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Journal articles on the topic 'Caspases'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

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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Villa, Pascal, Scott H. Kaufmann, and William C. Earnshaw. "Caspases and caspase inhibitors." Trends in Biochemical Sciences 22, no. 10 (1997): 388–93. http://dx.doi.org/10.1016/s0968-0004(97)01107-9.

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N, Nisha, Deepak Chand Sharma, Ravi Datta Sharma, and Jinny Tomar. "Prevalence Around Inflammatory Caspases in Urinary Tract Infections, Review." Biosciences Biotechnology Research Asia 21, no. 4 (2024): 1349–61. https://doi.org/10.13005/bbra/3308.

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ABSTRACT: Caspases are cysteinyl aspartate-specific proteases that play important roles in apoptosis, pyroptosis and cytokine maturation. Pyroptosis is a manifestation of inflammatory caspase mediated cell death induced by inflammatory caspases such as caspase-11, caspase 4, caspase 5 and caspase 1. These inflammatory caspases are involved in the inflammatory responses induced by these pathogens to control protozoan, viral, fungal and bacterial pathogen. This study aimed to understand the mechanism that involve different inflammatory caspases and their responses to urinary tract infections. By

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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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Marsden, Vanessa S., Paul G. Ekert, Mark Van Delft, David L. Vaux, Jerry M. Adams, and Andreas Strasser. "Bcl-2–regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9." Journal of Cell Biology 165, no. 6 (2004): 775–80. http://dx.doi.org/10.1083/jcb.200312030.

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Apoptosis in response to developmental cues and stress stimuli is mediated by caspases that are regulated by the Bcl-2 protein family. Although caspases 2 and 9 have each been proposed as the apical caspase in that pathway, neither is indispensable for the apoptosis of leukocytes or fibroblasts. To investigate whether these caspases share a redundant role in apoptosis initiation, we generated caspase-2−/−9−/− mice. Their overt phenotype, embryonic brain malformation and perinatal lethality mirrored that of caspase-9−/− mice but were not exacerbated. Analysis of adult mice reconstituted with ca

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Chang, Howard Y., and Xiaolu Yang. "Proteases for Cell Suicide: Functions and Regulation of Caspases." Microbiology and Molecular Biology Reviews 64, no. 4 (2000): 821–46. http://dx.doi.org/10.1128/mmbr.64.4.821-846.2000.

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SUMMARY Caspases are a large family of evolutionarily conserved proteases found from Caenorhabditis elegans to humans. Although the first caspase was identified as a processing enzyme for interleukin-1β, genetic and biochemical data have converged to reveal that many caspases are key mediators of apoptosis, the intrinsic cell suicide program essential for development and tissue homeostasis. Each caspase is a cysteine aspartase; it employs a nucleophilic cysteine in its active site to cleave aspartic acid peptide bonds within proteins. Caspases are synthesized as inactive precursors termed proc

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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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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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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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Flütsch, Andreas, Thilo Schroeder, Jonas Barandun, Rafael Ackermann, Martin Bühlmann, and Markus G. Grütter. "Specific targeting of human caspases using designed ankyrin repeat proteins." Biological Chemistry 395, no. 10 (2014): 1243–52. http://dx.doi.org/10.1515/hsz-2014-0173.

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Abstract Caspases play important roles in cell death, differentiation, and proliferation. Due to their high homology, especially of the active site, specific targeting of a particular caspase using substrate analogues is very difficult. Although commercially available small molecules based on peptides are lacking high specificity due to overlapping cleavage motives between different caspases, they are often used as specific tools. We have selected designed ankyrin repeat proteins (DARPins) against human caspases 1–9 and identified high-affinity binders for the targeted caspases, except for cas

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Kemp, C. M., T. Parr, R. G. Bardsley, and P. J. Buttery. "Comparison of the relative expression of caspase isoforms across muscle types." Proceedings of the British Society of Animal Science 2005 (2005): 107. http://dx.doi.org/10.1017/s1752756200010188.

