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      Increased fucoxanthin in Chaetoceros calcitrans extract exacerbates apoptosis in liver cancer cells via multiple targeted cellular pathways

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          Highlights

          • •

            Both treatments inhibited cancer proliferation in a time and dose dependent manner.

          • •

            FxRF treatment were effective in inducing apoptosis in HepG2 cells than crude extract.

          • •

            Treatments stimulated regulation in cell signalling, apoptotic and antioxidant genes.

          Abstract

          In this study, anti-proliferative effects of C. calcitrans extract and its fucoxanthin rich fraction (FxRF) were assessed on human liver HepG2 cancer cell line. Efficacy from each extract was determined by cytotoxicity assay, morphological observation, and cell cycle analysis. Mechanisms of action observed were evaluated using multiplex gene expression analysis. Results showed that CME and FxRF induced cytotoxicity to HepG2 cells in a dose and time-dependent manner. FxRF (IC 50: 18.89 μg.mL −1) was found to be significantly more potent than CME (IC 50: 87.5 μg.mL −1) (p < 0.05). Gene expression studies revealed that anti-proliferative effects in treated cells by C. calcitrans extracts were mediated partly through the modulation of numerous genes involved in cell signaling ( AKT1, ERK1/2, JNK), apoptosis ( BAX, BID, Bcl-2, APAF, CYCS) and oxidative stress ( SOD1, SOD2, CAT). Overall, C. calcitrans extracts demonstrated effective intervention against HepG2 cancer cells where enhanced apoptotic activities were observed with increased fucoxanthin content.

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          Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade.

          P. Li, D Nijhawan, I Budihardjo … (1997)
          We report here the purification of the third protein factor, Apaf-3, that participates in caspase-3 activation in vitro. Apaf-3 was identified as a member of the caspase family, caspase-9. Caspase-9 and Apaf-1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome c and dATP, an event that leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3. Depletion of caspase-9 from S-100 extracts diminished caspase-3 activation. Mutation of the active site of caspase-9 attenuated the activation of caspase-3 and cellular apoptotic response in vivo, indicating that caspase-9 is the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP.
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            Superoxide radical and superoxide dismutases.

            I Fridovich (1995)
            O2- oxidizes the [4Fe-4S] clusters of dehydratases, such as aconitase, causing-inactivation and release of Fe(II), which may then reduce H2O2 to OH- +OH.. SODs inhibit such HO. production by scavengingO2-, but Cu, ZnSODs, by virtue of a nonspecific peroxidase activity, may peroxidize spin trapping agents and thus give the appearance of catalyzing OH. production from H2O2. There is a glycosylated, tetrameric Cu, ZnSOD in the extracellular space that binds to acidic glycosamino-glycans. It minimizes the reaction of O2- with NO. E. coli, and other gram negative microorganisms, contain a periplasmic Cu, ZnSOD that may serve to protect against extracellular O2-. Mn(III) complexes of multidentate macrocyclic nitrogenous ligands catalyze the dismutation of O2- and are being explored as potential pharmaceutical agents. SOD-null mutants have been prepared to reveal the biological effects of O2-. SodA, sodB E. coli exhibit dioxygen-dependent auxotrophies and enhanced mutagenesis, reflecting O2(-)-sensitive biosynthetic pathways and DNA damage. Yeast, lacking either Cu, ZnSOD or MnSOD, are oxygen intolerant, and the double mutant was hypermutable and defective in sporulation and exhibited requirements for methionine and lysine. A Cu, ZnSOD-null Drosophila exhibited a shortened lifespan.
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              Triggering and modulation of apoptosis by oxidative stress.

