Requirement of Caspase-3(-like) Protease-mediated Hydrogen Peroxide Production for Apoptosis Induced by Various Anticancer Drugs

Simizu, Siro; Takada, Minoru; Umezawa, Kazuo; Imoto, Masaya

doi:10.1074/jbc.273.41.26900

Cited by 261 publications

(162 citation statements)

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“…9 Through the action of cytosolic NADPH oxidase, active caspase-3 can also induce hydrogen peroxide and ROS production independent of mitochondria. 10 Finally, caspase-3 activation by gzmB seems to be a key factor for the exposure of phosphatidylserine (PS) on the cell surface, one of several 'eat-me' signals for effective phagocytosis of apoptotic vesicles 11 as well as for the cellular uptake of propidium iodide (PI) due to increased plasma membrane permeability. 6,8,12 Other caspases such as caspase-2, -6, -7, -8, -9 and -10 have been reported to serve as direct or indirect targets of gzmB, but may amplify/enhance rather than trigger CTL-mediated apoptosis.…”

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confidence: 99%

Granzyme B-induced cell death exerted by ex vivo CTL: discriminating requirements for cell death and some of its signs

et al. 2007

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Granzyme B (gzmB) of cytotoxic T lymphocytes (CTL) is essential for recovery from intracellular pathogens, but the molecular basis of its action is still unresolved. Here, we analyzed gzmB-mediated death pathways under physiological conditions using ex vivo virus-immune CTLs that express perf and gzmB, but not gzmA (gzmB þ CTL). We show that gzmB þ CTL abrogate target cell proliferation most likely by inducing cell death, independent of caspases and mitochondrial signaling. In addition, the data reveal that gzmB þ CTL independently induce pro-apoptotic processes either via caspase-3/-7, leading to plasma membrane perturbance and ROS production or via Bid/Bak/Bax, resulting in cytochrome c release and that both pathways elicit loss of DW m . Our data provide evidence for a pleiotropic pro-apoptotic function of gzmB presumably to counteract evasion strategies of pathogens and to control tumors.

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confidence: 99%

Granzyme B-induced cell death exerted by ex vivo CTL: discriminating requirements for cell death and some of its signs

et al. 2007

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“…ROS induce apoptotic signals in cancer cells and apoptosis induction by anticancer drugs and ␥-rays is closely associated with intracellular ROS generation. [1][2][3][4][5][6][7] Apoptotic signals are transduced mainly through 2 pathways, one of which is originates from the mitochondria and the other is the Fas-associated route. 8 -10 The release of the main mitochondrial proapoptotic protein, cytochrome c, is under the regulation of ROS.…”

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confidence: 99%

Tyrosine‐nitration of caspase 3 and cytochrome c does not suppress apoptosis induction in squamous cell carcinoma cells