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Toughness is a determinant of meat quality and a common cause of unacceptability in meat products. Calpain proteases are believed to be involved in meat tenderisation by post mortem degradation of myofibrillar proteins (Sensky et al., 2001). However other proteases are likely to contribute to the proteolysis involved in meat-conditioning (Sentandreu et al., 2002). Caspases are proteases involved in protein degradation in apoptosis. Like calpains caspases are activated early in pathological events associated with hypoxia/ischaemia, which is not dissimilar to the hypoxic conditions in muscle aft

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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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Kesavardhana, Sannula, R. K. Subbarao Malireddi, and Thirumala-Devi Kanneganti. "Caspases in Cell Death, Inflammation, and Pyroptosis." Annual Review of Immunology 38, no. 1 (2020): 567–95. http://dx.doi.org/10.1146/annurev-immunol-073119-095439.

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Caspases are a family of conserved cysteine proteases that play key roles in programmed cell death and inflammation. In multicellular organisms, caspases are activated via macromolecular signaling complexes that bring inactive procaspases together and promote their proximity-induced autoactivation and proteolytic processing. Activation of caspases ultimately results in programmed execution of cell death, and the nature of this cell death is determined by the specific caspases involved. Pioneering new research has unraveled distinct roles and cross talk of caspases in the regulation of programm

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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 (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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Creagh, E. M., and S. J. Martin. "Caspases: cellular demolition experts." Biochemical Society Transactions 29, no. 6 (2001): 696–702. http://dx.doi.org/10.1042/bst0290696.

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Apoptosis is co-ordinated by a family of cysteine proteases, the caspases, that dismantle the cell by targeting a panoply of proteins for limited proteolysis. The mammalian caspase family contains 14 members, a subset of which participates in apoptosis, with the remainder likely to be involved in the processing of pro-inflammatory cytokines. Apical caspase activation events are typically initiated by adaptor molecules that promote caspase aggregation and facilitate caspase auto-activation. In contrast, distal caspase activation events are controlled by caspases activated earlier in the cascade

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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 (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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Janečková, Eva, Petra Bíliková, and Eva Matalová. "Osteogenic Potential of Caspases Related to Endochondral Ossification." Journal of Histochemistry & Cytochemistry 66, no. 1 (2017): 47–58. http://dx.doi.org/10.1369/0022155417739283.

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Caspases have functions particularly in apoptosis and inflammation. Increasing evidence indicates novel roles of these proteases in cell differentiation, including those involved in osteogenesis. This investigation provides a complex screening of osteogenic markers affected by pan caspase inhibition in micromass cultures derived from mouse forelimbs. PCR Array analysis showed significant alterations in expression of 49 osteogenic genes after 7 days of inhibition. The largest change was a decrease in CD36 expression, which was confirmed at organ level by caspase inhibition in cultured mouse uln

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Friesen, Claudia, Miriam Uhl, Ulrich Pannicke, Klaus Schwarz, Erich Miltner, and Klaus-Michael Debatin. "DNA-Ligase IV and DNA-Protein Kinase Play a Critical Role in Deficient Caspases Activation in Apoptosis-resistant Cancer Cells by Using Doxorubicin." Molecular Biology of the Cell 19, no. 8 (2008): 3283–89. http://dx.doi.org/10.1091/mbc.e08-03-0306.

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Resistance toward cytotoxic drugs is one of the primary causes for therapeutic failure in cancer therapy. DNA repair mechanisms as well as deficient caspases activation play a critical role in apoptosis resistance of tumor cells toward anticancer drug treatment. Here, we discovered that deficient caspases activation in apoptosis-resistant cancer cells depends on DNA-ligase IV and DNA-protein kinase (DNA-PK), playing crucial roles in the nonhomologous end joining (NHEJ) pathway, which is the predominant pathway for DNA double-strand break repair (DNA-DSB-repair) in mammalian cells. DNA-PK(+/+)

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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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Shrestha, Suman, Jessica Tung, Robert D. Grinshpon, et al. "Caspases from scleractinian coral show unique regulatory features." Journal of Biological Chemistry 295, no. 43 (2020): 14578–91. http://dx.doi.org/10.1074/jbc.ra120.014345.

