Relevant bibliographies by topics / Caspase-3

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Academic literature on the topic 'Caspase-3'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 March 2023

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Journal articles on the topic "Caspase-3"

1

Slee, Elizabeth A., Mary T. Harte, Ruth M. Kluck, Beni B. Wolf, Carlos A. Casiano, Donald D. Newmeyer, Hong-Gang Wang, et al. "Ordering the Cytochrome c–initiated Caspase Cascade: Hierarchical Activation of Caspases-2, -3, -6, -7, -8, and -10 in a Caspase-9–dependent Manner." Journal of Cell Biology 144, no. 2 (January 25, 1999): 281–92. http://dx.doi.org/10.1083/jcb.144.2.281.

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Exit of cytochrome c from mitochondria into the cytosol has been implicated as an important step in apoptosis. In the cytosol, cytochrome c binds to the CED-4 homologue, Apaf-1, thereby triggering Apaf-1–mediated activation of caspase-9. Caspase-9 is thought to propagate the death signal by triggering other caspase activation events, the details of which remain obscure. Here, we report that six additional caspases (caspases-2, -3, -6, -7, -8, and -10) are processed in cell-free extracts in response to cytochrome c, and that three others (caspases-1, -4, and -5) failed to be activated under the same conditions. In vitro association assays confirmed that caspase-9 selectively bound to Apaf-1, whereas caspases-1, -2, -3, -6, -7, -8, and -10 did not. Depletion of caspase-9 from cell extracts abrogated cytochrome c–inducible activation of caspases-2, -3, -6, -7, -8, and -10, suggesting that caspase-9 is required for all of these downstream caspase activation events. Immunodepletion of caspases-3, -6, and -7 from cell extracts enabled us to order the sequence of caspase activation events downstream of caspase-9 and reveal the presence of a branched caspase cascade. Caspase-3 is required for the activation of four other caspases (-2, -6, -8, and -10) in this pathway and also participates in a feedback amplification loop involving caspase-9.
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Zhuang, Shougang, and Gabriel Simon. "Peroxynitrite-induced apoptosis involves activation of multiple caspases in HL-60 cells." American Journal of Physiology-Cell Physiology 279, no. 2 (August 1, 2000): C341—C351. http://dx.doi.org/10.1152/ajpcell.2000.279.2.c341.

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In this study, we show that caspases 2, 3, 6, and 7 were activated during peroxynitrite-induced apoptosis in human leukemia HL-60 cells and that processing of these caspases was accompanied by cleavage of poly(ADP-ribose) polymerase and lamin B. Treatment of cells with DEVD-fluoromethyl ketone (FMK), a selective inhibitor for caspase 3-like proteases, resulted in a marked diminution of apoptotic cells. VAVAD-FMK, an inhibitor of caspase 2, partially inhibited the apoptotic response to peroxynitrite. However, selective inactivation of caspase 6 by VEID-FMK did not affect apoptosis rates. These data suggest that caspase 3-like proteases and caspase 2, but not caspase 6, are required for peroxynitrite-induced apoptosis in this cell type. Moreover, we demonstrate that peroxynitrite treatment stimulated activation of caspases 8 and 9, two initial caspases in the apoptotic signaling pathway, and preincubation of cells with their inhibitor, IETD-FMK, inhibited activation of caspase 3-like proteases and caspase 2 at the concentration that prevents the apoptosis. These observations, together, suggest that caspase 8 and/or caspase 9 mediates activation of caspase 3-like proteases and caspase 2 during the apoptosis induced by peroxynitrite in HL-60 cells.
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Qin, Yimin, Terry L. Vanden Hoek, Kim Wojcik, Travis Anderson, Chang-Qing Li, Zuo-Hui Shao, Lance B. Becker, and Kimm J. Hamann. "Caspase-dependent cytochrome c release and cell death in chick cardiomyocytes after simulated ischemia-reperfusion." American Journal of Physiology-Heart and Circulatory Physiology 286, no. 6 (June 2004): H2280—H2286. http://dx.doi.org/10.1152/ajpheart.01063.2003.

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We recently demonstrated that reperfusion rapidly induces the mitochondrial pathway of apoptosis in chick cardiomyocytes after 1 h of simulated ischemia. Here we tested whether ischemia-reperfusion (I/R)-induced apoptosis could be initiated by caspase-dependent cytochrome c release in this model of cardiomyocyte injury. Fluorometric assays of caspase activity showed little, if any, activation of caspases above baseline levels induced by 1 h of ischemia alone. However, these assays revealed rapid activation of caspase-2, yielding a 2.95 ± 0.52-fold increase (over ischemia only) within the 1st h of reperfusion, whereas activities of caspases-3, -8, and -9 increased only slightly from their baseline levels. The rapid and prominent activation of caspase-2 suggested that it could be an important initiator caspase in this model, and using specific caspase inhibitors given only at the point of reperfusion, we tested this hypothesis. The caspase-2 inhibitor benzyloxycarbonyl-Val-Asp(Ome)-Val-Ala-Asp(Ome)-CH2F was the only caspase inhibitor that significantly inhibited cytochrome c release from mitochondria. This inhibitor also completely blocked activation of caspases-3, -8, and -9. The caspase-3/7 inhibitor transiently and only partially blocked caspase-2 activity and was less effective in blocking the activities of caspases-8 and -9. The caspase-8 inhibitor failed to significantly block caspase-2 or -3, and the caspase-9 inhibitor blocked only caspase-9. Furthermore, the caspase-2 inhibitor protected against I/R-induced cell death, but the caspase-8 inhibitor failed to do so. These data suggest that active caspase-2 initiates cytochrome c release after reperfusion and that it is critical for the I/R-induced apoptosis in this model.
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MEERGANS, Thomas, Ann-Kristin HILDEBRANDT, Daniel HORAK, Christina HAENISCH, and Albrecht WENDEL. "The short prodomain influences caspase-3 activation in HeLa cells." Biochemical Journal 349, no. 1 (June 26, 2000): 135–40. http://dx.doi.org/10.1042/bj3490135.

