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Journal articles on the topic 'Caspase-3'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 June 2025

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1

Slee, Elizabeth A., Mary T. Harte, Ruth M. Kluck, 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 (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

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2

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 (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

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3

Qin, Yimin, Terry L. Vanden Hoek, Kim Wojcik, et al. "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 (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

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4

Rathbun, R. Keaney, Tracy A. Christianson, Gregory R. Faulkner та ін. "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, № 13 (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

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5

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 (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 lo

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6

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 (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 oli

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7

Rathbun, R. Keaney, Tracy A. Christianson, Gregory R. Faulkner та ін. "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, № 13 (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 tre

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8

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 (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 expr

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9

Demirci, Umut, Melek Yaman, and Umit E. Bagriacik. "Effects of acute doxorubicin exposure on caspase-mediated apoptosis in cardiomyocytes." Journal of Clinical Oncology 31, no. 15_suppl (2013): e12036-e12036. http://dx.doi.org/10.1200/jco.2013.31.15_suppl.e12036.

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e12036 Background: Doxorubicin binds to DNA-associated enzymes, intercalates the base pairs of the DNA and induces apoptosis in cancerous and healthy tissues especially in cardiomyocytes. Caspase mediated apoptosis in cardiomyocytes remains largely unknown. We investigated the role of doxorubicin via caspase system on apoptosis of cardiomyocytes. Methods: H9C2ratcardiomyocytes were incubated with doxorubicin a concentration of 10-6 Mfor 4 or 24 hours to perform gene expression and activity of caspases, respectively. Total RNA isolated and expression analysis were performed by real time PCR ass

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10

Su, Ching-Chyuan, Cheng-Chia Yu, Yi-Wen Shih, et al. "Protective Effect of Alpha-Linolenic Acid on Human Oral Squamous Cell Carcinoma Metastasis and Apoptotic Cell Death." Nutrients 15, no. 23 (2023): 4992. http://dx.doi.org/10.3390/nu15234992.

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Oral cancer ranks sixth among Taiwan’s top 10 cancers and most patients with poor prognosis acquire metastases. The essential fatty acid alpha-linolenic acid (ALA) has been found to diminish many cancer properties. However, the anti-cancer activity of ALA in oral cancer has yet to be determined. We examined the mechanisms underlying ALA inhibition of metastasis and induction of apoptotic cell death in oral squamous cell carcinoma (OSCC). Migration and invasion assays confirmed the cancer cells’ EMT capabilities, whereas flow cytometry and Western blotting identified molecular pathways in OSCC.

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11

Heilig, Rosalie, Marisa Dilucca, Dave Boucher, et al. "Caspase-1 cleaves Bid to release mitochondrial SMAC and drive secondary necrosis in the absence of GSDMD." Life Science Alliance 3, no. 6 (2020): e202000735. http://dx.doi.org/10.26508/lsa.202000735.

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Caspase-1 drives a lytic inflammatory cell death named pyroptosis by cleaving the pore-forming cell death executor gasdermin-D (GSDMD). Gsdmd deficiency, however, only delays cell lysis, indicating that caspase-1 controls alternative cell death pathways. Here, we show that in the absence of GSDMD, caspase-1 activates apoptotic initiator and executioner caspases and triggers a rapid progression into secondary necrosis. GSDMD-independent cell death required direct caspase-1–driven truncation of Bid and generation of caspase-3 p19/p12 by either caspase-8 or caspase-9. tBid-induced mitochondrial o

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12

Campbell, Douglas S., and Hitoshi Okamoto. "Local caspase activation interacts with Slit-Robo signaling to restrict axonal arborization." Journal of Cell Biology 203, no. 4 (2013): 657–72. http://dx.doi.org/10.1083/jcb.201303072.

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In addition to being critical for apoptosis, components of the apoptotic pathway, such as caspases, are involved in other physiological processes in many types of cells, including neurons. However, very little is known about their role in dynamic, nonphysically destructive processes, such as axonal arborization and synaptogenesis. We show that caspases were locally active in vivo at the branch points of young, dynamic retinal ganglion cell axonal arbors but not in the cell body or in stable mature arbors. Caspase activation, dependent on Caspase-3, Caspase-9, and p38 mitogen-activated protein

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13

Wolf, Beni B., Joshua C. Goldstein, Henning R. Stennicke, et al. "Calpain Functions in a Caspase-Independent Manner to Promote Apoptosis-Like Events During Platelet Activation." Blood 94, no. 5 (1999): 1683–92. http://dx.doi.org/10.1182/blood.v94.5.1683.