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Coral reefs are experiencing precipitous declines around the globe with coral diseases and temperature-induced bleaching being primary drivers of these declines. Regulation of apoptotic cell death is an important component in the coral stress response. Although cnidaria are known to contain complex apoptotic signaling pathways, similar to those in vertebrates, the mechanisms leading to cell death are largely unexplored. We identified and characterized two caspases each from Orbicella faveolata, a disease-sensitive reef-building coral, and Porites astreoides, a disease-resistant reef-building c

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Yang, Jie, Zhonghua Liu, Chuanping Wang, et al. "Mechanism of gasdermin D recognition by inflammatory caspases and their inhibition by a gasdermin D-derived peptide inhibitor." Proceedings of the National Academy of Sciences 115, no. 26 (2018): 6792–97. http://dx.doi.org/10.1073/pnas.1800562115.

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The inflammasomes are signaling platforms that promote the activation of inflammatory caspases such as caspases-1, -4, -5, and -11. Recent studies identified gasdermin D (GSDMD) as an effector for pyroptosis downstream of the inflammasome signaling pathways. Cleavage of GSDMD by inflammatory caspases allows its N-terminal domain to associate with membrane lipids and form pores that induce pyroptotic cell death. Despite the important role of GSDMD in pyroptosis, the molecular mechanisms of GSDMD recognition and cleavage by inflammatory caspases that trigger pyroptosis are poorly understood. Her

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Davies, Christopher W., Irma Stowe, Qui T. Phung, et al. "Discovery of a caspase cleavage motif antibody reveals insights into noncanonical inflammasome function." Proceedings of the National Academy of Sciences 118, no. 12 (2021): e2018024118. http://dx.doi.org/10.1073/pnas.2018024118.

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Inflammasomes sense a number of pathogen and host damage signals to initiate a signaling cascade that triggers inflammatory cell death, termed pyroptosis. The inflammatory caspases (1/4/5/11) are the key effectors of this process through cleavage and activation of the pore-forming protein gasdermin D. Caspase-1 also activates proinflammatory interleukins, IL-1β and IL-18, via proteolysis. However, compared to the well-studied apoptotic caspases, the identity of substrates and therefore biological functions of the inflammatory caspases remain limited. Here, we construct, validate, and apply an

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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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Mancini, Marie, Carolyn E. Machamer, Sophie Roy, et al. "Caspase-2 Is Localized at the Golgi Complex and Cleaves Golgin-160 during Apoptosis." Journal of Cell Biology 149, no. 3 (2000): 603–12. http://dx.doi.org/10.1083/jcb.149.3.603.

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Caspases are an extended family of cysteine proteases that play critical roles in apoptosis. Animals deficient in caspases-2 or -3, which share very similar tetrapeptide cleavage specificities, exhibit very different phenotypes, suggesting that the unique features of individual caspases may account for distinct regulation and specialized functions. Recent studies demonstrate that unique apoptotic stimuli are transduced by distinct proteolytic pathways, with multiple components of the proteolytic machinery clustering at distinct subcellular sites. We demonstrate here that, in addition to its nu

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Zermati, Yael, Carmen Garrido, Sophie Amsellem, et al. "Caspase Activation Is Required for Terminal Erythroid Differentiation." Journal of Experimental Medicine 193, no. 2 (2001): 247–54. http://dx.doi.org/10.1084/jem.193.2.247.