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Proteolytic activation of caspases is a key step in the process of apoptosis. According to their primary structure, caspases can be divided into a group with a long prodomain and a group with a short prodomain. Whereas long prodomains play a role in autocatalytic processing, little is known about the function of the short prodomain, for example the prodomain of caspase-3. We constructed caspase-3 variants lacking the prodomain and overexpressed these in HeLa and yeast cells. We found that removal of the caspase-3 prodomain resulted in spontaneous proteolytic activation of the protein when expressed in HeLa cells. This processing was only partially autocatalytic, as demonstrated by a catalytically inactive caspase-3 mutant. Co-expression of the anti-apoptotic protein XIAP (X-chromosome-linked inhibitor of apoptosis protein) completely blocked the observed spontaneous activation, which excluded a direct involvement of caspase-8. Our findings indicate that the short prodomain of caspase-3 serves as a silencing component in mammalian cells by retaining this executioner caspase in an inactive state.
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Rathbun, R. Keaney, Tracy A. Christianson, Gregory R. Faulkner, Gary Jones, Winifred Keeble, Michael O'Dwyer, and Grover C. Bagby. "Interferon-γ–induced apoptotic responses of Fanconi anemia group C hematopoietic progenitor cells involve caspase 8–dependent activation of caspase 3 family members." Blood 96, no. 13 (December 15, 2000): 4204–11. http://dx.doi.org/10.1182/blood.v96.13.4204.h8004204_4204_4211.

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Hematopoietic progenitor cells (HPC) from mice nullizygous at the Fanconi anemia (FA) group C locus and children with Fanconi anemia group C (FA-C) are hypersensitive to interferon-gamma (IFN-γ) and tumor necrosis factor-α. This hypersensitivity results, in part, from the capacity of these cytokines to prime the fas pathway. Because fas-mediated programmed cell death in many cells involves sequential activation of specific caspases, we tested the hypothesis that programmed cell death in FA HPC involves the ordered activation of specific caspase molecules. Lysates from lymphoblasts treated with both agonistic anti-fas antibody and IFN-γ contained activated caspase 3 family members (caspases 3, 6, and 7), as well as caspase 8, whereas activation of caspases 1, 2, 4, 9, and 10 was not detected. The apoptotic effects of fas agonists in IFN-γ-treated human and murine FA-C cells were blocked when pretreated with inhibitors (ac-DEVD-cho, CP-DEVD-cho, Z-DEVD-FMK) of the caspase 3 protease. Inhibitors (ac-YVAD-cho, CP-YVAD-cho, Z-YVAD-FMK) of caspase 1 did not block apoptosis or caspase 3 activation. Treatment of FA cells with the fluoromethyl ketone tetrapeptide caspase 8 inhibitor (ac-IETD-FMK) did suppress caspase 3 activation. A 4-fold greater fraction of IFN-induced FA-C cells expressed caspase 3 than FA-C cells complemented by retroviral-mediated transfer of FANCC. Therefore fas-induced apoptosis in Fanconi anemia cells of the C type involves the activation of caspase 8, which controls activation of caspase 3 family members and one direct or indirect function of the FANCC protein is to suppress apoptotic responses to IFN-γ upstream of caspase 3 activation.
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CAPANO, Michela, Sukaina VIRJI, and Martin CROMPTON. "Cyclophilin-A is involved in excitotoxin-induced caspase activation in rat neuronal B50 cells." Biochemical Journal 363, no. 1 (March 22, 2002): 29–36. http://dx.doi.org/10.1042/bj3630029.

