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      Marine Drugs Regulating Apoptosis Induced by Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand (TRAIL)

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          Abstract

          Marine biomass diversity is a tremendous source of potential anticancer compounds. Several natural marine products have been described to restore tumor cell sensitivity to TNF-related apoptosis inducing ligand (TRAIL)-induced cell death. TRAIL is involved during tumor immune surveillance. Its selectivity for cancer cells has attracted much attention in oncology. This review aims at discussing the main mechanisms by which TRAIL signaling is regulated and presenting how marine bioactive compounds have been found, so far, to overcome TRAIL resistance in tumor cells.

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          Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes.

          Olivier Micheau, Jurg Tschopp (2003)
          Apoptosis induced by TNF-receptor I (TNFR1) is thought to proceed via recruitment of the adaptor FADD and caspase-8 to the receptor complex. TNFR1 signaling is also known to activate the transcription factor NF-kappa B and promote survival. The mechanism by which this decision between cell death and survival is arbitrated is not clear. We report that TNFR1-induced apoptosis involves two sequential signaling complexes. The initial plasma membrane bound complex (complex I) consists of TNFR1, the adaptor TRADD, the kinase RIP1, and TRAF2 and rapidly signals activation of NF-kappa B. In a second step, TRADD and RIP1 associate with FADD and caspase-8, forming a cytoplasmic complex (complex II). When NF-kappa B is activated by complex I, complex II harbors the caspase-8 inhibitor FLIP(L) and the cell survives. Thus, TNFR1-mediated-signal transduction includes a checkpoint, resulting in cell death (via complex II) in instances where the initial signal (via complex I, NF-kappa B) fails to be activated.
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            Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis.

            Honglin Li, Hong Zhu, Chi-jie Xu … (1998)
            We report here that BID, a BH3 domain-containing proapoptotic Bcl2 family member, is a specific proximal substrate of Casp8 in the Fas apoptotic signaling pathway. While full-length BID is localized in cytosol, truncated BID (tBID) translocates to mitochondria and thus transduces apoptotic signals from cytoplasmic membrane to mitochondria. tBID induces first the clustering of mitochondria around the nuclei and release of cytochrome c independent of caspase activity, and then the loss of mitochondrial membrane potential, cell shrinkage, and nuclear condensation in a caspase-dependent fashion. Coexpression of BclxL inhibits all the apoptotic changes induced by tBID. Our results indicate that BID is a mediator of mitochondrial damage induced by Casp8.
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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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                Author and article information

                Contributors
                Keith Glaser: Role: Academic Editor
                Journal
                Journal ID (nlm-ta): Mar Drugs
                Journal ID (iso-abbrev): Mar Drugs
                Journal ID (publisher-id): marinedrugs
                Title: Marine Drugs
                Publisher: MDPI
                ISSN (Electronic): 1660-3397
                Publication date (Electronic): 13 November 2015
                Publication date Collection: November 2015
                Volume: 13
                Issue: 11
                Pages: 6884-6909
                Affiliations
                [1 ]Department of Chemistry, Faculty of Science, Helwan University, Ain Helwan, Cairo 11790, Egypt; E-Mail: mohamed_almallah@ 123456science.helwan.edu.eg
                [2 ]Institut National de la Santé et de la Recherche Médicale, UMR866, Dijon F-21079, France
                [3 ]Unité de Formation et de Recherche, Science de Santé, Dijon F-21079, France
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: olivier.micheau@ 123456inserm.fr ; Tel.: +33-380-393-468; Fax: +33-380-393-434.
                Article
                Publisher ID: marinedrugs-13-06884
                DOI: 10.3390/md13116884
                PMC ID: 4663558
                PubMed ID: 26580630
                SO-VID: b906fd04-9b01-4d8a-bf03-c4ea3e8b5102
                Copyright © © 2015 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 21 September 2015
                Date accepted : 09 November 2015
                Categories
                Subject: Review

                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: tnf,trail,apoptosis,resistance,cancer,marine drugs,alkaloids,carotenoids,sesquiterpenes,macrolactones
                Data availability:
                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: tnf, trail, apoptosis, resistance, cancer, marine drugs, alkaloids, carotenoids, sesquiterpenes, macrolactones

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