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The cysteine proteases known as caspases play a central role in most apoptotic pathways. Here, we show that caspase inhibitors arrest the maturation of human erythroid progenitors at early stages of differentiation, before nucleus and chromatin condensation. Effector caspases such as caspase-3 are transiently activated through the mitochondrial pathway during erythroblast differentiation and cleave proteins involved in nucleus integrity (lamin B) and chromatin condensation (acinus) without inducing cell death and cleavage of GATA-1. These observations indicate a new function for caspases as ke

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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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Rosebeck, Shaun, Mattina Alonge, Jagoda Jasielec, et al. "Anti-Myeloma Activity of Combined Inhibition of the Proteasome with Carfilzomib (CFZ) and XPO1/CRM1-Dependent Nuclear Export By Selinexor (KPT-330) Via a Novel Mechanism of Intracellular Activation of Caspase 10-Dependent Apoptosis." Blood 124, no. 21 (2014): 3443. http://dx.doi.org/10.1182/blood.v124.21.3443.3443.

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Abstract INTRODUCTION Previously, our work highlighted the synergistic activity of combining the selective inhibitor of nuclear export (SINE) selinexor with the irreversible proteasome inhibitor (PI) CFZ in multiple myeloma (MM) patient-derived plasma cells and cell lines, and in a murine xenograft model (Rosebeck et al, Blood 2013:122(21):279). Our studies were the first to suggest a role for both autophagy and apoptosis in response to combined SINE/PI treatment. Importantly, our results served as pre-clinical rationale for a currently-enrolling phase I clinical trial for the treatment of ref

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Hounsell, Caitlin, and Yun Fan. "The Duality of Caspases in Cancer, as Told through the Fly." International Journal of Molecular Sciences 22, no. 16 (2021): 8927. http://dx.doi.org/10.3390/ijms22168927.

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Caspases, a family of cysteine-aspartic proteases, have an established role as critical components in the activation and initiation of apoptosis. Alongside this a variety of non-apoptotic caspase functions in proliferation, differentiation, cellular plasticity and cell migration have been reported. The activity level and context are important factors in determining caspase function. As a consequence of their critical role in apoptosis and beyond, caspases are uniquely situated to have pathological roles, including in cancer. Altered caspase function is a common trait in a variety of cancers, w

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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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Baburamani, Ana A., Yasuka Miyakuni, Regina Vontell, et al. "Does Caspase-6 Have a Role in Perinatal Brain Injury?" Developmental Neuroscience 37, no. 4-5 (2015): 321–37. http://dx.doi.org/10.1159/000375368.

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Apoptotic mechanisms are centre stage for the development of injury in the immature brain, and caspases have been shown to play a pivotal role during brain development and in response to injury. The inhibition of caspases using broad-spectrum agents such as Q-VD-OPh is neuroprotective in the immature brain. Caspase-6, an effector caspase, has been widely researched in neurodevelopmental disorders and found to be important following adult stroke, but its function in the neonatal brain has yet to be detailed. Furthermore, caspases may be important in microglial activation; microglia are required

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Jacotot, Étienne. "Inhibition des caspases." médecine/sciences 36, no. 12 (2020): 1143–54. http://dx.doi.org/10.1051/medsci/2020222.

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Les caspases sont une famille de cystéines protéases bien connues pour leurs rôles centraux au cours de l’apoptose et de l’inflammation. Elles interviennent aussi dans des voies de mort cellulaire régulées non-apoptotiques, et contribuent à de très nombreux mécanismes physiologiques. Le développement d’approches thérapeutiques ciblant les caspases a engendré un fort intérêt industriel dès les années 1990, suscitant d’intenses recherches sur les mécanismes biologiques, et conduisant à la mise au point de nombreux inhibiteurs synthétiques. La plupart de ces inhibiteurs sont des dérivés de peptid

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Samejima, Kumiko, Shigenobu Toné, Timothy J. Kottke, et al. "Transition from Caspase-dependent to Caspase-independent Mechanisms at the Onset of Apoptotic Execution." Journal of Cell Biology 143, no. 1 (1998): 225–39. http://dx.doi.org/10.1083/jcb.143.1.225.

