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10.3727/000000001783992605 http://scihub22266oqcxt.onion/10.3727/000000001783992605 C5964942!5964942 !11444529     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=11444529 &cmd=llinks): Failed to open stream: HTTP request failed! 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Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c |pdf=|usr=}}{{11444529 }} gab.com Text Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c JO: Gene Expr http://www.kidney.de/pget.php?&tw=1&pmid=11444529 #FOAvip Mitochondrial cytochrome c release in response to pro-apoptotic signals leads to the formation of a cytochrome c/Apaf-1/procaspase-9 complex (the apoptosome) and resultant activation of caspase-9 and caspase-3. Here we demonstrate that the molecular chaperone, Hsp27, inhibits this cytochrome c-mediated activation of caspase-3. Immunodepeletion of Hsp27 from cytochrome c-activated cytosols resulted in decreased caspase activity. Furthermore, immunoprecipitation of Hsp27 resulted in the coprecipitation of both cytochrome c and procaspase-3. In reciprocal experiments, immunoprecipitation of both procaspase-3 and cytochrome c resulted in coprecipitation of Hsp27, indicating two independent interactions. These results point to Hsp27 mediating its inhibition of procaspase-3 activation through its ability to sequester both cytochrome c and procaspase-3, and thus prevent the correct formation/function of the apoptosome complex. Twit Text FOAVip Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c ????Gene Expr http://www.kidney.de/pget.php?&tw=1&pmid=11444529 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=11444529 #FOAvip English Wikipedia <ref>{{Cite pmid|11444529 }}</ref> Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c #MMPMID11444529 Concannon CG ; Orrenius S ; Samali A Gene Expr 2001[]; 9 (4-5 ): 195-201 PMID11444529 show ga Mitochondrial cytochrome c release in response to pro-apoptotic signals leads to the formation of a cytochrome c/Apaf-1/procaspase-9 complex (the apoptosome) and resultant activation of caspase-9 and caspase-3. Here we demonstrate that the molecular chaperone, Hsp27, inhibits this cytochrome c-mediated activation of caspase-3. Immunodepeletion of Hsp27 from cytochrome c-activated cytosols resulted in decreased caspase activity. Furthermore, immunoprecipitation of Hsp27 resulted in the coprecipitation of both cytochrome c and procaspase-3. In reciprocal experiments, immunoprecipitation of both procaspase-3 and cytochrome c resulted in coprecipitation of Hsp27, indicating two independent interactions. These results point to Hsp27 mediating its inhibition of procaspase-3 activation through its ability to sequester both cytochrome c and procaspase-3, and thus prevent the correct formation/function of the apoptosome complex. |*Caspase Inhibitors [MESH] |Apoptosis [MESH] |Caspase 3 [MESH] |Caspases/*metabolism [MESH] |Cytochrome c Group/*metabolism [MESH] |Enzyme Activation [MESH] |Enzyme Precursors/*metabolism [MESH] |Heat-Shock Proteins/immunology/*metabolism [MESH] |Humans [MESH] |Jurkat Cells [MESH] |Mitochondria/enzymology [MESH] |Precipitin Tests [MESH] |Protein Binding [MESH]Hsp27 inhibits cytochrome c-mediated caspase activation by sequesterin(epmc).pdf DeepDyve Pubget Overpricing