Ueta

Kamatani

Yamamoto

et al. 2002

Intl Journal of Cancer

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The influence of tyrosine nitration of cytochrome c and caspase 3 on apoptosis induction was investigated in an established squamous carcinoma cell line, OSC-4. The intracellular NO and O 2 ؊ levels were increased up to about 110 -120% and 140 -180% of the control levels, respectively, after the treatment of OSC-4 cells with 5-FU (100 g/ml), PLM (10 g/ml), CDDP (10 g/ml), or ␥-rays (20 Gy). The treatment of OSC-4 cells with ONOO ؊ (1 mM) and the above anticancer agents induced tyrosine nitration of 14, 32 kDa protein among others and nitration of tyrosine residues of cytochrome c and caspase 3 was identified by the Western blotting of immunoprecipitates obtained by antibodies to these proapoptotic proteins. When cytochrome c and procaspase 3 were treated with ONOO ؊ , tyrosine nitration was increased in a ONOO ؊ -dose dependent manner. Tyrosine nitration of cleaved (17 kDa) Key words: tyrosine-nitration; caspase 3; cytochrome c; apoptosis; squamous cell carcinoma cells; anticancer agentsSuccessful anticancer therapy with chemicals and radiation strongly depends on the strategy for differentiation and apoptosis induction of cancer cells. ROS induce apoptotic signals in cancer cells and apoptosis induction by anticancer drugs and ␥-rays is closely associated with intracellular ROS generation. [1][2][3][4][5][6][7] Apoptotic signals are transduced mainly through 2 pathways, one of which is originates from the mitochondria and the other is the Fas-associated route. 8 -10 The release of the main mitochondrial proapoptotic protein, cytochrome c, is under the regulation of ROS. 11,12 In addition to the generation of ROS, NO is also generated in anticancer drug-and ␥-ray-treated cancer cells and reaction of ROS with NO is allowed in a favorable circumstance. 13,14 The reactant ONOO Ϫ vigorously damages cells by impairment of proteins and DNA. [15][16][17][18][19] Inactivation of the proapoptotic proteins by ONOO Ϫ is therefore probable in chemoradiotherapy of cancers although the apoptosis-inducing activity of ONOO Ϫ has been demonstrated in multiple kinds of cancer cells. 20,21 NO reacts with molecular oxygen (O 2 ), O 2 Ϫ and transitional metals, yielding nitrogen dioxide (NO 2 ), ONOO Ϫ and metalnitrosyl adducts, respectively. 22-24 These reactants are highly reactive and exhibit a variety of physiological activities. 25 In many disorders including inflammatory diseases, the neurotoxicity of stroke, Alzheimer's disease, Parkinson's disease and multiple sclerosis, the highly reactive nitrogen chemicals, especially ONOO Ϫ , are deeply associated with the pathological degeneration of the tissues although the half life of ONOO Ϫ is very short, less than one second in the physiological condition. 26,27 ONOO Ϫ has a potential to cause DNA-strand breaks, lipid peroxidation and diverse modification of cellular molecules such as oxidation of thiol and methionine and nitration of tyrosine and tryptophane. 28 In these modifications, tyrosine nitration has been extensively explored with the aim of analysis of the cytotoxic mec...

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“…Caspase-3, which can be activated by the initiator caspase-8 and caspase-9, as well as by the serine protease granzyme B, is a wellcharacterized typical executioner caspase involved in many proteolytic processes in apoptotic cells [25,26]. In particular, caspase-3 mediates the cleavage of proteins that are essential for cell stability, DNA repair and activation of Dnases [27][28][29]. Once cytosolic caspase-3 is activated, most cells are destined to die primarily by an apoptotic phenotype.…”

Section: Discussionmentioning

confidence: 99%

Is caspase inhibition a valid therapeutic strategy in cryopreservation of ovarian tissue?

Zhang

Yao

et al. 2009

J Assist Reprod Genet

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Purpose The aim of this study is to determine whether inclusion of caspase inhibitor can improve the efficacy of cryopreservation of ovarian tissue. Methods Mice were randomly assigned to the Group A (fresh control group) Group B (inclusion of caspase inhibitor) and Group C (non-inclusion of caspase inhibitor). Ovarian tissue in Group B and Group C was vitrifiedthawed. TUNEL assay and Bax protein detection were measured after cryopreservation. The mice in all groups received autotransplantation. The number of days before the resumption of estrous cycles was measured daily from the 5th day after surgery, and the percentage of cells expressing PCNA in grafts was measured one month following transplantation. Results The incidence of TUNEL positive follicles in Group B was significantly higher than that in Group C. Similarly, the percentage of follicles expressing Bax protein in Group B was significantly higher than that in Group C. The number of days before the resumption of estrous cycles in Group B was significantly less than that in Group C. In addition, the percentage of follicular and stromal cells expressing PCNA of grafts in Group B was significantly higher than that in Group C. ConclusionsThe global caspase inhibitor Z-VAD-FMK decreases the incidence of apoptosis of ovarian tissue induced by cryopreservation, and inclusion of caspase inhibitor improves the efficacy of cryopreservation of ovarian tissue.

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Requirement of Caspase-3(-like) Protease-mediated Hydrogen Peroxide Production for Apoptosis Induced by Various Anticancer Drugs

Cited by 261 publications

References 50 publications

Granzyme B-induced cell death exerted by ex vivo CTL: discriminating requirements for cell death and some of its signs

Granzyme B-induced cell death exerted by ex vivo CTL: discriminating requirements for cell death and some of its signs

Tyrosine‐nitration of caspase 3 and cytochrome c does not suppress apoptosis induction in squamous cell carcinoma cells

Is caspase inhibition a valid therapeutic strategy in cryopreservation of ovarian tissue?

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