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      Call for Papers: Green Renal Replacement Therapy: Caring for the Environment

      Submit here before July 31, 2024

      About Blood Purification: 3.0 Impact Factor I 5.6 CiteScore I 0.83 Scimago Journal & Country Rank (SJR)

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      Comparative analysis of caspase activation and apoptosis in renal tubular epithelial cells and renal cell carcinomas.

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          Treatment of renal cell carcinoma (RCC) is limited by its resistance to conventional chemotherapies. This may occur, in part, from resistance to apoptosis. The role of caspase activation in apoptosis resistance in treated RCCs was investigated.

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          Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization.

          X Opitz-Araya, Patrice Lassus, Yuri Lazebnik (2002)
          A current view is that cytotoxic stress, such as DNA damage, induces apoptosis by regulating the permeability of mitochondria. Mitochondria sequester several proteins that, if released, kill by activating caspases, the proteases that disassemble the cell. Cytokines activate caspases in a different way, by assembling receptor complexes that activate caspases directly; in this case, the subsequent mitochondrial permeabilization accelerates cell disassembly by amplifying caspase activity. We found that cytotoxic stress causes activation of caspase-2, and that this caspase is required for the permeabilization of mitochondria. Therefore, we argue that cytokine-induced and stress-induced apoptosis act through conceptually similar pathways in which mitochondria are amplifiers of caspase activity rather than initiators of caspase activation.
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            Bcl-2 family: Life-or-death switch

            Yoshihide Tsujimoto, Shigeomi Shimizu (2000)
            The Bcl-2 family of proteins that consists of anti-apoptotic and pro-apoptotic members determines life-or-death of a cell by controlling the release of mitochondrial apoptogenic factors, cytochrome c and apoptosis-inducing factor (AIF), that activate downstream executional phases, including the activation of death proteases called caspases. Cytochrome c release is, thus, central to apoptotic signal transduction in mammals, making study of the mechanism for cytochrome c release a major issue. Several models for cytochrome c release have been proposed, including rupture of mitochondrial outer membrane and involvement of a specific channel. Here, we provide an overview of recent findings on the role of Bcl-2 family members in the life-or-death decision of a cell.
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              AMID, an apoptosis-inducing factor-homologous mitochondrion-associated protein, induces caspase-independent apoptosis.

              Xin-Min Wu, Zhonghe Zhai, Xiaoyan Li … (2002)
              Apoptosis-inducing factor (AIF) is a mitochondrial flavoprotein that triggers caspase-independent apoptosis. We describe here the cloning and characterization of a novel AIF-homologous molecule designated AMID (AIF-homologous mitochondrion-associated inducer of death). AMID lacks a mitochondrial localization sequence but shares significant homology with AIF and NADH oxidoreductases from bacteria to mammalian species. Immunofluorescent staining and biochemical experiments indicated that AMID was co-localized with mitochondria. Overexpression of AMID induced cell death with characteristic apoptotic morphology. Furthermore, AMID-induced apoptosis was independent of caspase activation and p53 and was not inhibited by Bcl-2. These findings suggest that AMID induces a novel caspase-independent apoptotic pathway.
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                Author and article information

                Journal
                Journal ID (iso-abbrev): Nephron Exp. Nephrol.
                Title: Nephron. Experimental nephrology
                Publisher: S. Karger AG
                ISSN (Electronic): 1660-2129
                ISSN (Print): 1660-2129
                Publication date (Electronic): 2005
                Volume: 99
                Issue: 4
                Affiliations
                [1 ] Molecular and Cellular Pathology, School of Medicine, University of Queensland, Herston, Australia.
                Article
                Publisher Item ID: 83926
                DOI: 10.1159/000083926
                PubMed ID: 15711100
                SO-VID: 72273832-65d2-4cc8-870a-1a88137ba6b6
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