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      Selenium Accumulation in Unicellular Green Alga Chlorella vulgaris and Its Effects on Antioxidant Enzymes and Content of Photosynthetic Pigments

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      Author(s): 1 , 2 , 1 , 2 , 3 , 1 , 2 , *
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      Journal: PLoS ONE
      Publisher: Public Library of Science

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          Abstract

          The aim of the present study was to investigate selenite effects in the unicellular green algae Chlorella vulgaris as a primary producer and the relationship with intracellular bioaccumulation. The effects of selenite were evaluated by measuring the effect of different selenite concentrations on algal growth during a 144 h exposure period. It was found that lower Se concentrations (≤75 mg L −1) positively promoted C. vulgaris growth and acted as antioxidant by inhibiting lipid peroxidation (LPO) and intracellular reactive oxygen species (ROS). The antioxidative effect was associated with an increase in guaiacol peroxidase (GPX), catalase (CAT), superoxide dismutase (SOD) and photosynthetic pigments. Meanwhile, significant increase in the cell growth rate and organic Se content was also detected in the algae. In contrast, these changes were opposite in C. vulgaris exposed to Se higher than 100 mg L −1. The antioxidation and toxicity appeared to be correlated to Se bioaccumulation, which suggests the appropriate concentration of Se in the media accumulation of C. vulgaris should be 75 mg L −1. Taken together, C. vulgaris possesses tolerance to Se, and Se-Chlorella could be developed as antioxidative food for aquaculture and human health.

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          Selenocysteine.

          T C Stadtman (1996)
          Selenocysteine is recognized as the 21st amino acid in ribosome-mediated protein synthesis and its specific incorporation is directed by the UGA codon. Unique tRNAs that have complementary UCA anticodons are aminoacylated with serine, the seryl-tRNA is converted to selenocysteyl-tRNA and the latter binds specifically to a special elongation factor and is delivered to the ribosome. Recognition elements within the mRNAs are essential for translation of UGA as selenocysteine. A reactive oxygen-labile compound, selenophosphate, is the selenium donor required for synthesis of selenocysteyl-tRNA. Selenophosphate synthetase, which forms selenophosphate from selenide and ATP, is found in various prokaryotes, eukaryotes, and archaebacteria. The distribution and properties of selenocysteine-containing enzymes and proteins that have been discovered to date are discussed. Artificial selenoenzymes such as selenosubtilisin have been produced by chemical modification. Genetic engineering techniques also have been used to replace cysteine residues in proteins with selenocysteine. The mechanistic roles of selenocysteine residues in the glutathione peroxidase family of enzymes, the 5' deiodinases, formate dehydrogenases, glycine reductase, and a few hydrogenases are discussed. In some cases a marked decrease in catalytic activity of an enzyme is observed when a selenocysteine residue is replaced with cysteine. This substitution caused complete loss of glycine reductase selenoprotein A activity.
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            Selenium supplementation restores the antioxidative capacity and prevents cell damage in bone marrow stromal cells in vitro.

            Sabine Zeck, Tara M Ulmer, Nicole Schupp … (2006)
            Bone marrow stromal cells (BMSCs) and other cell populations derived from mesenchymal precursors are developed for cell-based therapeutic strategies and undergo cellular stress during ex vivo procedures. Reactive oxygen species (ROS) of cellular and environmental origin are involved in redox signaling, cumulative cell damage, senescence, and tumor development. Selenium-dependent (glutathione peroxidases [GPxs] and thioredoxin reductases [TrxRs]) and selenium-independent (superoxide dismutases [SODs] and catalase [CAT]) enzyme systems regulate cellular ROS steady state levels. SODs process superoxide anion to hydrogen peroxide, which is subsequently neutralized by GPx and CAT; TrxR neutralizes other ROS, such as peroxinitrite. Primary BMSCs and telomerase-immortalized human mesenchymal stem cells (hMSC-TERT) express GPx1-3, TrxR1, TrxR2, SOD1, SOD2, and CAT. We show here that in standard cell cultures (5%-10% fetal calf serum, 5-10 nM selenite), the activity of antioxidative selenoenzymes is impaired in hMSC-TERT and BMSCs. Under these conditions, the superoxide anion processing enzyme SOD1 is not sufficiently stimulated by an ROS load. Resulting oxidative stress favors generation of micronuclei in BMSCs. Supplementation of selenite (100 nM) restores basal GPx and TrxR activity, rescues basal and ROS-stimulated SOD1 mRNA expression and activity, and reduces ROS accumulation in hMSC-TERT and micronuclei generation in BMSCs. In conclusion, BMSCs in routine cell culture have low antioxidative capacity and are subjected to oxidative stress, as indicated by the generation of micronuclei. Selenite supplementation of BMSC cultures appears to be an important countermeasure to restore their antioxidative capacity and to reduce cell damage in the context of tissue engineering and transplantation procedures.
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              Between a rock and a hard place: trace element nutrition in Chlamydomonas.