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Glutamate and the NO donor, nitroprusside, synergistically induced the death of B50 cells from a rat CNS-derived neuroblastoma cell line. With low [nitroprusside] (10μM) both nitroprusside and glutamate were required. Under these conditions, nuclei became pyknotic and caspases were activated. The activities of caspase-3 and caspase-6 (effector caspases) were higher than those of caspase-8 and caspase-9 (initiator caspases). The activation of all four caspases was inhibited by cyclosporin A, with the order of susceptibility caspase-8=caspase-9=caspase-6>caspase-3. To identify the possible locus of cyclosporin A action, we used an antisense oligodeoxynucleotide to suppress the level of cyclophilin-A to < 5% of its control value. Cyclophilin-A suppression largely reproduced the inhibitory effects of cyclosporin A. These results provide the first indication that cyclophilin-A participates in the activation of the caspase cascade in neuronal cells, in particular in the form of cascade elicited by excitotoxic stimuli. It is concluded that neuroprotection by cyclosporin A against excitotoxin-induced apoptosis is, at least partly, due to inhibition of cyclophilin-A.
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Boatright, Kelly M., and Guy S. Salvesen. "Caspase activation." Biochemical Society Symposia 70 (September 1, 2003): 233–42. http://dx.doi.org/10.1042/bss0700233.

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Caspase activation is the 'point of no return' commitment to cell death. Synthesized as inactive zymogens, it is essential that the caspases remain inactive until the death signal is received. It is known for the downstream executioner caspases-3 and -7 that the activation event is proteolytic cleavage, and this had been assumed to apply to the initiator caspases as well. However, recent studies conducted on caspases-2, -8 and -9 have challenged this tenet of caspase activation. In this review we focus on the molecular details of caspase activation, with emphasis on recent work that provides a pleasing explanation for the differential requirements for the activation of executioner and initiator caspases.
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Fahy, Ruairi J., Andrea I. Doseff, and Mark D. Wewers. "Spontaneous Human Monocyte Apoptosis Utilizes a Caspase-3-Dependent Pathway That Is Blocked by Endotoxin and Is Independent of Caspase-1." Journal of Immunology 163, no. 4 (August 15, 1999): 1755–62. http://dx.doi.org/10.4049/jimmunol.163.4.1755.

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Abstract Apoptosis is an important mechanism for regulating the numbers of monocytes and macrophages. Caspases (cysteine-aspartate-specific proteases) are key molecules in apoptosis and require proteolytic removal of prodomains for activity. Caspase-1 and caspase-3 have both been connected to apoptosis in other model systems. The present study attempted to delineate what role these caspases play in spontaneous monocyte apoptosis. In serum-free conditions, monocytes showed a commitment to apoptosis as early as 4 h in culture, as evidenced by caspase-3-like activity. Apoptosis, as defined by oligonucleosomal DNA fragmentation, was prevented by a generalized caspase inhibitor, z-VAD-FMK, and the more specific caspase inhibitor, z-DEVD-FMK. The caspase activity was specifically attributable to caspase-3 by the identification of cleavage of procaspase-3 to active forms by immunoblots and by cleavage of the fluorogenic substrate DEVD-AFC. In contrast, a caspase-1 family inhibitor, YVAD-CMK, did not protect monocytes from apoptosis, and the fluorogenic substrate YVAD-AFC failed to show an increase in activity in apoptotic monocytes. When cultured with LPS (1 μg/ml), monocyte apoptosis was prevented, as was the activation of caspase-3. Unexpectedly, LPS did not change baseline caspase-1 activity. These findings link spontaneous monocyte apoptosis to the proteolytic activation of caspase-3.
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Rathbun, R. Keaney, Tracy A. Christianson, Gregory R. Faulkner, Gary Jones, Winifred Keeble, Michael O'Dwyer, and Grover C. Bagby. "Interferon-γ–induced apoptotic responses of Fanconi anemia group C hematopoietic progenitor cells involve caspase 8–dependent activation of caspase 3 family members." Blood 96, no. 13 (December 15, 2000): 4204–11. http://dx.doi.org/10.1182/blood.v96.13.4204.

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Abstract Hematopoietic progenitor cells (HPC) from mice nullizygous at the Fanconi anemia (FA) group C locus and children with Fanconi anemia group C (FA-C) are hypersensitive to interferon-gamma (IFN-γ) and tumor necrosis factor-α. This hypersensitivity results, in part, from the capacity of these cytokines to prime the fas pathway. Because fas-mediated programmed cell death in many cells involves sequential activation of specific caspases, we tested the hypothesis that programmed cell death in FA HPC involves the ordered activation of specific caspase molecules. Lysates from lymphoblasts treated with both agonistic anti-fas antibody and IFN-γ contained activated caspase 3 family members (caspases 3, 6, and 7), as well as caspase 8, whereas activation of caspases 1, 2, 4, 9, and 10 was not detected. The apoptotic effects of fas agonists in IFN-γ-treated human and murine FA-C cells were blocked when pretreated with inhibitors (ac-DEVD-cho, CP-DEVD-cho, Z-DEVD-FMK) of the caspase 3 protease. Inhibitors (ac-YVAD-cho, CP-YVAD-cho, Z-YVAD-FMK) of caspase 1 did not block apoptosis or caspase 3 activation. Treatment of FA cells with the fluoromethyl ketone tetrapeptide caspase 8 inhibitor (ac-IETD-FMK) did suppress caspase 3 activation. A 4-fold greater fraction of IFN-induced FA-C cells expressed caspase 3 than FA-C cells complemented by retroviral-mediated transfer of FANCC. Therefore fas-induced apoptosis in Fanconi anemia cells of the C type involves the activation of caspase 8, which controls activation of caspase 3 family members and one direct or indirect function of the FANCC protein is to suppress apoptotic responses to IFN-γ upstream of caspase 3 activation.
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Pu, Xuan, Sarah J. Storr, Yimin Zhang, Emad A. Rakha, Andrew R. Green, Ian O. Ellis, and Stewart G. Martin. "Caspase-3 and caspase-8 expression in breast cancer: caspase-3 is associated with survival." Apoptosis 22, no. 3 (October 31, 2016): 357–68. http://dx.doi.org/10.1007/s10495-016-1323-5.