              J. Chandra, A Samali, S Orrenius (2000)
              Cell survival requires multiple factors, including appropriate proportions of molecular oxygen and various antioxidants. Although most oxidative insults can be overcome by the cell's natural defenses, sustained perturbation of this balance may result in either apoptotic or necrotic cell death. Numerous, recent studies have shown that the mode of cell death that occurs depends on the severity of the insult. Oxidants and antioxidants can not only determine cell fate, but can also modulate the mode of cell death. Effects of oxidative stress on components of the apoptotic machinery may mediate this modulation. This review will address some of the current paradigms for oxidative stress and apoptosis, and discuss the potential mechanisms by which oxidants can modulate the apoptotic pathway.
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                Author and article information

                Contributors
                Fatimah Md. Yusoff
                Journal
                Journal ID (nlm-ta): Biotechnol Rep (Amst)
                Journal ID (iso-abbrev): Biotechnol Rep (Amst)
                Title: Biotechnology Reports
                Publisher: Elsevier
                ISSN (Electronic): 2215-017X
                Publication date PMC-release: 06 December 2018
                Publication date Collection: March 2019
                Publication date (Electronic): 06 December 2018
                Volume: 21
                Page: e00296
                Affiliations
                [a ]Institute of Bioscience, Universiti Putra Malaysia, 43400 UPM, Serdang, Selangor Darul Ehsan, Malaysia
                [b ]School of Science, Monash University Malaysia, Jalan Lagoon Selatan, 47500, Bandar Sunway, Selangor Darul Ehsan, Malaysia
                [c ]The International Institute of Aquaculture and Aquatic Science, Universiti Putra Malaysia, 43400, UPM, Serdang, Selangor Darul Ehsan, Malaysia
                [d ]Department of Aquaculture, Faculty of Agriculture, Universiti Putra Malaysia, 43400 UPM, Serdang, Selangor Darul Ehsan, Malaysia
                [e ]Department of Cell and Molecular Biology, Faculty of Biotechnology & Biomolecular Sciences, Universiti Putra Malaysia, 43400 UPM, Serdang, Selangor, Malaysia
                [f ]Department of Medical Biochemistry, College of Health Sciences, Usmanu Danfodio University, Sokoto, Nigeria
                [g ]School of Pharmacy, Faculty of Health & Medical Sciences, Taylor’s University, No. 1 Jalan Taylor's, 47500, Subang Jaya, Selangor Darul Ehsan, Malaysia
                [h ]School of Biosciences, Faculty of Health & Medical Sciences, Taylor’s University, No. 1 Jalan Taylor's, 47500, Subang Jaya, Selangor Darul Ehsan, Malaysia
                Author notes
                [* ]Corresponding author at: Institute of Bioscience, Universiti Putra Malaysia, 43400 UPM, Serdang, Selangor Darul Ehsan, Malaysia. fatimahyus@ 123456gmail.com
                Article
                Publisher ID: S2215-017X(18)30244-3 Publisher ID: e00296
                DOI: 10.1016/j.btre.2018.e00296
                PMC ID: 6296166
                SO-VID: 9395d79a-f738-4104-a546-2d3afac93089
                Copyright © © 2018 Published by Elsevier B.V.
                License:

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                Date received : 8 October 2018
                Date revision received : 14 November 2018
                Date accepted : 3 December 2018
                Categories
                Subject: Article

                Keywords: mtt, 3-(4,5-dimethylthizol-2-yl-2,5 diphenyltetrazolium bromide),rna, ribonucleic acid,dmso, dimethyl sulfoxide,cme, crude methanolic extract,fxrf, fucoxanthin rich fraction,pbs, phosphate buffered saline,mg fx.g−1 extract, milligram of fucoxanthin per gram of chaetoceros calcitrans extract,chaetoceros calcitrans,microalgae,fucoxanthin,rich fraction,apoptosis,gene expression
                Data availability:
                Keywords: mtt, 3-(4,5-dimethylthizol-2-yl-2,5 diphenyltetrazolium bromide), rna, ribonucleic acid, dmso, dimethyl sulfoxide, cme, crude methanolic extract, fxrf, fucoxanthin rich fraction, pbs, phosphate buffered saline, mg fx.g−1 extract, milligram of fucoxanthin per gram of chaetoceros calcitrans extract, chaetoceros calcitrans, microalgae, fucoxanthin, rich fraction, apoptosis, gene expression

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