              Anand Merchant, Janette Kropat, Stephen Tottey … (2006)
              Photosynthetic organisms are among the earliest life forms on earth and their biochemistry is strictly dependent on a wide range of inorganic nutrients owing to the use of metal cofactor-dependent enzymes in photosynthesis, respiration, inorganic nitrogen and sulfur assimilation. Chlamydomonas reinhardtii is a photosynthetic eukaryotic model organism for the study of trace metal homeostasis. Chlamydomonas spp. are widely distributed and can be found in soil, glaciers, acid mines and sewage ponds, suggesting that the genus has significant capacity for acclimation to micronutrient availability. Analysis of the draft genome indicates that metal homeostasis mechanisms in Chlamydomonas represent a blend of mechanisms operating in animals, plants and microbes. A combination of classical genetics, differential expression and genomic analysis has led to the identification of homologues of components known to operate in fungi and animals (e.g., Fox1, Ftr1, Fre1, Fer1, Ctr1/2) as well as novel molecules involved in copper and iron nutrition (Crr1, Fea1/2). Besides activating iron assimilation pathways, iron-deficient Chlamydomonas cells re-adjust metabolism by reducing light delivery to photosystem I (to avoid photo-oxidative damage resulting from compromised FeS clusters) and by modifying the ferredoxin profile (perhaps to accommodate preferential allocation of reducing equivalents). Up-regulation of a MnSOD isoform may compensate for loss of FeSOD. Ferritin could function to buffer the iron released from programmed degradation of iron-containing enzymes in the chloroplast. Some metabolic adjustments are made in anticipation of deficiency while others occur only with sustained or severe deficiency. Copper-deficient Chlamydomonas cells induce a copper assimilation pathway consisting of a cell surface reductase and a Cu(+) transporter (presumed CTR homologue). There are metabolic adaptations in addition: the synthesis of "back-up" enzymes for plastocyanin in photosynthesis and the ferroxidase in iron assimilation plus activation of alternative oxidase to handle the electron "overflow" resulting from reduced cytochrome oxidase function. Oxygen-dependent enzymes in the tetrapyrrole pathway (coproporphyrinogen oxidase and aerobic oxidative cyclase) are also increased in expression and activity by as much as 10-fold but the connection between copper nutrition and tetrapyrroles is not understood. The copper-deficiency responses are mediated by copper response elements that are defined by a GTAC core sequence and a novel metalloregulator, Crr1, which uses a zinc-dependent SBP domain to bind to the CuRE. The Chlamydomonas model is ideal for future investigation of nutritional manganese deficiency and selenoenzyme function. It is also suited for studies of trace nutrient interactions, nutrition-dependent metabolic changes, the relationship between photo-oxidative stress and metal homeostasis, and the important questions of differential allocation of limiting metal nutrients (e.g., to respiration vs. photosynthesis).
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                Author and article information

                Contributors
                Paul A. Cobine: Role: Editor
                Journal
                Journal ID (nlm-ta): PLoS One
                Journal ID (iso-abbrev): PLoS ONE
                Journal ID (publisher-id): plos
                Journal ID (pmc): plosone
                Title: PLoS ONE
                Publisher: Public Library of Science (San Francisco, USA )
                ISSN (Electronic): 1932-6203
                Publication date Collection: 2014
                Publication date (Electronic): 6 November 2014
                Volume: 9
                Issue: 11
                Electronic Location Identifier: e112270
                Affiliations
                [1 ]Institute of Hydrobiology, Jinan University, Guangzhou, 510632, P.R. China
                [2 ]Key Laboratory of Aquatic Eutrophication and Control of Harmful Algal Blooms, Guangdong Higher Education Institutes, Guangzhou, 510632, P.R. China
                [3 ]Department of Biotechnology, Jinan University, Guangzhou, 510632, P.R. China
                Auburn University, United States of America
                Author notes

                Competing Interests: The authors have declared that no competing interests exist.

                Conceived and designed the experiments: XS YY. Performed the experiments: XS YZ. Analyzed the data: XS YZ. Contributed reagents/materials/analysis tools: YY. Contributed to the writing of the manuscript: XS ZH.

                Article
                Publisher ID: PONE-D-14-15379
                DOI: 10.1371/journal.pone.0112270
                PMC ID: 4223018
                PubMed ID: 25375113
                SO-VID: a4b74783-7c4b-4d2e-844b-257a5ed36fd5
                Copyright statement: Copyright @ 2014
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

                History
                Date received : 8 April 2014
                Date accepted : 3 October 2014
                Page count
                Pages: 8
                Funding
                This work was supported by Nature Science Foundation of China (U1301235, 41173079) and the Support Project of the Science and Technology, China (2012BAC07B05, 2012BAD18B01). ( http://www.nsfc.gov.cn/). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
                Categories
                Subject: Research Article
                Subject: Biology and Life Sciences
                Subject: Agriculture
                Subject: Aquaculture
                Subject: Algaculture
                Subject: Biochemistry
                Subject: Enzymology
                Subject: Enzymes
                Subject: Oxidative Damage
                Subject: Reactive Oxygen Species
                Subject: Antioxidants
                Subject: Cell Biology
                Subject: Oxidative Stress
                Subject: Toxicology
                Subject: Toxicity
                Custom metadata
                Data Availability The authors confirm that all data underlying the findings are fully available without restriction. All relevant data are within the paper.

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