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Dissertations / Theses on the topic "Caspase-3"

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Talebizadeh, Nooshin. "Caspase-3 in lens epithelium." Doctoral thesis, Uppsala universitet, Oftalmiatrik, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-267543.

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Purpose: To model the time evolution of active caspase-3 protein expression in a healthy lens, and in a lens exposed to UVR-300 nm (UVR-B). To develop an automated method to classify the fluorescent signal of biomarkers in the lens epithelial cells. Methods: Six-week old Sprague-Dawley rats were used. Firstly, expression of active caspase-3 was studied in the lens epithelium of healthy rats. Secondly, rats were unilaterally exposed in vivo to 1 kJ/m2 UVR-B for 15 minutes. At 0.5, 8, 16, and 24 hours after the UVR-B exposure, the exposed and the contralateral non-exposed lenses were removed. Immunohistochemistry was done on three mid-sagittal sections from each lens. The florescent labelling for active caspase-3 in each lens section was counted three times. The time evolution of active caspase-3 expression in response to UVR-B exposure was modelled as a function of cell position in the lens epithelium. An automated objective method was developed to quantify the lens epithelial cells and to classify the fluorescent signal of active caspase-3. Active caspase-3 was selected as a model signal. Results: Active caspase-3 was abundant in the anterior pole of the normal lenses. Spatial distribution of active caspase-3 labelling in the lens epithelium was fitted to a logistic model. The probability of active caspase-3 expression was higher in the UVR-B exposed lenses (95% CI = 0.12 ± 0.01). There was no difference in the expression of active caspase-3 between the 0.5 and the 24 hours groups or between the 8 and the 16 hours groups. A difference was noted, when comparing the 0.5 and 24 hours groups with the 8 and 16 hours groups (Test statistic 7.01, F1;36;0.95= 4.11). Exposure to UVR-B has an impact on the average probability of labelling for active caspase-3 as a function of cell position. The probability of labelling as a function of cell number also varied as a function of time after UVR-B exposure. The automated method counted the lens epithelial cells and estimated the proportion of active caspase-3 labelling in the lens epithelium. Conclusions: Active caspase-3 is present in the healthy lens epithelial cells. Active caspase-3 exhibits higher expression at the anterior pole of the lens and the expression decreases towards the periphery. After UVR-B exposure, the expression of active caspase-3 in the lens epithelium increases with a peak of expression occurring around 16 hours after exposure. The average probability of labelling in the lens epithelium is dependent on both the UVR-B exposure and the time period elapsed after the exposure. The automated method enables objective and fast quantification of lens epithelial cells and the expression of fluorescent signal in the lens cells.
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Shao, Wei 1970. "Identification of caspase-1 and caspase-3 substrates and study on caspase-1 substrates in glycolytic pathway." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=100248.

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Apoptosis is executed by caspase-mediated cleavage of various proteins. Elucidating the consequence of substrate cleavage provides us with insight into cell death and other biological processes. In this study, we applied the diagonal gel approach, a proteomic strategy, to identify substrates of the inflammatory caspase, caspase-1 and the cell death executioner caspase, caspase-3. Our results showed significant overlap between the substrates cleaved by both caspase-1 and -3. Such substrates are implicated in common cellular functions, including maintenance of the cytoskeleton, folding of proteins, translation, glycolysis, bioenergetics, signaling and trafficking. An important finding is that many glycolysis enzymes were targeted specifically by caspase-1. Processing of these glycolysis enzymes by caspase-1 was confirmed by cleaving in vitro transcribed and translated substrates with recombinant caspase-1. We have focused our further analysis on certain glycolysis enzymes. We have characterized the caspase-1 cleavage site in GAPDH. Point mutation of the Aspartic acid at position 189 to Alanine (D189A) in GAPDH blocked its cleavage by caspase-1. In vivo, in a mice model of septic shock, characterized by hyperactivation of caspase-1, we observed depletion of the full-length forms of these glycolysis enzymes in the diaphragm muscle. Further studies in caspase-1 deficient mice will confirm whether this depletion, in caspase-1 proficient mice, was due to caspase-1 processing of the glycolysis enzymes. This provides a direct link between caspase-1 activation and inhibition of glycolysis, which might have important implications on loss of muscle contractility in septic shock.
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Voss, Oliver H. "Regulation of Cell Fate by Caspase-3." The Ohio State University, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=osu1281536983.

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Woo, Minna. "Understanding the role of caspase-3 in vivo." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/NQ58614.pdf.