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Abstract Apoptosis and platelet activation share common morphological and biochemical features. Because caspases are essential mediators of apoptosis, we examined whether platelets contain these proteinases and use them during platelet activation. Human platelets contained caspase-9, caspase-3, and the caspase activators APAF-1 and cytochrome c as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting. Upon treatment with cytochrome c and dATP, platelet cytoplasmic extracts recapitulated apoptotic events, including sequential activation of procaspase-9 and proc

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14

Wolf, Beni B., Joshua C. Goldstein, Henning R. Stennicke, et al. "Calpain Functions in a Caspase-Independent Manner to Promote Apoptosis-Like Events During Platelet Activation." Blood 94, no. 5 (1999): 1683–92. http://dx.doi.org/10.1182/blood.v94.5.1683.417k37_1683_1692.

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Apoptosis and platelet activation share common morphological and biochemical features. Because caspases are essential mediators of apoptosis, we examined whether platelets contain these proteinases and use them during platelet activation. Human platelets contained caspase-9, caspase-3, and the caspase activators APAF-1 and cytochrome c as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting. Upon treatment with cytochrome c and dATP, platelet cytoplasmic extracts recapitulated apoptotic events, including sequential activation of procaspase-9 and procaspase-3

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15

Fennell, Myles, Helen Chan, and Andrew Wood. "Multiparameter Measurement of Caspase 3 Activation and Apoptotic Cell Death in NT2 Neuronal Precursor Cells Using High-Content Analysis." Journal of Biomolecular Screening 11, no. 3 (2006): 296–302. http://dx.doi.org/10.1177/1087057105284618.

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Caspase activation is a component of a number of neurodegenerative disorders, including stroke. In this study, the authors describe a multiplexed assay for caspase 3 activation, nuclear condensation, and cell viability in a neuronal precursor cell line Ntera-2, injuredwith staurosporine and etoposide. Using a high-content screening approach, cells were identified by staining with the nuclear stain Hoechst 33342; cell viability wasmeasured by staining cells with YoPro-1, which is taken up by damaged cells but excluded from healthy cells; and caspase 3/7 activation was detected using the cell-pe

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16

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

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17

MacFarlane, Marion, Wendy Merrison, David Dinsdale, and Gerald M. Cohen. "Active Caspases and Cleaved Cytokeratins Are Sequestered into Cytoplasmic Inclusions in Trail-Induced Apoptosis." Journal of Cell Biology 148, no. 6 (2000): 1239–54. http://dx.doi.org/10.1083/jcb.148.6.1239.

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Tumor necrosis factor–related apoptosis- inducing ligand (TRAIL) –induced apoptosis, in transformed human breast epithelial MCF-7 cells, resulted in a time-dependent activation of the initiator caspases-8 and -9 and the effector caspase-7. Cleavage of caspase-8 and its preferred substrate, Bid, preceded processing of caspases-7 and -9, indicating that caspase-8 is the apical initiator caspase in TRAIL-induced apoptosis. Using transient transfection of COOH-terminal–tagged green fluorescent protein fusion constructs, caspases-3, -7, and -8 were localized throughout the cytoplasm of MCF-7 cells.

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18

Wang, J., and M. J. Lenardo. "Roles of caspases in apoptosis, development, and cytokine maturation revealed by homozygous gene deficiencies." Journal of Cell Science 113, no. 5 (2000): 753–57. http://dx.doi.org/10.1242/jcs.113.5.753.

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Caspases are a group of cysteine proteases critical for apoptosis of eukaryotic cells. Deletion of genes that encode murine caspases suggests that caspases are involved not only in apoptosis but also in cytokine maturation and cell growth and differentiation. Among them, caspase-1 and caspase-11 are primarily involved in the processing of pro-inflammatory cytokines. Caspase-3 and caspase-9 are essential for apoptosis during brain development. Caspase-8 is required for the development of heart muscle, cell proliferation in the hematopoietic lineage and death-receptor-mediated apoptosis. These s

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19

Hirata, Hirokazu, Atsushi Takahashi, Susumu Kobayashi, et al. "Caspases Are Activated in a Branched Protease Cascade and Control Distinct Downstream Processes in Fas-induced Apoptosis." Journal of Experimental Medicine 187, no. 4 (1998): 587–600. http://dx.doi.org/10.1084/jem.187.4.587.

