Now showing 1 - 2 of 2
  • 2009Journal Article
    [["dc.bibliographiccitation.firstpage","1079"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Microbes and Infection"],["dc.bibliographiccitation.lastpage","1087"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Graumann, Kristin"],["dc.contributor.author","Hippe, Diana"],["dc.contributor.author","Gross, Uwe"],["dc.contributor.author","Lueder, Carsten Guenter Kurt"],["dc.date.accessioned","2018-11-07T11:22:58Z"],["dc.date.available","2018-11-07T11:22:58Z"],["dc.date.issued","2009"],["dc.description.abstract","Programmed cell death is an essential mechanism of the host to combat infectious agents and to regulate immunity during infection Consequently, activation and deactivation of the hosts' cell death pathways by protozoan parasites play critical roles in parasite control. pathogenesis, immune evasion and parasite dissemination within the host Here, we discuss advances in the understanding of these fascinating host-parasite interactions with special emphasis on how protozoa can modulate the cell death apparatus of its host. (C) 2009 Elsevier Masson SAS All rights reserved."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [LU777/4-1]"],["dc.identifier.doi","10.1016/j.micinf.2009.08.011"],["dc.identifier.isi","000271557300011"],["dc.identifier.pmid","19733682"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56091"],["dc.notes.status","zu prĂĽfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1286-4579"],["dc.title","Mammalian apoptotic signalling pathways: multiple targets of protozoan parasites to activate or deactivate host cell death"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]
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  • 2015Journal Article
    [["dc.bibliographiccitation.firstpage","150"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Microbial Cell"],["dc.bibliographiccitation.lastpage","162"],["dc.bibliographiccitation.volume","2"],["dc.contributor.author","Graumann, Kristin"],["dc.contributor.author","Schaumburg, Frieder"],["dc.contributor.author","Reubold, Thomas"],["dc.contributor.author","Hippe, Diana"],["dc.contributor.author","Eschenburg, Susanne"],["dc.contributor.author","LĂĽder, Carsten G. K."],["dc.date.accessioned","2019-07-09T11:42:42Z"],["dc.date.available","2019-07-09T11:42:42Z"],["dc.date.issued","2015"],["dc.description.abstract","Inhibition of programmed cell death pathways of mammalian cells often facilitates the sustained survival of intracellular microorganisms. The apicomplexan parasite Toxoplasma gondii is a master regulator of host cell apoptotic pathways. Here, we have characterized a novel anti-apoptotic activity of T. gondii. Using a cell-free cytosolic extract model, we show that T. gondii interferes with the activities of caspase 9 and caspase 3/7 which have been induced by exogenous cytochrome c and dATP. Proteolytic cleavage of caspases 9 and 3 is also diminished suggesting inhibition of holo-apoptosome function. Parasite infection of Jurkat T cells and subsequent triggering of apoptosome formation by exogenous cytochrome c in vitro and in vivo indicated that T. gondii also interferes with caspase activation in infected cells. Importantly, parasite inhibition of cytochrome c-induced caspase activation considerably contributes to the overall anti-apoptotic activity of T. gondii as observed in staurosporine-treated cells. Co-immunoprecipitation showed that T. gondii abolishes binding of caspase 9 to Apaf-1 whereas the interaction of cytochrome c with Apaf-1 remains unchanged. Finally, T. gondii lysate mimics the effect of viable parasites and prevents holo-apoptosome functionality in a reconstituted in vitro system comprising recombinant Apaf-1 and caspase 9. Beside inhibition of cytochrome c release from host cell mitochondria, T. gondii thus also targets the holo-apoptosome assembly as a second mean to efficiently inhibit the caspase-dependent intrinsic cell death pathway."],["dc.identifier.doi","10.15698/mic2015.05.201"],["dc.identifier.fs","618353"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13656"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58731"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.issn","2311-2638"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Toxoplasma gondii inhibits cytochrome c-induced caspase activation in its host cell by interference with holo-apoptosome assembly"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
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