<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Saleh, Maya</style></author><author><style face="normal" font="default" size="100%">Mathison, John C</style></author><author><style face="normal" font="default" size="100%">Wolinski, Melissa K</style></author><author><style face="normal" font="default" size="100%">Bensinger, Steve J</style></author><author><style face="normal" font="default" size="100%">Fitzgerald, Patrick</style></author><author><style face="normal" font="default" size="100%">Droin, Nathalie</style></author><author><style face="normal" font="default" size="100%">Ulevitch, Richard J</style></author><author><style face="normal" font="default" size="100%">Green, Douglas R</style></author><author><style face="normal" font="default" size="100%">Nicholson, Donald W</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice.</style></title><secondary-title><style face="normal" font="default" size="100%">Nature</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Nature</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Caspase 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Caspase 12</style></keyword><keyword><style  face="normal" font="default" size="100%">Caspase Inhibitors</style></keyword><keyword><style  face="normal" font="default" size="100%">Caspases</style></keyword><keyword><style  face="normal" font="default" size="100%">Catalysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Disease Susceptibility</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Interferon-gamma</style></keyword><keyword><style  face="normal" font="default" size="100%">Interleukin-1</style></keyword><keyword><style  face="normal" font="default" size="100%">Interleukin-18</style></keyword><keyword><style  face="normal" font="default" size="100%">Listeria monocytogenes</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Knockout</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Peritonitis</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Sepsis</style></keyword><keyword><style  face="normal" font="default" size="100%">Shock, Septic</style></keyword><keyword><style  face="normal" font="default" size="100%">Survival Rate</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2006 Apr 20</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">440</style></volume><pages><style face="normal" font="default" size="100%">1064-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Caspases function in both apoptosis and inflammatory cytokine processing and thereby have a role in resistance to sepsis. Here we describe a novel role for a caspase in dampening responses to bacterial infection. We show that in mice, gene-targeted deletion of caspase-12 renders animals resistant to peritonitis and septic shock. The resulting survival advantage was conferred by the ability of the caspase-12-deficient mice to clear bacterial infection more efficiently than wild-type littermates. Caspase-12 dampened the production of the pro-inflammatory cytokines interleukin (IL)-1beta, IL-18 (interferon (IFN)-gamma inducing factor) and IFN-gamma, but not tumour-necrosis factor-alpha and IL-6, in response to various bacterial components that stimulate Toll-like receptor and NOD pathways. The IFN-gamma pathway was crucial in mediating survival of septic caspase-12-deficient mice, because administration of neutralizing antibodies to IFN-gamma receptors ablated the survival advantage that otherwise occurred in these animals. Mechanistically, caspase-12 associated with caspase-1 and inhibited its activity. Notably, the protease function of caspase-12 was not necessary for this effect, as the catalytically inactive caspase-12 mutant Cys299Ala also inhibited caspase-1 and IL-1beta production to the same extent as wild-type caspase-12. In this regard, caspase-12 seems to be the cFLIP counterpart for regulating the inflammatory branch of the caspase cascade. In mice, caspase-12 deficiency confers resistance to sepsis and its presence exerts a dominant-negative suppressive effect on caspase-1, resulting in enhanced vulnerability to bacterial infection and septic mortality.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">7087</style></issue><custom1><style face="normal" font="default" size="100%">&lt;p&gt;http://www.ncbi.nlm.nih.gov/pubmed/16625199?dopt=Abstract&lt;/p&gt;
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