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Two novel synthetic tetrapeptides, VEID-CHO and DMQD-CHO, could selectively inhibit caspase-6 and caspase-3, respectively. We used these inhibitors to dissect the pathway of caspase activation in Fas-stimulated Jurkat cells and identify the roles of each active caspase in apoptotic processes. Affinity labeling techniques revealed a branched protease cascade in which caspase-8 activates caspase-3 and -7, and caspase-3, in turn, activates caspase-6. Both caspase-6 and -3 have major roles in nuclear apoptosis. Caspase-6 cleaves nuclear mitotic apparatus protein (NuMA) and mediates the shrinkage a

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20

Takemoto, Kiwamu, Takeharu Nagai, Atsushi Miyawaki, and Masayuki Miura. "Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects." Journal of Cell Biology 160, no. 2 (2003): 235–43. http://dx.doi.org/10.1083/jcb.200207111.

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Indicator molecules for caspase-3 activation have been reported that use fluorescence resonance energy transfer (FRET) between an enhanced cyan fluorescent protein (the donor) and enhanced yellow fluorescent protein (EYFP; the acceptor). Because EYFP is highly sensitive to proton (H+) and chloride ion (Cl−) levels, which can change during apoptosis, this indicator's ability to trace the precise dynamics of caspase activation is limited, especially in vivo. Here, we generated an H+- and Cl−-insensitive indicator for caspase activation, SCAT, in which EYFP was replaced with Venus, and monitored

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21

Mannick, Joan B., Christopher Schonhoff, Natalia Papeta, et al. "S-Nitrosylation of mitochondrial caspases." Journal of Cell Biology 154, no. 6 (2001): 1111–16. http://dx.doi.org/10.1083/jcb.200104008.

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Caspase-3 is a cysteine protease located in both the cytoplasm and mitochondrial intermembrane space that is a central effector of many apoptotic pathways. In resting cells, a subset of caspase-3 zymogens is S-nitrosylated at the active site cysteine, inhibiting enzyme activity. During Fas-induced apoptosis, caspases are denitrosylated, allowing the catalytic site to function. In the current studies, we sought to identify the subpopulation of caspases that is regulated by S-nitrosylation. We report that the majority of mitochondrial, but not cytoplasmic, caspase-3 zymogens contain this inhibit

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22

Duval, R., V. Bellet, S. Delebassée, and C. Bosgiraud. "Implication of caspases during maedi–visna virus-induced apoptosis." Journal of General Virology 83, no. 12 (2002): 3153–61. http://dx.doi.org/10.1099/0022-1317-83-12-3153.

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Maedi–visna virus (MVV) causes encephalitis, pneumonia and arthritis in sheep. In vitro, MVV infection and replication lead to strong cytopathic effects characterized by syncytia formation and subsequent cellular lysis. It was demonstrated previously that MVV infection in vitro induces cell death of sheep choroid plexus cells (SCPC) by a mechanism that can be associated with apoptotic cell death. Here, the relative implication of several caspases during acute infection with MVV is investigated by employing diverse in vitro and in situ strategies. It was demonstrated using specific pairs of cas

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Faleiro, Lavina, and Yuri Lazebnik. "Caspases Disrupt the Nuclear-Cytoplasmic Barrier." Journal of Cell Biology 151, no. 5 (2000): 951–60. http://dx.doi.org/10.1083/jcb.151.5.951.

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During apoptosis, caspases, a family of proteases, disassemble a cell by cleaving a set of proteins. Caspase-3 plays a major role in the disassembly of the nucleus by processing several nuclear substrates. The question is how caspase-3, which is usually cytoplasmic, gains access to its nuclear targets. It was suggested that caspase-3 is actively transported to the nucleus through the nuclear pores. We found that caspase-9, which is activated earlier than caspase-3, directly or indirectly inactivates nuclear transport and increases the diffusion limit of the nuclear pores. This increase allows

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Suresh, Karthik, Kathleen Carino, Laura Johnston, et al. "A nonapoptotic endothelial barrier-protective role for caspase-3." American Journal of Physiology-Lung Cellular and Molecular Physiology 316, no. 6 (2019): L1118—L1126. http://dx.doi.org/10.1152/ajplung.00487.2018.