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Riedl, Stefan. "Röntgenstrukturanalyse der Caspase-3-XIAP-BIR2, Caspase-7-XIAP-BIR2-Komplexe und der Procaspase-7." [S.l.] : [s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=964905426.

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Larsen, Brian D. "Role of Caspase 3/Caspase Activated DNase induced DNA Strand Breaks during Skeletal Muscle Differentiation." Thèse, Université d'Ottawa / University of Ottawa, 2012. http://hdl.handle.net/10393/20709.

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Cell fate decisions incorporate distinct and overlapping mechanisms. The activity of caspase 3 was initially understood to be a cell death restricted event, however numerous studies have implicated this enzyme in the regulation of both differentiation and proliferation. How the activity of caspase 3 promotes a non-death cell fate remains unclear. Here we examine the role caspase 3 activity plays during skeletal muscle differentiation; in particular we explore the hypothesis that the mechanism of inducing DNA strand breaks during cell death is also a key feature of differentiation, albeit with a distinctly different outcome. We delineate the transient formation of Caspase 3/Caspase activated DNase (CAD) dependent DNA strand breaks during differentiation. The formation of these breaks is essential for differentiation and the regulation of specific genes. In particular expression of the cell cycle inhibitor p21 is related to the formation of a DNA strand break within the gene’s promoter element. Further, we explored the genome wide association of CAD using Chromatin Immunoprecipitation coupled to high through put sequencing (ChIP-seq). This approach identified a potential role for Caspase3/CAD in regulating the expression of Pax7. Here, a CAD directed DNA strand break in the Pax7 gene is correlated with decreased Pax7 expression, an outcome that has been shown to be critical for progress of the myogenic differentiation program. The regulation of Pax7 expression through a CAD induced DNA strand break raises an intriguing connection between this regulation and oncogenic transformation observed in alveolar rhabdomyosarcoma. The putative site of CAD induced DNA strand breaks that promote decreased Pax7 expression during differentiation corresponds to site of chromosomal translocations responsible for Pax7 fusion events in alveolar rhabdomyosarcoma.
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Jahani-asl, Arezu. "Influence of phosphorylation on caspase-3-mediated Akt1 cleavage." Thesis, University of Ottawa (Canada), 2005. http://hdl.handle.net/10393/26931.

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Caspase-3, an executioner of apoptosis, is negatively regulated by X-linked inhibitor of apoptosis protein (XIAP), a determinant of cisplatin resistance. XIAP down-regulation in ovarian cancer cells or treatment with cisplatin induces caspase-3-mediated AKT cleavage and apoptosis, while XIAP over-expression suppresses this cleavage and increases phospho-AKT content. The identity of the caspase-3 cleavage site(s) in AM and the possible dependence of caspase-3-mediated cleavage on its phosphorylation status are unknown. The objectives of this thesis were to determine the caspase-3 cleavage site(s) in Akt1 and to examine the influence of phosphorylation on Akt1 cleavage in vitro. Our results suggested presence of three non-consensus (EEEE 117, EEMD119, DAKE398) and one consensus (DQDD456) cleavage sites, and posphorylation of Akt1 influenced the pattern of cleavage in a site-specific manner: Whereas cleavage at site "EEEE117" was facilitated by phosphorylation, that at sites "EEMD119 and DAKE398'' were attenuated. The biological significance of these observations requires future investigation.
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Turner, Claire. "The role of caspase-3 in drug-induced apoptosis." Thesis, University of Nottingham, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342127.

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Beiche, Alexandra. "Expression von Caspasen in Kopf-Hals-Tumoren - immunhistochemischer Nachweis von Caspase 1, 2, 3 und Proliferationsmarker Ki67." Ulm : Universität Ulm, Medizinische Fakultät, 2000. http://www.bsz-bw.de/cgi-bin/xvms.cgi?SWB9186905.

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Benetone, Maria Zilah. "Apoptose e proliferação na placenta de búfalas." Universidade de São Paulo, 2005. http://www.teses.usp.br/teses/disponiveis/10/10132/tde-23062006-182309/.

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A apoptose é um processo fisiológico que desempenha papel crucial no desenvolvimento, remodelagem e senescência teciduais, inclusive placentários. A placenta, enquanto órgão temporário, atravessa todas estas fases em aproximadamente 10 meses, na espécie bubalina. O crescimento da placenta e a nutrição fetal requerem altas taxas de renovação e diferenciação celulares, e a maturação placentária está relacionada à redução das células epiteliais das criptas carunculares maternas. As modificações morfológicas celulares decorrentes do processo de apoptose são fruto de eventos bioquímicos complexos promovidos por uma família de cisteína-proteases, as caspases, especialmente as caspases executoras, dentre as quais se destaca a caspase-3, capaz de degradar várias proteínas citoplasmáticas e nucleares. Durante a apoptose, ocorre a clivagem caspase-mediada da citoqueratina 18, proteína dos filamentos intermediários do citoesqueleto, e com isso a formação de um neoepítopo específico. Por meio de métodos imunoistoquímicos pode-se detectar a presença tanto deste neoepítopo, quanto da forma ativa da caspase-3, o que demonstra que a célula entrou em estágio irreversível de morte celular. Morfologicamente, algumas das principais alterações celulares observadas são condensação da cromatina, a degradação e fragmentação do DNA, a formação de ?blebs? (pregas/bolhas) na membrana plasmática, além da fragmentação celular em corpúsculos apoptóticos, os quais podem ser identificados em cortes corados pelo método de rotina hematoxilina e eosina, utilizando-se microscópio de imunofluorescência, devido à eosinofluorescência das células em apoptose. Assim como a apoptose, a proliferação celular participa no equilíbrio homeostático tissular. Neste estudo, pretende-se avaliar a ocorrência de apoptose e proliferação celular em 42 placentônios de diferentes animais em diversas fases gestacionais (2-10 meses de gestação), em tecidos fixados em 4% paraformoldeído, incluídos em paraplast e submetidos à imunoistoquímica (anticorpo monoclonal M30 CytoDeath; Caspase-3 Clivada; PCNA - antígeno de marcação nuclear), sendo também avaliada a presença de corpúsculos apoptóticos eosinofluorescentes nas amostras. Utilizando-se M30 e caspase-3 clivada pudemos constatar a ocorrência de apoptose nos epitélios uterino e trofoblástico, em células gigantes placentárias e, ocasionalmente, em células mesenquimais fetais, do estroma uterino e endoteliais. Não houve diferenças significativas (p<0.05) entre os métodos adotados, mas sim entre os estágios gestacionais. Para o M30, houve um aumento significante da apoptose do primeiro grupo (2-4.5 meses) em relação ao quarto grupo (9-10 meses); no caso da Caspase-3 Clivada houve um aumento estatísticamente significante (p<0.05) entre os três primeiros grupos (2-4.5; 5-6.5; e 7-8.5 meses de gestação, respectivamente) de animais em relação ao quarto grupo. Para o PCNA, ocorreu uma diminuição no número de células em proliferação dos dois primeiros grupos de animais em relação ao quarto grupo (p<0.05). A presença de corpúsculos apoptóticos eosinofluorescentes pôde ser observada em todas as amostras. Nossos resultados sugerem haver uma relação entre a ocorrência de apoptose e a maturação, senescência e liberação placentárias em ruminantes.
Apoptosis is a physiological process that plays a crucial role in the development, remodeling and aging of the placenta. The placenta is a temporary organ that undergoes growth and development, followed by senescence and death in 10 months in the buffalo species. Placental growth and fetal nutrition require high rates of cellular turnover and differentiation, and placental maturation is correlated to the reduction of the number of epithelial cells of the maternal crypts. The morphological changes of the apoptotic cells are product of complex variety of biochemical events promoted by a family of cystein-proteases, the caspases, mainly the effectors caspases, and among them the caspase-3, which is able to degrade cytoplasmic and nuclear proteins. During apoptosis, the caspase-mediated cleavage of cytokeratin 18, which is one of the first intermediate filament proteins of the cytoskeleton, leads to the formation of a specific neo-epitope. It is possible to detect the presence of this neo-epitope by immunohistochemistry, as well as the active form of caspase-3, showing that the cell has entered an irreversible stage of cell death. Morphologically, some of the main observed cellular alterations are condensation of the chromatin, degradation and spalling of the DNA, blebbing of the cell membrane and the formation of apoptotic bodies. These bodies can be identified in slides stained by hematoxilin and eosin with a fluorescent microscope, due to the eosinofluorescent property of the apoptotic cells. Like apoptosis, cellular proliferation also contributes to the tissue homeostasis. In the present study, we intend to evaluate the occurrence of apoptosis and cellular proliferation in 42 placentomes, collected from different animals in several gestacional phases (2-10 months of gestation), fixed in 4% paraformaldehyde, processed for embedding in paraplast and cut in sections, through immunohistochemistry (monoclonal antibody M30 CytoDeath; Cleaved Caspase-3; PCNA - antigen of nuclear proliferation). The presence of eosinofluorescent apoptotic bodies were also studied in the samples. M30 and Cleaved Caspase-3 allowed to show the occurrence of apoptosis in the uterine and trophoblastic ephitelium, in placental giant cells and, occasionally, in the fetal mesenquimal cells, in the uterine stroma and endothelium cells. There were no significant differences (p<0.05) between the adopted methods, although there were differences between the gestational phases studied. For M30, there was an increase of the number of apoptotic cells (p<0.05) from the first group (2-4.5 months) in relation to the fourth group of animals (9-10 months); for the Cleaved Caspase-3 there was a statistical significant increase (p<0.05) between the first three groups of animals (2-4.5; 5-6.5; and 7-8.5 months of gestation, respectively) and the last one. In relation to the PCNA, a decrease in the number of proliferative cells occurred from the first two groups of animals to the fourth group (p<0.05). The occurrence of eosinofluorescent apoptotic bodies was observed in all the samples studied . Our data suggest a relationship between apoptosis and the maturation, senescence and release of the ruminant placenta.
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Books on the topic "Caspase-3"

1

Liadis, Nicole. The role of caspase-3 in regulating neurotrophic and NMDA-dependent PCD in the mammalian CNS in vivo. Ottawa: National Library of Canada, 2001.

