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Article: Requirement of FADD for tumor necrosis factor-induced activation of acid sphingomyelinase

TitleRequirement of FADD for tumor necrosis factor-induced activation of acid sphingomyelinase
Authors
Issue Date1999
Citation
Journal of Biological Chemistry, 1999, v. 274, n. 9, p. 5267-5270 How to Cite?
AbstractThe generation of mice strains deficient for select members of the signaling complex of the 55-kDa tumor necrosis factor receptor (TNF-R55) has allowed the assignment of specific cellular responses to distinct TNF-R55- associated proteins. In particular, the TNF-R55-associated protein FADD seems to be responsible for recruitment and subsequent activation of caspase 8. In this report we demonstrate the requirement of FADD for TNF-induced activation of endosomal acid sphingomyelinase (A-SMase). In primary embryonic fibroblasts from FADD-deficient mice the activation of A-SMase by TNF-R55 ligation was almost completely impaired. This effect is specific in that other TNF responses like activation of NF-κB or neutral (N-)SMase remained unaffected. In addition, interleukin-1-induced activation of A-SMase in FADD- deficient cells was unaltered. In FADD(-/-) embryonic fibroblasts reconstituted by transfection with a FADD cDNA expression construct, the TNF responsiveness of A-SMase was restored. The results of this study suggest that FADD, in addition to its role in triggering a proapoptotic caspase cascade, is required for TNF-induced activation of A-SMase.
Persistent Identifierhttp://hdl.handle.net/10722/291507
ISSN
2020 Impact Factor: 5.157
2023 SCImago Journal Rankings: 1.766
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWiegmann, Katja-
dc.contributor.authorSchwandner, Ralf-
dc.contributor.authorKrut, Oleg-
dc.contributor.authorYeh, Wen Chen-
dc.contributor.authorMak, Tak W.-
dc.contributor.authorKrönke, Martin-
dc.date.accessioned2020-11-17T14:54:31Z-
dc.date.available2020-11-17T14:54:31Z-
dc.date.issued1999-
dc.identifier.citationJournal of Biological Chemistry, 1999, v. 274, n. 9, p. 5267-5270-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10722/291507-
dc.description.abstractThe generation of mice strains deficient for select members of the signaling complex of the 55-kDa tumor necrosis factor receptor (TNF-R55) has allowed the assignment of specific cellular responses to distinct TNF-R55- associated proteins. In particular, the TNF-R55-associated protein FADD seems to be responsible for recruitment and subsequent activation of caspase 8. In this report we demonstrate the requirement of FADD for TNF-induced activation of endosomal acid sphingomyelinase (A-SMase). In primary embryonic fibroblasts from FADD-deficient mice the activation of A-SMase by TNF-R55 ligation was almost completely impaired. This effect is specific in that other TNF responses like activation of NF-κB or neutral (N-)SMase remained unaffected. In addition, interleukin-1-induced activation of A-SMase in FADD- deficient cells was unaltered. In FADD(-/-) embryonic fibroblasts reconstituted by transfection with a FADD cDNA expression construct, the TNF responsiveness of A-SMase was restored. The results of this study suggest that FADD, in addition to its role in triggering a proapoptotic caspase cascade, is required for TNF-induced activation of A-SMase.-
dc.languageeng-
dc.relation.ispartofJournal of Biological Chemistry-
dc.titleRequirement of FADD for tumor necrosis factor-induced activation of acid sphingomyelinase-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/jbc.274.9.5267-
dc.identifier.pmid10026132-
dc.identifier.scopuseid_2-s2.0-0033605293-
dc.identifier.volume274-
dc.identifier.issue9-
dc.identifier.spage5267-
dc.identifier.epage5270-
dc.identifier.isiWOS:000078804400003-
dc.identifier.issnl0021-9258-

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