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Programmed Cell Death: The Biology of Cell Death in the Nematode Caenorhabditis elegans and Implications for the Understanding and Treatment of Human Brain Injury after Cardiac Surgery
Published in Richard A. Jonas, Jane W. Newburger, Joseph J. Volpe, John W. Kirklin, Brain Injury and Pediatric Cardiac Surgery, 2019
It is striking that human bcl-2 can act in C. elegans. Genes and their protein products do not work in isolation. Rather, every gene must interact with other genes to exert its biological effects. That bcl-2 can act in C. elegans to prevent cell death, and can do so apparently by substituting for worm ced-9, suggests that in humans bcl-2 functions by interacting with genes similar to those that interact with ced-9 in worms, for example, genes similar to ced-3 and ced-4. The findings that cysteine proteases similar to CED-3 control programmed cell death in vertebrates strongly support the hypothesis that genes similar to ced-3 and ced-4 interact with bcl-2 in the process of programmed cell death in humans.
The Stress System
Published in Len Wisneski, The Scientific Basis of Integrative Health, 2017
Apoptosis can be called a programmed cellular death because it is genetically determined (Hetts, 1998). Tissue-specific signals elicit protein products from a gene that researchers named the CED-4 gene. CED-4 activates the CED-3 gene to instigate the process of apoptosis. Various commitment signals cause the process of apoptosis to begin, while other signals inhibit it. In other words, there are prodeath ligands, and there are antideath ligands. Research is still being conducted on various commitment signals, but let us look at one death ligand, the Fas protein, to generally explain the process. When a cytotoxic T lymphocyte binds to an antigen, it causes the elaboration of the Fas ligand (FasL). The FasL easily binds to Fas, which is a cell-surface death receptor that is found on most cells. This interaction results in apoptosis, which in this instance would cause the death of the cell. The Fas receptor is like a smart bomb; it turns on the genetic material to initiate a cascade that commits the cell to destruction.
The role of apoptosis in non-mammalian host-parasite relationships
Published in G. F. Wiegertjes, G. Flik, Host-Parasite Interactions, 2004
Three of the C. elegans genes, in particular, were of great importance in the analysis of apoptosis in both nematodes and mammals. These are components of the central control mechanism of cell death, i.e. ced-3, ced-4 and ced-9 (Ellis et al., 1991). C. elegans in which ced-3 or ced-4 have been inactivated by mutation illustrate the effects of failure of developmental cell death, since both these genes are required in the cell death process. In both cases, mammalian homologues have now been identified which also play important roles in apoptosis. In the case of ced-3, at least 12 mammalian homologues have been identified and the family encoded by these genes, the caspase family, makes up the biochemical core of the apoptotic process.
Temperature signaling underlying thermotaxis and cold tolerance in Caenorhabditis elegans
Published in Journal of Neurogenetics, 2020
Asuka Takeishi, Natsune Takagaki, Atsushi Kuhara
Downstream molecules of ENDU-2 have been identified by transcriptome analysis. One downstream gene is an apoptotic gene, ced-3 encoding caspase (Ujisawa et al., 2018). ced-3 mutants exhibit decreased cold tolerance, which is caused by defective CED-3 functions in ADL and muscle cells (Ujisawa et al., 2018). It is reported that CED-3 controls synaptic remodeling in neurons during development (Meng et al., 2015). ENDU-2 plays a role as a negative regulator of CED-3-dependent synaptic remodeling (Figure 6). These imply that ENDU-2 is involved in cold tolerance and synaptic remodeling through the caspase pathway (Figure 6) (Ujisawa et al., 2018).
Lycopene and Chrysin through Mitigation of Neuroinflammation and Oxidative Stress Exerted Antidepressant Effects in Clonidine-Induced Depression-like Behavior in Rats
Published in Journal of Dietary Supplements, 2023
Ekram Nemr Abd Al Haleem, Hebatalla I. Ahmed, Reem N. El-Naga
All caspases are synthesized as proenzymes activated by proteolytic cleavage at Asp-X sites and contain a conserved pentapeptide QACXG sequence. Among the caspases, caspase-3 (CPP32) (64) has the highest homology to CED-3 in terms of both amino acid sequence and substrate specificity (65), cleaved caspase3 was found to promote apoptosis. Caspase-3p32 is activated by cleavage into p20 and p12 fragments and cleaves several intracellular substrates (66).