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      Role of Smac/DIABLO in cancer progression

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          Abstract

          Second mitochondria-derived activator of caspase/direct inhibitor of apoptosis-binding protein with low pI (Smac/DIABLO) is a proapoptogenic mitochondrial protein that is released to the cytosol in response to diverse apoptotic stimuli, including commonly used chemotherapeutic drugs. In the cytosol, Smac/DIABLO interacts and antagonizes inhibitors of apoptosis proteins (IAPs), thus allowing the activation of caspases and apoptosis. This activity has prompted the synthesis of peptidomimetics that could potentially be used in cancer therapy. For these reasons, several authors have analyzed the expression levels of Smac/DIABLO in samples of patients from different tumors. Although dissimilar results have been found, a tissue-specific role of this protein emerges from the data. The objective of this review is to present the current knowledge of the Smac/DIABLO role in cancer and its possible use as a marker or therapeutic target for drug design.

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          IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis.

          James Vince, W Wei-Lynn Wong, Nufail Khan … (2007)
          XIAP prevents apoptosis by binding to and inhibiting caspases, and this inhibition can be relieved by IAP antagonists, such as Smac/DIABLO. IAP antagonist compounds (IACs) have therefore been designed to inhibit XIAP to kill tumor cells. Because XIAP inhibits postmitochondrial caspases, caspase 8 inhibitors should not block killing by IACs. Instead, we show that apoptosis caused by an IAC is blocked by the caspase 8 inhibitor crmA and that IAP antagonists activate NF-kappaB signaling via inhibtion of cIAP1. In sensitive tumor lines, IAP antagonist induced NF-kappaB-stimulated production of TNFalpha that killed cells in an autocrine fashion. Inhibition of NF-kappaB reduced TNFalpha production, and blocking NF-kappaB activation or TNFalpha allowed tumor cells to survive IAC-induced apoptosis. Cells treated with an IAC, or those in which cIAP1 was deleted, became sensitive to apoptosis induced by exogenous TNFalpha, suggesting novel uses of these compounds in treating cancer.
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            Cell death in development.

            David L Vaux, Stanley Korsmeyer (1999)
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              An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9.

              H. Zou, Y. Li, X. Liu … (1999)
              We report here the reconstitution of the de novo procaspase-9 activation pathway using highly purified cytochrome c, recombinant APAF-1, and recombinant procaspase-9. APAF-1 binds and hydrolyzes ATP or dATP to ADP or dADP, respectively. The hydrolysis of ATP/dATP and the binding of cytochrome c promote APAF-1 oligomerization, forming a large multimeric APAF-1.cytochrome c complex. Such a complex can be isolated using gel filtration chromatography and is by itself sufficient to recruit and activate procaspase-9. The stoichiometric ratio of procaspase-9 to APAF-1 is approximately 1 to 1 in the complex. Once activated, caspase-9 disassociates from the complex and becomes available to cleave and activate downstream caspases such as caspase-3.
              Article 0 comments Cited 218 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): J Exp Clin Cancer Res
                Title: Journal of Experimental & Clinical Cancer Research : CR
                Publisher: BioMed Central
                ISSN (Print): 0392-9078
                ISSN (Electronic): 1756-9966
                Publication date Collection: 2008
                Publication date (Electronic): 26 September 2008
                Volume: 27
                Issue: 1
                Page: 48
                Affiliations
                [1 ]Functional Cancer Genomics Laboratory, National Institute of Genomic Medicine, Periferico Sur 4124, Torre Zafiro II 5to piso, Col. Ex-Rancho de Anzaldo, Alvaro Obregon 01900, Mexico City, México
                [2 ]Molecular Biology Laboratory, Subdireccion de Investigacion Basica, Instituto Nacional de Cancerologia, Mexico City, 14000, México
                [3 ]Medical Proteomics unit, National Institute of Genomic Medicine, Mexico City, 01900, México
                Article
                Publisher ID: 1756-9966-27-48
                DOI: 10.1186/1756-9966-27-48
                PMC ID: 2566557
                PubMed ID: 18822137
                SO-VID: f7e6630b-40dd-4a21-85d5-d9d041701f2b
                Copyright © Copyright © 2008 Martinez-Ruiz et al; licensee BioMed Central Ltd.
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 14 August 2008
                Date accepted : 26 September 2008
                Categories
                Subject: Review

                ScienceOpen disciplines: Oncology & Radiotherapy
                Data availability:
                ScienceOpen disciplines: Oncology & Radiotherapy

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