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Noncanonical roles for caspase-3 are emerging in the fields of cancer and developmental biology. However, little is known of nonapoptotic functions of caspase-3 in most cell types. We have recently demonstrated a disassociation between caspase-3 activation and execution of apoptosis with accompanying cytoplasmic caspase-3 sequestration and preserved endothelial barrier function. Therefore, we tested the hypothesis that nonapoptotic caspase-3 activation promotes endothelial barrier integrity. Human lung microvascular endothelial cells were exposed to thrombin, a nonapoptotic stimulus, and endot

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Kang, Shin-Jung, Suyue Wang, Hideaki Hara, et al. "Dual Role of Caspase-11 in Mediating Activation of Caspase-1 and Caspase-3 under Pathological Conditions." Journal of Cell Biology 149, no. 3 (2000): 613–22. http://dx.doi.org/10.1083/jcb.149.3.613.

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Caspase-11, a member of the murine caspase family, has been shown to be an upstream activator of caspase-1 in regulating cytokine maturation. We demonstrate here that in addition to its defect in cytokine maturation, caspase-11–deficient mice have a reduced number of apoptotic cells and a defect in caspase-3 activation after middle cerebral artery occlusion (MCAO), a mouse model of stroke. Recombinant procaspase-11 can autoprocess itself in vitro. Purified active recombinant caspase-11 cleaves and activates procaspase-3 very efficiently. Using a positional scanning combinatorial library method

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26

McComb, Scott, Pik Ki Chan, Anna Guinot, et al. "Efficient apoptosis requires feedback amplification of upstream apoptotic signals by effector caspase-3 or -7." Science Advances 5, no. 7 (2019): eaau9433. http://dx.doi.org/10.1126/sciadv.aau9433.

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Apoptosis is a complex multi-step process driven by caspase-dependent proteolytic cleavage cascades. Dysregulation of apoptosis promotes tumorigenesis and limits the efficacy of chemotherapy. To assess the complex interactions among caspases during apoptosis, we disrupted caspase-8, -9, -3, -7, or -6 and combinations thereof, using CRISPR-based genome editing in living human leukemia cells. While loss of apical initiator caspase-8 or -9 partially blocked extrinsic or intrinsic apoptosis, respectively, only combined loss of caspase-3 and -7 fully inhibited both apoptotic pathways, with no disce

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27

EDELSTEIN, CHARLES L., YUEXIAN SHI, and ROBERT W. SCHRIER. "Role of Caspases in Hypoxia-Induced Necrosis of Rat Renal Proximal Tubules." Journal of the American Society of Nephrology 10, no. 9 (1999): 1940–49. http://dx.doi.org/10.1681/asn.v1091940.

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Abstract. The role of the caspases, a newly discovered group of cysteine proteases, was investigated in a model of hypoxia-induced necrotic injury of rat renal proximal tubules. An assay for caspases in freshly isolated rat proximal tubules was developed. There was a 40% increase in tubular caspase activity after 15 min of hypoxia in association with increased cell membrane damage as indicated by a threefold increase in lactate dehydrogenase release. The specific caspase inhibitor Z-Asp-2,6-dichlorobenzoyloxymethylketone (Z-D-DCB) attenuated the increase in caspase activity during 15 min of hy

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Komoriya, Akira, Beverly Z. Packard, Martin J. Brown, Ming-Lei Wu, and Pierre A. Henkart. "Assessment of Caspase Activities in Intact Apoptotic Thymocytes Using Cell-Permeable Fluorogenic Caspase Substrates." Journal of Experimental Medicine 191, no. 11 (2000): 1819–28. http://dx.doi.org/10.1084/jem.191.11.1819.

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To detect caspase activities in intact apoptotic cells at the single cell level, cell-permeable fluorogenic caspase substrates were synthesized incorporating the optimal peptide recognition motifs for caspases 1, 3/7, 6, 8, and 9. Caspase activities were then assessed at various times after in vitro treatment of mouse thymocytes with dexamethasone or anti-Fas antibody. Dexamethasone induced the following order of appearance of caspase activities as judged by flow cytometry: LEHDase, WEHDase, VEIDase, IETDase, and DEVDase. Since the relative order of caspases 3 (DEVDase) and 6 (VEIDase) in the

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Nowak, Grażyna, Peter M. Price, and Rick G. Schnellmann. "Lack of a functional p21WAF1/CIP1 gene accelerates caspase-independent apoptosis induced by cisplatin in renal cells." American Journal of Physiology-Renal Physiology 285, no. 3 (2003): F440—F450. http://dx.doi.org/10.1152/ajprenal.00233.2002.

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The lack of cyclin-dependent kinase inhibitor p21WAF1/CIP1 (p21) in mice increases renal proximal tubular cell death and enhances sensitivity to acute renal failure produced by the chemotherapeutic agent cisplatin. We used primary cultures of mouse renal proximal tubular cells (MPTC) grown in optimized culture conditions to investigate the cellular basis for increased apoptosis in p21 knockout mice. Cisplatin (15 μM) activated caspase-3 but not caspase-8 or caspase-9 and produced phosphatidylserine externalization, chromatin condensation, and nuclear fragmentation in wild-type [p21(+/+)] MPTC.

