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      The green microalga Tetraselmis suecica reduces oxidative stress and induces repairing mechanisms in human cells

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          Abstract

          Green microalgae contain many active pigments such as carotenoids having antioxidant and protective activity on human cells. Here we investigate the biological activity of an ethanol/water extract of the marine green microalga Tetraselmis suecica containing high levels of carotenoids such as the xanthophylls lutein, violaxanthin, neoxanthin, antheraxanthin and loroxanthin esters. This extract has a strong antioxidant and repairing activity in the human lung cancer cell line (A549) as shown by the increased expression of dehydrocholesterol reductase-24 (DHCR24) and prostaglandin reductase 1 (PTGR1) genes and proteins. The extract also reduces prostaglandin E 2 (PGE 2) levels in cells damaged by H 2O 2 and has tissue repairing effects on reconstructed human epidermal tissue cells (EpiDerm TM) indicating a potential cosmeceutical activity of this microalgal species.

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          Use of MTT colorimetric assay to measure cell activation.

          Denis Gerlier, Nicole Thomasset (1986)
          The MTT tetrazolium salt colorimetric assay previously described by Mosmann (1983, J. Immunol. Methods 65, 55) to measure cytotoxicity and cell proliferation was further explored to extend its application to the measurement of cell activation. The level of MTT cleavage by viable cells of various origins was found to be directly proportional to the number of cells but to increase as a non-linear function of time. This non-linear relationship was related to a time-linear cell death during MTT incubation. The cleavage of MTT by viable cells was found to follow first order kinetics and could be fitted to Michaelis' kinetics. Different cell types exhibited similar apparent Km values (1949 microM) and different apparent maximal velocities (V). The apparent V values determined for a given cell type under different experimental conditions were rigorously similar. This analysis of MTT cleavage by viable cells suggests that the colorimetric MTT test can be useful to quantify the activation level of cells, independently of proliferation.
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            Probiotics in aquaculture

            A Irianto, B. Austin (2002)
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              Activation of superoxide dismutases: putting the metal to the pedal.

              Valeria Cizewski Culotta, Mei Yang, Thomas V. O'Halloran (2006)
              Superoxide dismutases (SOD) are important anti-oxidant enzymes that guard against superoxide toxicity. Various SOD enzymes have been characterized that employ either a copper, manganese, iron or nickel co-factor to carry out the disproportionation of superoxide. This review focuses on the copper and manganese forms, with particular emphasis on how the metal is inserted in vivo into the active site of SOD. Copper and manganese SODs diverge greatly in sequence and also in the metal insertion process. The intracellular copper SODs of eukaryotes (SOD1) can obtain copper post-translationally, by way of interactions with the CCS copper chaperone. CCS also oxidizes an intrasubunit disulfide in SOD1. Adventitious oxidation of the disulfide can lead to gross misfolding of immature forms of SOD1, particularly with SOD1 mutants linked to amyotrophic lateral sclerosis. In the case of mitochondrial MnSOD of eukaryotes (SOD2), metal insertion cannot occur post-translationally, but requires new synthesis and mitochondrial import of the SOD2 polypeptide. SOD2 can also bind iron in vivo, but is inactive with iron. Such metal ion mis-incorporation with SOD2 can become prevalent upon disruption of mitochondrial metal homeostasis. Accurate and regulated metallation of copper and manganese SOD molecules is vital to cell survival in an oxygenated environment.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Sci Rep
                Journal ID (iso-abbrev): Sci Rep
                Title: Scientific Reports
                Publisher: Nature Publishing Group
                ISSN (Electronic): 2045-2322
                Publication date (Electronic): 24 January 2017
                Publication date Collection: 2017
                Volume: 7
                Electronic Location Identifier: 41215
                Affiliations
                [1 ]Integrative Marine Ecology Department, Stazione Zoologica Anton Dohrn , Villa Comunale, Naples 80121, Italy
                [2 ]University of Naples “Federico II”, Department of Veterinary Medicine and Animal Production , Via Federico Delpino 1, Naples 80137, Italy
                [3 ]Bio-Organic Chemistry Unit, Institute of Biomolecular Chemistry-CNR , Via Campi Flegrei 34, Pozzuoli, Naples 80078, Italy
                Author notes
                Article
                Publisher Item ID: srep41215
                DOI: 10.1038/srep41215
                PMC ID: 5259714
                PubMed ID: 28117410
                SO-VID: a2d12767-c406-4518-9058-507807a7e93f
                Copyright © Copyright © 2017, The Author(s)
                License:

                This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

                History
                Date received : 21 December 2015
                Date accepted : 04 November 2016
                Categories
                Subject: Article

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