A novel proteolytic cleavage of ROCK 1 in cell death: Not only by caspases 3 and 7 but also by caspase 2

2021 ◽  
Vol 547 ◽  
pp. 118-124
Author(s):  
Aysun Özdemir ◽  
Burçin İbişoğlu ◽  
Yaprak Dilber Şimay Demir ◽  
Elifnur Benhür ◽  
Farzaneh Valipour ◽  
...  
Keyword(s):  
Cell Death ◽  
Proteolytic Cleavage ◽  
Caspase 2

scholarly journals Caspase-2 and oxidative stress underlie the immunogenic potential of high hydrostatic pressure-induced cancer cell death

2016 ◽  
Vol 6 (1) ◽  
pp. e1258505 ◽  
Author(s):  
Irena Moserova ◽  
Iva Truxova ◽  
Abhishek D. Garg ◽  
Jakub Tomala ◽  
Patrizia Agostinis ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Death ◽  
Hydrostatic Pressure ◽  
Cancer Cell ◽  
High Hydrostatic Pressure ◽  
Cancer Cell Death ◽  
Caspase 2 ◽  
And Oxidative Stress

scholarly journals Analysis of programmed cell death in mouse fetal oocytes

Reproduction ◽  
2007 ◽  
Vol 134 (2) ◽  
pp. 241-252 ◽  
Author(s):  
A M Lobascio ◽  
F G Klinger ◽  
M L Scaldaferri ◽  
D Farini ◽  
M De Felici
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Specific Inhibitor ◽  
Annexin V ◽  
Death Process ◽  
Parp Cleavage ◽  
Tunel Staining ◽  
Calpain Inhibitor ◽  
Dna Ladder ◽  
Caspase 2

We report a short-term culture system that allowsto define novel characteristic of programmed cell death (PCD) in fetal oocytes and to underscore newaspects of this process. Mouse fetal oocytes culturedin conditions allowingmeiotic prophase I progression underwent apoptotic degeneration waves as revealed by TUNEL staining. TEM observations revealed recurrent atypical apoptotic morphologies characterized by the absence of chromatin margination and nuclear fragmentation; oocytes with autophagic and necrotic features were also observed. Further characterization of oocyte death evidenced DNA ladder, Annexin V binding, PARP cleavage, and usually caspase activation (namely caspase-2). In the aim to modulate the oocyte death process, we found that the addition to the culture medium of the pancaspase inhibitors Z-VAD orcaspase-2-specific inhibitor Z-VDVAD resulted in a partial and transient prevention of this process. Oocyte death was significantly reduced by the antioxidant agent NAC and partly prevented by KL and IGF-I growth factors. Finally, oocyte apoptosis was reduced by calpain inhibitor I and increased by rapamycin after prolonged culture.These results support the notion that fetal oocytes undergo degeneration mostly by apoptosis. This process is, however, often morphologically atypical and encompasses other forms of cell death including caspase-independent apoptosis and autophagia. The observation that oocyte death occurs mainly at certain stages of meiosis and can only be attenuated by typical anti-apoptotic treatments favors the notion that it is controlled at least in part by stage-specific oocyte-autonomous meiotic checkpoints and when activated is little amenable to inhibition being the oocyte able to switch back and forth among different death pathways.

scholarly journals Caspase-2 is required for cell death induced by cytoskeletal disruption

Oncogene ◽  
2008 ◽  
Vol 27 (24) ◽  
pp. 3393-3404 ◽  
Author(s):  
L H Ho ◽  
S H Read ◽  
L Dorstyn ◽  
L Lambrusco ◽  
S Kumar
Keyword(s):  
Cell Death ◽  
Caspase 2 ◽  
Cytoskeletal Disruption

scholarly journals Caspase-2 Mediates Site-Specific Retinal Ganglion Cell Death After Blunt Ocular Injury

2018 ◽  
Vol 59 (11) ◽  
pp. 4453 ◽  
Author(s):  
Chloe N. Thomas ◽  
Adam M. Thompson ◽  
Eleanor McCance ◽  
Martin Berry ◽  
Ann Logan ◽  
...  
Keyword(s):  
Cell Death ◽  
Ganglion Cell ◽  
Retinal Ganglion Cell ◽  
Ocular Injury ◽  
Retinal Ganglion ◽  
Site Specific ◽  
Retinal Ganglion Cell Death ◽  
Ganglion Cell Death ◽  
Caspase 2

scholarly journals Hepatitis C Virus-Induced Degradation of Cell Death-Inducing DFFA-Like Effector B Leads to Hepatic Lipid Dysregulation

2016 ◽  
Vol 90 (8) ◽  
pp. 4174-4185 ◽  
Author(s):  
Emily M. Lee ◽  
Ali Alsagheir ◽  
Xianfang Wu ◽  
Christy Hammack ◽  
John McLauchlan ◽  
...  
Keyword(s):  
Cell Death ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Hepatic Steatosis ◽  
Hepatoma Cell ◽  
Biological Significance ◽  
Proteolytic Cleavage ◽  
Hcv Infection ◽  
Hepatoma Cell Line ◽  
Liver Protein

ABSTRACTIndividuals chronically infected with hepatitis C virus (HCV) commonly exhibit hepatic intracellular lipid accumulation, termed steatosis. HCV infection perturbs host lipid metabolism through both cellular and virus-induced mechanisms, with the viral core protein playing an important role in steatosis development. We have recently identified a liver protein, the cell death-inducing DFFA-like effector B (CIDEB), as an HCV entry host dependence factor that is downregulated by HCV infection in a cell culture model. In this study, we investigated the biological significance and molecular mechanism of this downregulation. HCV infection in a mouse model downregulated CIDEB in the liver tissue, and knockout of the CIDEB gene in a hepatoma cell line results in multiple aspects of lipid dysregulation that can contribute to hepatic steatosis, including reduced triglyceride secretion, lower lipidation of very-low-density lipoproteins, and increased lipid droplet (LD) stability. The potential link between CIDEB downregulation and steatosis is further supported by the requirement of the HCV core and its LD localization for CIDEB downregulation, which utilize a proteolytic cleavage event that is independent of the cellular proteasomal degradation of CIDEB.IMPORTANCEOur data demonstrate that HCV infection of human hepatocytesin vitroandin vivoresults in CIDEB downregulation via a proteolytic cleavage event. Reduction of CIDEB protein levels by HCV or gene editing, in turn, leads to multiple aspects of lipid dysregulation, including LD stabilization. Consequently, CIDEB downregulation may contribute to HCV-induced hepatic steatosis.

Caspase activation

2003 ◽  
Vol 70 ◽  
pp. 233-242 ◽  
Author(s):  
Kelly M. Boatright ◽  
Guy S. Salvesen
Keyword(s):  
Cell Death ◽  
Recent Work ◽  
Proteolytic Cleavage ◽  
Caspase Activation ◽  
Point Of No Return ◽  
Initiator Caspases ◽  
Executioner Caspases ◽  
Activation Event

Caspase activation is the 'point of no return' commitment to cell death. Synthesized as inactive zymogens, it is essential that the caspases remain inactive until the death signal is received. It is known for the downstream executioner caspases-3 and -7 that the activation event is proteolytic cleavage, and this had been assumed to apply to the initiator caspases as well. However, recent studies conducted on caspases-2, -8 and -9 have challenged this tenet of caspase activation. In this review we focus on the molecular details of caspase activation, with emphasis on recent work that provides a pleasing explanation for the differential requirements for the activation of executioner and initiator caspases.

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