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Dursun, Belda, Zhibin He, Hilary Somerset, Dong-Jin Oh, Sarah Faubel, and Charles L. Edelstein. "Caspases and calpain are independent mediators of cisplatin-induced endothelial cell necrosis." American Journal of Physiology-Renal Physiology 291, no. 3 (2006): F578—F587. http://dx.doi.org/10.1152/ajprenal.00455.2005.

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The role of caspases and calpain in cisplatin-induced endothelial cell death is unknown. Thus we investigated whether caspases and calpain are mediators of cisplatin-induced apoptosis and necrosis in endothelial cells. Cultured pancreatic microvascular endothelial (MS1) cells were exposed to 10 and 50 μM cisplatin. Apoptosis or necrosis was determined by Hoechst 33342 and propidium iodide (PI) nuclear staining. Cells treated with 10 μM cisplatin had normal ATP levels, increased caspase-3-like activity, excluded PI and demonstrated morphological characteristics of apoptosis at 24 h. Cells treat

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Talanian, Robert V., XiaoHe Yang, Jane Turbov, et al. "Granule-mediated Killing: Pathways for Granzyme B–initiated Apoptosis." Journal of Experimental Medicine 186, no. 8 (1997): 1323–31. http://dx.doi.org/10.1084/jem.186.8.1323.

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We report that the serine protease granzyme B (GrB), which is crucial for granule-mediated cell killing, initiates apoptosis in target cells by first maturing caspase-10. In addition, GrB has a limited capacity to mature other caspases and to cause cell death independently of the caspases. Compared with other members, GrB in vitro most efficiently processes caspase-7 and -10. In a human cell model, full maturation of caspase-7 does not occur unless caspase-10 is present. Furthermore, GrB matured caspase-3 with less efficiency than caspase-7 or caspase-10. With the caspases fully inactivated by

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Pu, Xuan, Sarah J. Storr, Yimin Zhang, et al. "Caspase-3 and caspase-8 expression in breast cancer: caspase-3 is associated with survival." Apoptosis 22, no. 3 (2016): 357–68. http://dx.doi.org/10.1007/s10495-016-1323-5.

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ANNAND, Robert R., Jeffrey R. DAHLEN, Cindy A. SPRECHER та ін. "Caspase-1 (interleukin-1β-converting enzyme) is inhibited by the human serpin analogue proteinase inhibitor 9". Biochemical Journal 342, № 3 (1999): 655–65. http://dx.doi.org/10.1042/bj3420655.

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The regulation of caspases, cysteine proteinases that cleave their substrates after aspartic residues, is poorly understood, even though they are involved in tightly regulated cellular processes. The recently discovered serpin analogue proteinase inhibitor 9 (PI9) is unique among human serpin analogues in that it has an acidic residue in the putative specificity-determining position of the reactive-site loop. We measured the ability of PI9 to inhibit the amidolytic activity of several caspases. The hydrolysis of peptide substrates by caspase-1 (interleukin-1β-converting enzyme), caspase-4 and

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Kamada, Shinji, Ushio Kikkawa, Yoshihide Tsujimoto, and Tony Hunter. "A-Kinase-Anchoring Protein 95 Functions as a Potential Carrier for the Nuclear Translocation of Active Caspase 3 through an Enzyme-Substrate-Like Association." Molecular and Cellular Biology 25, no. 21 (2005): 9469–77. http://dx.doi.org/10.1128/mcb.25.21.9469-9477.2005.

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ABSTRACT Caspase-mediated proteolysis is a critical and central element of the apoptotic process, and caspase 3, one of the effector caspases, is proposed to play essential roles in the nuclear morphological changes of apoptotic cells. Although many substrates for caspase 3 localize in the nucleus and caspase 3 translocates from the cytoplasm to the nuclei after activation in apoptotic cells, the molecular mechanisms of nuclear translocation of active caspase 3 have been unclear. Recently, we suggested that a substrate-like protein(s) served as a carrier to transport caspase 3 from the cytopla

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Hernandez, Ambrosio, Xiang Y. Xue, Alex Westerband, Lois A. Killewich, and Glenn C. Hunter. "TRAIL Mediated Apoptosis Increases Carotid Plaque Vulnerability." Stroke 32, suppl_1 (2001): 360. http://dx.doi.org/10.1161/str.32.suppl_1.360-a.