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Bennett, Lunawati L. Caspase-3: Structure, Functions and Interactions. Nova Science Publishers, Incorporated, 2020.

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Bennett, Lunawati L. Caspase-3: Structure, Functions and Interactions. Nova Science Publishers, Incorporated, 2020.

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Woo, Minna. Understanding the role of caspase-3 in vivo. 2001.

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Bushell, Martin. The caspase-3 dependent cleavage of eIF4G during the induction of apoptosis. 2000.

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Pollett, Jonathan Barclay. Caspase-3, a novel therapeutic approach to the treatment of multiple myeloma. 2004.

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Book chapters on the topic "Caspase-3"

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Kavanagh, Edel. "Quantification of Active Caspase-3 and Active Caspase-8 in Microglia Cells." In Microglia, 113–20. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-520-0_13.

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Fox, Richard, and Martine Aubert. "Flow Cytometric Detection of Activated Caspase-3." In Apoptosis and Cancer, 47–56. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-339-4_5.

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Mazumder, Suparna, Dragos Plesca, and Alexandru Almasan. "Caspase-3 Activation is a Critical Determinant of Genotoxic Stress-Induced Apoptosis." In Apoptosis and Cancer, 13–21. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-339-4_2.

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Choudhary, Gaurav S., Sayer Al-harbi, and Alexandru Almasan. "Caspase-3 Activation Is a Critical Determinant of Genotoxic Stress-Induced Apoptosis." In Methods in Molecular Biology, 1–9. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1661-0_1.

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Dohi, Kenji, H. Ohtaki, R. Inn, Y. Ikeda, H. S. Shioda, and T. Aruga. "Peroxynitrite and caspase-3 expression after ischemia/reperfusion in mouse cardiac arrest model." In Brain Edema XII, 87–91. Vienna: Springer Vienna, 2003. http://dx.doi.org/10.1007/978-3-7091-0651-8_20.

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Leibowitz, Julian L., and Elena Belyavskaya. "Caspase Inhibitors Block MHV-3 Induced Apoptosis and Enhance Viral Replication and Pathogenicity." In Advances in Experimental Medicine and Biology, 109–14. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1325-4_17.

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Tanaka, Sakae, Hidetoshi Wakeyama, Toru Akiyama, Katsuhiko Takahashi, Hitoshi Amano, Keiichi I. Nakayama, and Kozo Nakamura. "Regulation of Osteoclast Apoptosis by Bcl-2 Family Protein Bim and Caspase-3." In Advances in Experimental Medicine and Biology, 111–16. Boston, MA: Springer US, 2009. http://dx.doi.org/10.1007/978-1-4419-1050-9_12.

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Alasia, Silvia, Carolina Cocito, Adalberto Merighi, and Laura Lossi. "Real-Time Visualization of Caspase-3 Activation by Fluorescence Resonance Energy Transfer (FRET)." In Methods in Molecular Biology, 99–113. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-2152-2_8.

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Seng, Wen Lin, Dawei Zhang, and Patricia McGrath. "Microplate-Based Whole Zebrafish Caspase 3/7 Assay for Screening Small Molecule Compounds." In Methods in Pharmacology and Toxicology, 193–209. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3588-8_11.

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Chen, J., and R. P. Simon. "The Role of Caspase-3-like Protease in the Hippocampus After Transient Global lschemia." In Maturation Phenomenon in Cerebral Ischemia III, 41–46. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-58602-6_5.

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Conference papers on the topic "Caspase-3"

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İlhan, A., M. E. Derin, I. Karadağ, H. O. Doğan, A. C. Urhan, M. Şahin, and A. Şahin. "AB0049 Evaluation of caspase-3, caspase-9, caspase-14 and pannexin-1 levels in behÇet’s disease." In Annual European Congress of Rheumatology, EULAR 2018, Amsterdam, 13–16 June 2018. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-eular.3897.

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Liu, Xiaoqiu, and James S. Hagood. "Thy-1 Expression Promotes Fibroblast Susceptibility To Apoptosis Via Fas-, Caspase 8- And Caspase 3- Dependent Mechanisms." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a3490.

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Wu, Dan, Hongye Dan, Huan Liu, Peng Yu, and Yuou Teng. "Fast establishment and application of caspase-3 inhibitor detection system." In 3rd International Conference on Material, Mechanical and Manufacturing Engineering (IC3ME 2015). Paris, France: Atlantis Press, 2015. http://dx.doi.org/10.2991/ic3me-15.2015.109.

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Guzikowski, Anthony P., Christina Shipp, Rachel A. Howard, Rod C. Schutte, Michael R. Braden, and John J. Naleway. "Cyclic peptidase substrates for fluorescent analysis of Caspase 3 enzyme activity." In BiOS 2000 The International Symposium on Biomedical Optics, edited by Gerald E. Cohn. SPIE, 2000. http://dx.doi.org/10.1117/12.382040.