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We have compared cytoplasmic extracts from chicken DU249 cells at various stages along the apoptotic pathway. Extracts from morphologically normal “committed stage” cells induce apoptotic morphology and DNA cleavage in substrate nuclei but require ongoing caspase activity to do so. In contrast, extracts from frankly apoptotic cells induce apoptotic events in added nuclei in a caspase-independent manner. Biochemical fractionation of these extracts reveals that a column fraction enriched in endogenous active caspases is unable to induce DNA fragmentation or chromatin condensation in substrate nu

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Los, Marek, Ingrid Herr, Claudia Friesen, Simone Fulda, Klaus Schulze-Osthoff, and Klaus-Michael Debatin. "Cross-Resistance of CD95- and Drug-Induced Apoptosis as a Consequence of Deficient Activation of Caspases (ICE/Ced-3 Proteases)." Blood 90, no. 8 (1997): 3118–29. http://dx.doi.org/10.1182/blood.v90.8.3118.

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Abstract The cytotoxic effect of anticancer drugs has been shown to involve induction of apoptosis. We report here that tumor cells resistant to CD95 (APO-1/Fas) -mediated apoptosis were cross-resistant to apoptosis-induced by anticancer drugs. Apoptosis induced in tumor cells by cytarabine, doxorubicin, and methotrexate required the activation of ICE/Ced-3 proteases (caspases), similarly to the CD95 system. After drug treatment, a strong increase of caspase activity was found that preceded cell death. Drug-induced activation of caspases was also found in ex vivo-derived T-cell leukemia cells.

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Yang, Jiang-Yan, and Christian Widmann. "Antiapoptotic Signaling Generated by Caspase-Induced Cleavage of RasGAP." Molecular and Cellular Biology 21, no. 16 (2001): 5346–58. http://dx.doi.org/10.1128/mcb.21.16.5346-5358.2001.

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ABSTRACT Activation of caspases 3 and 9 is thought to commit a cell irreversibly to apoptosis. There are, however, several documented situations (e.g., during erythroblast differentiation) in which caspases are activated and caspase substrates are cleaved with no associated apoptotic response. Why the cleavage of caspase substrates leads to cell death in certain cases but not in others is unclear. One possibility is that some caspase substrates generate antiapoptotic signals when cleaved. Here we show that RasGAP is one such protein. Caspases cleave RasGAP into a C-terminal fragment (fragment

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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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Nyormoi, Okot, Zhi Wang, Dao Doan, Maribelis Ruiz, David McConkey та Menashe Bar-Eli. "Transcription Factor AP-2α Is Preferentially Cleaved by Caspase 6 and Degraded by Proteasome during Tumor Necrosis Factor Alpha-Induced Apoptosis in Breast Cancer Cells". Molecular and Cellular Biology 21, № 15 (2001): 4856–67. http://dx.doi.org/10.1128/mcb.21.15.4856-4867.2001.

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ABSTRACT Several reports have linked activating protein 2α (AP-2α) to apoptosis, leading us to hypothesize that AP-2α is a substrate for caspases. We tested this hypothesis by examining the effects of tumor necrosis factor alpha (TNF-α) on the expression of AP-2 in breast cancer cells. Here, we provide evidence that TNF-α downregulates AP-2α and AP-2γ expression posttranscriptionally during TNF-α-induced apoptosis. Both a general caspase antagonist (zVADfmk) and a caspase 6-preferred antagonist (zVEIDfmk) inhibited TNF-α-induced apoptosis and AP-2α downregulation. In vivo tests showed that AP-

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Martins, Luis M., Timothy J. Kottke, Scott H. Kaufmann, and William C. Earnshaw. "Phosphorylated Forms of Activated Caspases Are Present in Cytosol From HL-60 Cells During Etoposide-Induced Apoptosis." Blood 92, no. 9 (1998): 3042–49. http://dx.doi.org/10.1182/blood.v92.9.3042.