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P116 Background: TRAIL, a TNF family protein, and its receptors DR 4 and 5 (TNF-R) are known to induce apoptosis in tumor cells via caspase activation. In this study, we examined the relationship between TRAIL, its effector caspases and apoptosis in carotid plaque (CP). Materials and Methods: Forty CPs were examined by immunohistochemistry, Western blotting and RNA protection assay for evidence of apoptosis (Tunel), TRAIL, caspase 3, 8 and PARP. We compared the expression of these pro-apoptotic proteins within plaque (P), and in areas of intimal thickening (IT) adjacent to the plaque to that o

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Zheng, Timothy S., Stéphane Hunot, Keisuke Kuida, et al. "Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation." Nature Medicine 6, no. 11 (2000): 1241–47. http://dx.doi.org/10.1038/81343.

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Lu, Ying, and Guo-Qiang Chen. "Effector Caspases and Leukemia." International Journal of Cell Biology 2011 (2011): 1–8. http://dx.doi.org/10.1155/2011/738301.

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Caspases, a family of aspartate-specific cysteine proteases, play a major role in apoptosis and a variety of physiological and pathological processes. Fourteen mammalian caspases have been identified and can be divided into two groups: inflammatory caspases and apoptotic caspases. Based on the structure and function, the apoptotic caspases are further grouped into initiator/apical caspases (caspase-2, -8, -9, and -10) and effector/executioner caspases (caspase-3, -6, and -7). In this paper, we discuss what we have learned about the role of individual effector caspase in mediating both apoptoti

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Ekert, Paul G., John Silke, Christine J. Hawkins, Anne M. Verhagen, and David L. Vaux. "Diablo Promotes Apoptosis by Removing Miha/Xiap from Processed Caspase 9." Journal of Cell Biology 152, no. 3 (2001): 483–90. http://dx.doi.org/10.1083/jcb.152.3.483.

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MIHA is an inhibitor of apoptosis protein (IAP) that can inhibit cell death by direct interaction with caspases, the effector proteases of apoptosis. DIABLO is a mammalian protein that can bind to IAPs and antagonize their antiapoptotic effect, a function analogous to that of the proapoptotic Drosophila molecules, Grim, Reaper, and HID. Here, we show that after UV radiation, MIHA prevented apoptosis by inhibiting caspase 9 and caspase 3 activation. Unlike Bcl-2, MIHA functioned after release of cytochrome c and DIABLO from the mitochondria and was able to bind to both processed caspase 9 and p

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Sgorbissa, A., R. Benetti, S. Marzinotto, C. Schneider, and C. Brancolini. "Caspase-3 and caspase-7 but not caspase-6 cleave Gas2 in vitro: implications for microfilament reorganization during apoptosis." Journal of Cell Science 112, no. 23 (1999): 4475–82. http://dx.doi.org/10.1242/jcs.112.23.4475.

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Apoptosis is characterized by proteolysis of specific cellular proteins by a family of cystein proteases known as caspases. Gas2, a component of the microfilament system, is cleaved during apoptosis and the cleaved form specifically regulates microfilaments and cell shape changes. We now demonstrate that Gas2 is a substrate of caspase-3 but not of caspase-6. Proteolytic processing both in vitro and in vivo is dependent on aspartic residue 279. Gas2 cleavage was only partially impaired in apoptotic MCF-7 cells which lack caspase-3, thus indicating that different caspases can process Gas2 in viv

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Renema, Phoibe, Natalya Kozhukhar, Viktoriya Pastukh, et al. "Exoenzyme Y induces extracellular active caspase-7 accumulation independent from apoptosis: modulation of transmissible cytotoxicity." American Journal of Physiology-Lung Cellular and Molecular Physiology 319, no. 2 (2020): L380—L390. http://dx.doi.org/10.1152/ajplung.00508.2019.

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Caspase-3 and -7 are executioner caspases whose enzymatic activity is necessary to complete apoptotic cell death. Here, we questioned whether endothelial cell infection leads to caspase-3/7-mediated cell death. Pulmonary microvascular endothelial cells (PMVECs) were infected with Pseudomonas aeruginosa (PA103). PA103 caused cell swelling with a granular appearance, paralleled by intracellular caspase-3/7 activation and cell death. In contrast, PMVEC infection with ExoY+ (PA103 Δ exoUexoT::Tc pUCP exoY) caused cell rounding, but it did not activate intracellular caspase-3/7 and it did not cause

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COHEN, Gerald M. "Caspases: the executioners of apoptosis." Biochemical Journal 326, no. 1 (1997): 1–16. http://dx.doi.org/10.1042/bj3260001.