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Del Rosario, O. L., A. P. Shah, S. Reuven, L. Servinsky, K. Suresh, V. Yun, J. Huetsch, et al. "MK2 Phosphorylates Caspase-3 Facilitating Its Nuclear Translocation and Promoting Apoptosis." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a5398.

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Nelson, W. B., Ashley J. Smuder, Matthew B. Hudson, and Scott Powers. "Calpain And Caspase-3 Contribute To Mechanical Ventilation-Induced Diaphragmatic Weakness." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a6612.

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Crowder, Roslyn N., David T. Dicker, and Wafik S. El-Deiry. "Abstract 4095: Decreased caspase 8 protein expression and incomplete caspase 3 activation in TRAIL-resistant normal human fibroblasts and epithelial cells." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4095.

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Fuchs, Y., Y. Yosefzon, D. Soteriou, L. Kostic, E. Koren, E. Sedov, and F. Glaser. "SPOT-002 Caspase-3 regulates YAP-dependent organ size and tumour development." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.36.

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Shah, A., S. Reuven, O. L. Del Rosario, L. Servinsky, K. Suresh, J. Huetsch, V. Yun, L. A. Shimoda, and M. Damarla. "Caspase-3 Promotes Migration and Proliferation During Recovery of Endothelial Barrier Function." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a7847.

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Damarla, Mahendra, Bo Kim, Tiffany Simms, Hemang Yadav, Allen C. Myers, Sekhar P. Reddy, Rachel L. Damico, and Paul M. Hassoun. "Phosphorylation Of HSP27 Potentiates Caspase 3 Activation In Response To Mechanical Stress." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2661.

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Reports on the topic "Caspase-3"

1

Hansen, Peter J., and Amir Arav. Embryo transfer as a tool for improving fertility of heat-stressed dairy cattle. United States Department of Agriculture, September 2007. http://dx.doi.org/10.32747/2007.7587730.bard.

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Abstract:
The overall objective of the current proposal is to develop procedures to improve the pregnancy rate achieved following transfer of fresh or cryopreserved embryos produced in the laboratory into heat-stress recipients. The overall hypothesis is that pregnancy rate in heat-stressed lactating cows can be improved by use of embryo transfer and that additional gains in pregnancy rate can be achieved through development of procedures to cryopreserve embryos, select embryos most likely to establish and maintain pregnancy after transfer, and to enhance embryo competence for post-transfer survival through manipulation of culture conditions. The original specific objectives were to 1) optimize procedures for cryopreservation (Israel/US), 2) develop procedures for identifying embryos with the greatest potential for development and survival using the remote monitoring system called EmbryoGuard (Israel), 3) perform field trials to test the efficacy of cryopreservation and the EmbryoGuard selection system for improving pregnancy rates in heat-stressed, lactating cows (US/Israel), 4) test whether selection of fresh or frozen-thawed blastocysts based on measurement of group II caspase activity is an effective means of increasing survival after cryopreservation and post-transfer pregnancy rate (US), and 5) identify genes in blastocysts induced by insulin-like growth factor-1 (IGF-1) (US). In addition to these objectives, additional work was carried out to determine additional cellular determinants of embryonic resistance to heat shock. There were several major achievements. Results of one experiment indicated that survival of embryos to freezing could be improved by treating embryos with cytochalasin B to disrupt the cytoskeleton. An additional improvement in the efficacy of embryo transfer for achieving pregnancy in heat-stressed cows follows from the finding that IGF-1 can improve post-transfer survival of in vitro produced embryos in the summer but not winter. Expression of several genes in the blastocyst was regulated by IGF-1 including IGF binding protein-3, desmocollin II, Na/K ATPase, Bax, heat shock protein 70 and IGF-1 receptor. These genes are likely candidates 1) for developing assays for selection of embryos for transfer and 2) as marker genes for improving culture conditions for embryo production. The fact that IGF-1 improved survival of embryos in heat-stressed recipients only is consistent with the hypothesis that IGF-1 confers cellular thermotolerance to bovine embryos. Other experiments confirmed this action of IGF-1. One action of IGF-1, the ability to block heat-shock induced apoptosis, was shown to be mediated through activation of the phosphatidylinositol 3-kinase pathway. Other cellular determinants of resistance of embryos to elevated temperature were identified including redox status of the embryo and the ceramide signaling pathway. Developmental changes in embryonic apoptosis responses in response to heat shock were described and found to include alterations in the capacity of the embryo to undergo caspase-9 and caspase-3 activation as well as events downstream from caspase-3 activation. With the exception of IGF-1, other possible treatments to improve pregnancy rate to embryo transfer were not effective including selection of embryos for caspase activity, treatment of recipients with GnRH.and bilateral transfer of twin embryos. In conclusion, accomplishments achieved during the grant period have resulted in methods for improving post-transfer survival of in vitro produced embryos transferred into heat-stressed cows and have lead to additional avenues for research to increase embryo resistance to elevated temperature and improve survival to cryopreservation. In addition, embryo transfer of vitrified IVF embryos increased significantly the pregnancy rate in repeated breeder cows.
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