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Abstract Treatment of HL-60 human leukemia cells with etoposide induces apoptotic cell death and activation of at least 18 electrophoretically distinct cysteine-dependent aspartate-directed protease (caspase) isoforms, several of which differ only in their isoelectric points. The purpose of the present study was to determine whether activated caspases are phosphorylated. Phosphatase treatment of cytosolic extracts containing active caspases followed by affinity labeling with N-(N-benzyloxycarbonylglutamyl-N-biotinyllysyl)aspartic acid [(2,6-dimethylbenzoyl)oxy] methyl ketone (Z-EK(bio)D-aomk

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Martins, Luis M., Timothy J. Kottke, Scott H. Kaufmann, and William C. Earnshaw. "Phosphorylated Forms of Activated Caspases Are Present in Cytosol From HL-60 Cells During Etoposide-Induced Apoptosis." Blood 92, no. 9 (1998): 3042–49. http://dx.doi.org/10.1182/blood.v92.9.3042.421k55_3042_3049.

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Treatment of HL-60 human leukemia cells with etoposide induces apoptotic cell death and activation of at least 18 electrophoretically distinct cysteine-dependent aspartate-directed protease (caspase) isoforms, several of which differ only in their isoelectric points. The purpose of the present study was to determine whether activated caspases are phosphorylated. Phosphatase treatment of cytosolic extracts containing active caspases followed by affinity labeling with N-(N-benzyloxycarbonylglutamyl-N-biotinyllysyl)aspartic acid [(2,6-dimethylbenzoyl)oxy] methyl ketone (Z-EK(bio)D-aomk) showed

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Jones, Blake, Patricia J. Roberts, William A. Faubion, Eiki Kominami, and Gregory J. Gores. "Cystatin A expression reduces bile salt-induced apoptosis in a rat hepatoma cell line." American Journal of Physiology-Gastrointestinal and Liver Physiology 275, no. 4 (1998): G723—G730. http://dx.doi.org/10.1152/ajpgi.1998.275.4.g723.

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We have previously demonstrated abrogation of bile salt-induced apoptosis by cathepsin B inhibitors. However, caspases have been strongly implicated in apoptosis, and the mechanistic interface between caspase and cathepsin B activation is unclear. Thus our aims were to determine the mechanistic relationship between caspases and cathepsin B in bile salt-induced apoptosis in a rat hepatoma cell line. Expression of cystatin A was used to inhibit cathepsin B, whereas Z-Val-Ala-Asp-fluoromethyl ketone (Z-VAD-FMK) was used to inhibit caspases. Cystatin A expression prevented cathepsin B activation a

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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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Bloomer, David T., Tanja Kitevska-Ilioski, Delara Pantaki-Eimany, et al. "CrmA orthologs from diverse poxviruses potently inhibit caspases-1 and -8, yet cleavage site mutagenesis frequently produces caspase-1-specific variants." Biochemical Journal 476, no. 9 (2019): 1335–57. http://dx.doi.org/10.1042/bcj20190202.

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AbstractPoxviruses encode many proteins that enable them to evade host anti-viral defense mechanisms. Spi-2 proteins, including Cowpox virus CrmA, suppress anti-viral immune responses and contribute to poxviral pathogenesis and lethality. These proteins are ‘serpin’ protease inhibitors, which function via a pseudosubstrate mechanism involving initial interactions between the protease and a cleavage site within the serpin. A conformational change within the serpin interrupts the cleavage reaction, deforming the protease active site and preventing dissociation. Spi-2 proteins like CrmA potently

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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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ZECH, Birgit, Roman KÖHL, Andreas von KNETHEN, and Bernhard BRÜNE. "Nitric oxide donors inhibit formation of the Apaf-1/caspase-9 apoptosome and activation of caspases." Biochemical Journal 371, no. 3 (2003): 1055–64. http://dx.doi.org/10.1042/bj20021720.

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Caspases are critical for the initiation and execution of apoptosis. Nitric oxide (NO) or derived species can prevent programmed cell death in several cell types, reportedly through S-nitrosation and inactivation of active caspases. Although we find that S-nitrosation of caspases can occur in vitro, our study questions whether this post-translational modification is solely responsible for NO-mediated inhibition of apoptosis. Indeed, using Jurkat cells as a model system, we demonstrate that NO donors block Fas- and etoposide-induced caspase activation and apoptosis (downstream of mitochondrial

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Logue, Susan E., and Seamus J. Martin. "Caspase activation cascades in apoptosis." Biochemical Society Transactions 36, no. 1 (2008): 1–9. http://dx.doi.org/10.1042/bst0360001.