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Apoptosis is a major form of cell death, characterized initially by a series of stereotypic morphological changes. In the nematode Caenorhabditis elegans, the gene ced-3 encodes a protein required for developmental cell death. Since the recognition that CED-3 has sequence identity with the mammalian cysteine protease interleukin-1β-converting enzyme (ICE), a family of at least 10 related cysteine proteases has been identified. These proteins are characterized by almost absolute specificity for aspartic acid in the P1 position. All the caspases (ICE-like proteases) contain a conserved QACXG (wh

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Wilkins, Nikhil, Timothy Stephens, and Laura Felix. "EXTH-49. BXQ-350 TARGETS TO THE LYSOSOME AND KILLS GLIOBLASTOMA (GBM) CELLS VIA ACTIVATION OF APOPTOTIC CASPASES IN VITRO." Neuro-Oncology 22, Supplement_2 (2020): ii97—ii98. http://dx.doi.org/10.1093/neuonc/noaa215.403.

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Abstract BACKGROUND Apoptosis is a programmed cell death mechanism where cells respond to internal or external stimuli by initiating a cascade of events and enzymes leading to cell death. One of the hallmarks of cancer is the ability to resist apoptotic stimuli. Removing resistances to apoptosis can result in the death of these tumor cells. METHOD The GBM cell line Gli36ΔEGFR was used to determine Caspase activity and BXQ-350 cytotoxicity. Cells were treated with 9uM to 30uM BXQ-350 in triplicate and incubated for 24 hours at 37oC. Promega’s Caspase-Glo 9 or Caspase-Glo 3/7 reagent was added t

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Peluffo, Marina C., Richard L. Stouffer, and Marta Tesone. "Activity and expression of different members of the caspase family in the rat corpus luteum during pregnancy and postpartum." American Journal of Physiology-Endocrinology and Metabolism 293, no. 5 (2007): E1215—E1223. http://dx.doi.org/10.1152/ajpendo.00261.2007.

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Studies were designed to examine the expression and activity of four caspases that contribute to the initial (caspases-2, -8, and -9) and final (caspase-3) events in apoptosis in the rat corpus luteum (CL) during pregnancy ( days 7, 17, 19, and 21 of gestation), postpartum ( days 1 and 4), and after injection (0, 8, 16, 24, and 36 h) of the physiological luteolysin PGF2α. In addition, the temporal relationship of caspase expression/activity relative to steroid production and luteal regression was evaluated. During pregnancy, the activity of all four caspases was significantly greater on day 19

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Ge, Y., Y.-M. Cai, L. Bonneau, et al. "Inhibition of cathepsin B by caspase-3 inhibitors blocks programmed cell death in Arabidopsis." Cell Death & Differentiation 23, no. 9 (2016): 1493–501. http://dx.doi.org/10.1038/cdd.2016.34.

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Abstract Programmed cell death (PCD) is used by plants for development and survival to biotic and abiotic stresses. The role of caspases in PCD is well established in animal cells. Over the past 15 years, the importance of caspase-3-like enzymatic activity for plant PCD completion has been widely documented despite the absence of caspase orthologues. In particular, caspase-3 inhibitors blocked nearly all plant PCD tested. Here, we affinity-purified a plant caspase-3-like activity using a biotin-labelled caspase-3 inhibitor and identified Arabidopsis thaliana cathepsin B3 (AtCathB3) by liquid c

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Denault, Jean-Bernard, Brendan P. Eckelman, Hwain Shin, Cristina Pop, and Guy S. Salvesen. "Caspase 3 attenuates XIAP (X-linked inhibitor of apoptosis protein)–mediated inhibition of caspase 9." Biochemical Journal 405, no. 1 (2007): 11–19. http://dx.doi.org/10.1042/bj20070288.

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During apoptosis, the initiator caspase 9 is activated at the apoptosome after which it activates the executioner caspases 3 and 7 by proteolysis. During this process, caspase 9 is cleaved by caspase 3 at Asp330, and it is often inferred that this proteolytic event represents a feedback amplification loop to accelerate apoptosis. However, there is substantial evidence that proteolysis per se does not activate caspase 9, so an alternative mechanism for amplification must be considered. Cleavage at Asp330 removes a short peptide motif that allows caspase 9 to interact with IAPs (inhibitors of ap

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Brad, Amber M., Katherine E. M. Hendricks, and Peter J. Hansen. "The block to apoptosis in bovine two-cell embryos involves inhibition of caspase-9 activation and caspase-mediated DNA damage." Reproduction 134, no. 6 (2007): 789–97. http://dx.doi.org/10.1530/rep-07-0146.

