About: Synergistic activation of p53 by actinomycin D and nutlin-3a is associated with the upregulation of crucial regulators and effectors of innate immunity

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About: Synergistic activation of p53 by actinomycin D and nutlin-3a is associated with the upregulation of crucial regulators and effectors of innate immunity Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Synergistic activation of p53 by actinomycin D and nutlin-3a is associated with the upregulation of crucial regulators and effectors of innate immunity
Creator	Gdowicz-Kłosok, Agnieszka Głowala-Kosińska, Magdalena Krześniak, Małgorzata Rusin, Marek Zajkowicz, Artur
Source	Elsevier; Medline; PMC
abstract	Abstract Actinomycin D and nutlin-3a (A + N) activate p53, partly through induction of phosphorylation on Ser392. The death of A549 cells induced by A + N morphologically resembles inflammation-inducing pyroptosis - cell destruction triggered by activated caspase-1. The treatment with A + N (or camptothecin) strongly upregulated caspase-1 and its two activators: IFI16 and NLRP1, however, caspase-1 activation was not detected. A549 cells may have been primed for pyroptosis, with the absence of a crucial trigger. The investigation of additional innate immunity elements revealed that A + N (or camptothecin) stimulated the expression of NLRX1, STING (stimulator of interferon genes) and two antiviral proteins, IFIT1 and IFIT3. IFI16 and caspase-1 are coded by p53-regulated genes which led us to investigate regulation of NLRP1, NLRX1, STING, IFIT1 and IFIT3 in p53-dependent mode. The upregulation of NLRP1, NLRX1 and STING was attenuated in p53 knockdown cells. The upsurge of the examined genes, and activation of p53, was inhibited by C16, an inhibitor of PKR kinase. PKR was tested due to its ability to phosphorylate p53 on Ser392. Surprisingly, C16 was active even in PKR knockdown cells. The ability of C16 to prevent activation of p53 and expression of innate immunity genes may be the source of its strong anti-inflammatory action. Moreover, cells exposed to A + N can influence neighboring cells in paracrine fashion, for instance, they shed ectodomain of COL17A1 protein and induce, in p53-dependent mode, the expression of gene for interleukin-7. Further, the activation of p53 also spurred the expression of SOCS1, an inhibitor of interferon triggered STAT1-dependent signaling. We conclude that, stimulation of p53 primes cells for the production of interferons (through upregulation of STING), and may activate negative-feedback within this signaling system by enhancing the production of SOCS1.
has issue date	2020-05-31(xsd:dateTime)
bibo:doi	10.1016/j.cellsig.2020.109552
bibo:pmid	32032660
has license	els-covid
sha1sum (hex)	9fb07c0520781ebd106f2bb752c8a54b60362656
schema:url	https://doi.org/10.1016/j.cellsig.2020.109552
resource representing a document's title	Synergistic activation of p53 by actinomycin D and nutlin-3a is associated with the upregulation of crucial regulators and effectors of innate immunity
has PubMed Central identifier	PMC7126238
has PubMed identifier	32032660
schema:publication	Cellular Signalling
resource representing a document's body	covid:9fb07c0520781ebd106f2bb752c8a54b60362656#body_text
is schema:about of	named entity 'caspase' named entity 'interferons' named entity 'immunity' named entity 'activation' named entity 'proteins' named entity 'instance' named entity 'camptothecin' named entity 'gene' named entity 'activate' named entity 'activate' named entity 'p53' named entity 'activation' named entity 'genes' named entity 'cells' named entity 'p53' covid:arg/9fb07c0520781ebd106f2bb752c8a54b60362656 named entity 'neighboring' named entity 'triggered' named entity 'camptothecin' named entity 'treatment' named entity 'anti-inflammatory' named entity 'STING' named entity 'spurred' named entity 'mode' named entity 'expression' named entity 'p53' named entity 'C16' named entity 'expression' named entity 'IFI16' named entity 'primes' named entity 'pyroptosis' named entity 'triggered' named entity 'induction' named entity 'production' named entity 'upregulated' named entity 'effectors' named entity 'p53' named entity 'STAT1' named entity 'upregulation' named entity 'COL17A1' named entity 'p53' named entity 'antiviral' named entity 'pyroptosis' named entity 'SOCS1' named entity 'NLRX1' named entity 'NLRX1' named entity 'inflammation' named entity 'IFI16' named entity 'STING' named entity 'caspase-1' named entity 'Actinomycin' named entity 'IFIT3' named entity 'STING' named entity 'STING' named entity 'upregulation' named entity 'Synergistic' named entity 'ectodomain' named entity 'STING' named entity 'IFIT3' named entity 'caspase-1' named entity 'IFIT1' named entity 'IFI16' named entity 'caspase-1' named entity 'A549' named entity 'NLRP1' named entity 'NLRP1' named entity 'interferons' named entity 'p53' named entity 'interferon' named entity 'p53' named entity 'p53' named entity 'knockdown' named entity 'cells' named entity 'pyroptosis' named entity 'caspase-1' named entity 'nutlin' named entity 'p53'

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