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10.1042/BSR20100111 http://scihub22266oqcxt.onion/10.1042/BSR20100111 C4485920!4485920!20942802     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biosci+Rep 2011 ; 31 (4): 283-94 Nephropedia Template TP {{tp|p=20942802|t=2011. Molecular determinants involved in activation of caspase 7 |pdf=|usr=}}{{20942802}} gab.com Text Molecular determinants involved in activation of caspase 7 JO: Biosci Rep http://www.kidney.de/pget.php?&tw=1&pmid=20942802 #FOAvip During apoptosis, initiator caspases (8, 9, and 10) activate downstream executioner caspases (3, 6, and 7) by cleaving the interdomain connector (IDC) at two sites. Here, we demonstrate that both activation sites, site 1 and site 2, of caspase 7 are suboptimal for activation by initiator caspases 8 and 9 in cellulo, and in vitro using recombinant proteins and activation kinetics. Indeed, when both sites are replaced with the preferred motifs recognized by either caspases 8 and 9, we measured improvement in activation of up to 36 folds. Moreover, cleavage at site 1 is preferred over site 2 because of its location within the IDC since swapping sites does not lead to a more efficient activation. We also demonstrate the paramount role of Ile195 of site 1 involved in maintaining a network of contacts that preserves the proper conformation of the active enzyme. Finally, we show that the length of the IDC plays a crucial role in maintaining the need for proteolysis for activation. In fact, although we were unable to generate a caspase 7 that does not require proteolysis for activity, shortening the IDC of the initiator caspase 8 by four residues was sufficient to confer a requirement for proteolysis, a key feature of executioner caspases. Altogether, the results demonstrate the critical role of the primary structure of caspase 7?s IDC for its activation and proteolytic activity. Twit Text FOAVip Molecular determinants involved in activation of caspase 7 ????Biosci Rep http://www.kidney.de/pget.php?&tw=1&pmid=20942802 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=20942802 #FOAvip English Wikipedia <ref>{{Cite pmid|20942802}}</ref> Molecular determinants involved in activation of caspase 7 #MMPMID20942802 BOUCHER D; BLAIS V; DRAG M; DENAULT JB Biosci Rep 2011[Aug]; 31 (4): 283-94 PMID20942802show ga During apoptosis, initiator caspases (8, 9, and 10) activate downstream executioner caspases (3, 6, and 7) by cleaving the interdomain connector (IDC) at two sites. Here, we demonstrate that both activation sites, site 1 and site 2, of caspase 7 are suboptimal for activation by initiator caspases 8 and 9 in cellulo, and in vitro using recombinant proteins and activation kinetics. Indeed, when both sites are replaced with the preferred motifs recognized by either caspases 8 and 9, we measured improvement in activation of up to 36 folds. Moreover, cleavage at site 1 is preferred over site 2 because of its location within the IDC since swapping sites does not lead to a more efficient activation. We also demonstrate the paramount role of Ile195 of site 1 involved in maintaining a network of contacts that preserves the proper conformation of the active enzyme. Finally, we show that the length of the IDC plays a crucial role in maintaining the need for proteolysis for activation. In fact, although we were unable to generate a caspase 7 that does not require proteolysis for activity, shortening the IDC of the initiator caspase 8 by four residues was sufficient to confer a requirement for proteolysis, a key feature of executioner caspases. Altogether, the results demonstrate the critical role of the primary structure of caspase 7?s IDC for its activation and proteolytic activity. äMolecular determinants involved in activation of caspase 7 (epmc).pdf DeepDyve Pubget Overpricing