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The capacity of the preimplantation embryo to undergo apoptosis in response to external stimuli is developmentally regulated. Acquisition of apoptosis does not occur in the cow embryo until between the 8- and 16-cell stages. The purpose of the present experiments was to determine the mechanism by which apoptosis is blocked in the bovine two-cell embryo. Heat shock (41 °C for 15 h) did not increase activity of caspase-9 or group II caspases (caspase-2, -3, and -7) in two-cell embryos but did in day 5 embryos. Exposure of embryos to carbonyl cyanide 3-chlorophenylhydrazone (CCCP) to depolarize m

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Cao, Guodong, Yumin Luo, Tetsuya Nagayama, et al. "Cloning and Characterization of Rat Caspase-9: Implications for a Role in Mediating Caspase-3 Activation and Hippocampal Cell Death after Transient Cerebral Ischemia." Journal of Cerebral Blood Flow & Metabolism 22, no. 5 (2002): 534–46. http://dx.doi.org/10.1097/00004647-200205000-00005.

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Delayed hippocampal neurodegeneration after transient global ischemia is mediated, at least in part, through the activation of terminal caspases, particularly caspase-3, and the subsequent proteolytic degradation of critical cellular proteins. Caspase-3 may be activated by the membrane receptor-initiated caspase-8–dependent extrinsic pathway and the mitochondria-initiated caspase-9–dependent intrinsic pathway; however, the precise role of these deduced apoptosis-signaling pathways in activating caspase-3 in ischemic neurons remains elusive. The authors cloned the caspase-9 gene from the rat br

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Imbriani, Paola, Annalisa Tassone, Maria Meringolo, et al. "Loss of Non-Apoptotic Role of Caspase-3 in the PINK1 Mouse Model of Parkinson’s Disease." International Journal of Molecular Sciences 20, no. 14 (2019): 3407. http://dx.doi.org/10.3390/ijms20143407.

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Caspases are a family of conserved cysteine proteases that play key roles in multiple cellular processes, including programmed cell death and inflammation. Recent evidence shows that caspases are also involved in crucial non-apoptotic functions, such as dendrite development, axon pruning, and synaptic plasticity mechanisms underlying learning and memory processes. The activated form of caspase-3, which is known to trigger widespread damage and degeneration, can also modulate synaptic function in the adult brain. Thus, in the present study, we tested the hypothesis that caspase-3 modulates syna

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Grinshpon, Robert D., Suman Shrestha, James Titus-McQuillan, Paul T. Hamilton, Paul D. Swartz, and A. Clay Clark. "Resurrection of ancestral effector caspases identifies novel networks for evolution of substrate specificity." Biochemical Journal 476, no. 22 (2019): 3475–92. http://dx.doi.org/10.1042/bcj20190625.

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Apoptotic caspases evolved with metazoans more than 950 million years ago (MYA), and a series of gene duplications resulted in two subfamilies consisting of initiator and effector caspases. The effector caspase genes (caspases-3, -6, and -7) were subsequently fixed into the Chordata phylum more than 650 MYA when the gene for a common ancestor (CA) duplicated, and the three effector caspases have persisted throughout mammalian evolution. All caspases prefer an aspartate residue at the P1 position of substrates, so each caspase evolved discrete cellular roles through changes in substrate recogni

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Okinaga, Toshinori, Hironori Kasai, Toshiyuki Tsujisawa, and Tatsuji Nishihara. "Role of caspases in cleavage of lamin A/C and PARP during apoptosis in macrophages infected with a periodontopathic bacterium." Journal of Medical Microbiology 56, no. 10 (2007): 1399–404. http://dx.doi.org/10.1099/jmm.0.47193-0.

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The periodontopathic bacterium Actinobacillus actinomycetemcomitans has been implicated in the pathogenesis of periodontal diseases. It has been reported previously that infection with the organism induced apoptosis in the mouse macrophage cell line J774.1. In the present study, the role of caspases during apoptosis in A. actinomycetemcomitans-infected J774.1 cells was examined. A large number of apoptotic cells was detected by flow cytometric analysis in infected J774.1 cells; however, inhibitors of caspase-9, -6 and -3/7 completely blocked the induction of apoptosis. Expression of the cleave

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