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Apoptosis, a highly controlled mode of cell death, is utilized to eliminate superfluous, aged, injured or infected cells from the body. Caspases, a family of aspartic acid-specific proteases, are the major effectors of apoptosis. To curtail their activity, caspases are normally synthesized as inactive precursors, but become activated at the onset of apoptosis by activation signals. Once active, caspases preside over the ordered dismantling of the cell through restricted proteolysis of hundreds of substrate proteins. Over the last 10 years, intense research has focused upon the pathways that co

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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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Fernández, Daniel Jiménez, and Mohamed Lamkanfi. "Inflammatory caspases: key regulators of inflammation and cell death." Biological Chemistry 396, no. 3 (2015): 193–203. http://dx.doi.org/10.1515/hsz-2014-0253.

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Abstract The innate immune system represents the first line of defence against infectious agents, and co-ordinates cellular and molecular mechanisms that result in effective inflammatory and anti-microbial responses against pathogens. Infection and cellular stress trigger assembly of canonical and noncanonical inflammasome complexes that activate the inflammatory caspases-1 and -11, respectively. These inflammatory caspases play key roles in innate immune responses by inducing pyroptosis to halt intracellular replication of pathogens, and by engaging the extracellular release of pro-inflammato

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Koto, Akiko, Erina Kuranaga, and Masayuki Miura. "Temporal regulation of Drosophila IAP1 determines caspase functions in sensory organ development." Journal of Cell Biology 187, no. 2 (2009): 219–31. http://dx.doi.org/10.1083/jcb.200905110.

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The caspases comprise a family of cysteine proteases that function in various cellular processes, including apoptosis. However, how the balance is struck between the caspases’ role in cell death and their nonapoptotic functions is unclear. To address this issue, we monitored the protein turnover of an endogenous caspase inhibitor, Drosophila IAP1 (DIAP1). DIAP1 is an E3 ubiquitin ligase that promotes the ubiquitination of caspases and thereby prevents caspase activation. For this study, we developed a fluorescent probe to monitor DIAP1 turnover in the external sensory organ precursor (SOP) lin

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Wei, Zhongcheng, Wei Ding, Moli Li, et al. "The Caspase Homologues in Scallop Chlamys farreri and Their Expression Responses to Toxic Dinoflagellates Exposure." Toxins 14, no. 2 (2022): 108. http://dx.doi.org/10.3390/toxins14020108.

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The cysteine aspartic acid-specific protease (caspase) family is distributed across vertebrates and invertebrates, and its members are involved in apoptosis and response to cellular stress. The Zhikong scallop (Chlamys farreri) is a bivalve mollusc that is well adapted to complex marine environments, yet the diversity of caspase homologues and their expression patterns in the Zhikong scallop remain largely unknown. Here, we identified 30 caspase homologues in the genome of the Zhikong scallop and analysed their expression dynamics during all developmental stages and following exposure to paral

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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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Kersse, K., T. Vanden Berghe, M. Lamkanfi, and P. Vandenabeele. "A phylogenetic and functional overview of inflammatory caspases and caspase-1-related CARD-only proteins." Biochemical Society Transactions 35, no. 6 (2007): 1508–11. http://dx.doi.org/10.1042/bst0351508.

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Caspase 1 is a cysteinyl aspartate-specific proteinase involved in the maturation of inflammatory cytokines such as pro-IL-1β (interleukin-1β) and pro-IL-18. Caspase 1 clusters phylogenetically together with human caspases 4, 5 and 12 and murine caspases 11 and 12, and forms the group of the so-called inflammatory caspases. Caspase 1 consists of an N-terminal CARD (caspase recruitment domain) and a proteolytic domain containing the catalytic residues. The CARD-containing prodomain is involved in the formation of the protease-activating inflammasome complex. We have also found that the prodomai

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