File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development

TitleRequirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development
Authors
Issue Date2000
Citation
Immunity, 2000, v. 12, n. 6, p. 633-642 How to Cite?
AbstractCasper (c-FLIP) associates with FADD and caspase-8 in signaling complexes downstream of death receptors like Fas. We generated Casper-deficient mice and cells and noted a duality in the physiological functions of this molecule. casper(-/-) embryos do not survive past day 10.5 of embryogenesis and exhibit impaired heart development. This phenotype is reminiscent of that reported for FADD(-/-) and caspase-8(-/-) embryos. However, unlike FADD(-/-) and caspase-8(-/-) cells, casper(-/-) embryonic fibroblasts are highly sensitive to FasL- or TNF-induced apoptosis and show rapid induction of caspase activities. NF-κB and JNK/SAPK activation is intact in TNF-stimulated casper(-/-) cells. These results suggest that Casper has two distinct roles: to cooperate with FADD and caspase-8 during embryonic development and to mediate cytoprotection against death factor-induced apoptosis.
Persistent Identifierhttp://hdl.handle.net/10722/291510
ISSN
2023 Impact Factor: 25.5
2023 SCImago Journal Rankings: 13.578
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYeh, Wen Chen-
dc.contributor.authorItie, Annick-
dc.contributor.authorElia, Andrew J.-
dc.contributor.authorNg, Michelle-
dc.contributor.authorShu, Hong Bing-
dc.contributor.authorWakeham, Andrew-
dc.contributor.authorMirtsos, Christine-
dc.contributor.authorSuzuki, Nobutaka-
dc.contributor.authorBonnard, Madeleine-
dc.contributor.authorGoeddel, David V.-
dc.contributor.authorMak, Tak W.-
dc.date.accessioned2020-11-17T14:54:31Z-
dc.date.available2020-11-17T14:54:31Z-
dc.date.issued2000-
dc.identifier.citationImmunity, 2000, v. 12, n. 6, p. 633-642-
dc.identifier.issn1074-7613-
dc.identifier.urihttp://hdl.handle.net/10722/291510-
dc.description.abstractCasper (c-FLIP) associates with FADD and caspase-8 in signaling complexes downstream of death receptors like Fas. We generated Casper-deficient mice and cells and noted a duality in the physiological functions of this molecule. casper(-/-) embryos do not survive past day 10.5 of embryogenesis and exhibit impaired heart development. This phenotype is reminiscent of that reported for FADD(-/-) and caspase-8(-/-) embryos. However, unlike FADD(-/-) and caspase-8(-/-) cells, casper(-/-) embryonic fibroblasts are highly sensitive to FasL- or TNF-induced apoptosis and show rapid induction of caspase activities. NF-κB and JNK/SAPK activation is intact in TNF-stimulated casper(-/-) cells. These results suggest that Casper has two distinct roles: to cooperate with FADD and caspase-8 during embryonic development and to mediate cytoprotection against death factor-induced apoptosis.-
dc.languageeng-
dc.relation.ispartofImmunity-
dc.titleRequirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1016/S1074-7613(00)80214-9-
dc.identifier.pmid10894163-
dc.identifier.scopuseid_2-s2.0-0033662341-
dc.identifier.volume12-
dc.identifier.issue6-
dc.identifier.spage633-
dc.identifier.epage642-
dc.identifier.isiWOS:000087937300005-
dc.identifier.issnl1074-7613-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats