, and high identities were also found with Mn-SODs from other plant species.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 104 (1998), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Peroxisomes are subcellular organelles with an essentially oxidative type of metabolism. The presence in these organelles of superoxide dismutases and the generation of superoxide radicals (O2•−) was first demonstrated in plant tissues and in recent years different experimental evidence has suggested the existence of cellular functions related to activated oxygen species. Some of these functions are analyzed in this work.In purified intact peroxisomes from pea (Pisum sativum L.) leaves, xanthine oxidase and urate oxidase were found to be present. The occurrence and the level of the metabolites xanthine, hypoxanthine, uric acid, and allantoin were studied in extracts of pea leaf peroxisomes by HPLC. Xanthine, uric acid, and allantoin were detected in peroxisomes. These results suggest a cellular role for leaf peroxisomes in the catabolism of purines.In peroxisomal membranes, 3 polypeptides (PMPs) with molecular masses of 18, 29 and 32 kDa, respectively, have been shown to generate superoxide radicals. These PMPs were purified from pea leaf peroxisomal membranes and characterized. While the 18- and 32-kDa PMPs use NADH as electron donor for O2•− production, the 29-kDa PMP was clearly dependent on NADPH.Very recently, the occurrence in pea leaf peroxisomes of all the enzymes of the ascorbate-glutathione cycle has been demonstrated. NADPH is required for the glutathione reductase activity of the cycle and this implies the reduction of NADP+ to NADPH. This recycling function could be carried out by the NADP-dependent glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH), and isocitrate dehydrogenase (ICDH). These 3 dehydrogenases have been demonstrated to be present in the matrix of pea leaf peroxisomes.The catabolism of purines, the superoxide-generating PMPs, the ascorbate-glutathione cycle, and the dehydrogenase-mediated recycling of NADPH, are activated oxygen roles of leaf peroxisomes that add to other functions previously known for peroxisomes from eukaryotic cells.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The subcellular localization of superoxide dismutase (SOD; EC. 1.15.1.1) was studied in leaves of two ureide-producing leguminous plants (Phaseolus vulgaris L. cv. Contender and Vigna unguiculata [L.] Walp). In leaves of Vigna and Phaseolus, three superoxide dismutases were found, an Mn-SOD and two Cu, Zn-containing SODs (I and II). Chloroplasts, mitochondria, and peroxisomes were purified by differential and density-gradient centrifugation using either Percoll or sucrose gradients. The yields obtained in intact chloroplasts and peroxisomes from Vigna were considerably higher than those achieved for Phaseolus. Purified chloroplasts only contained the Cu, Zn-SOD II isozyme, but in mitochondria both Mn-SOD and Cu, Zn-SOD I isozymes were present. In purified peroxisomes no SOD activity was detected. The absence of SOD activity in leaf peroxisomes from Vigna contrasts with results reported for the amide-metabolizing legume Pisum sativum L. where the occurrence of Mn-SOD was demonstrated in leaf peroxisomes (del Río et al. 1983. Planta 158: 216–224; Sandalio et al. 1987. Plant Sci. 51: 1–8). This suggests that in leaf peroxisomes from Vigna plants the generation of O2- radicals under normal conditions probably does not take place.
    Type of Medium: Electronic Resource
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