Key result
LPS-mediated NLRP3 inflammasome priming is dependent on ERK1 phosphorylation and proteasome function, licensing the inflammasome for ATP-induced activation independent of new protein synthesis.
Population
Human monocytes
Design
Preclinical
Authors
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May guide ERK1-targeted studies in cardiovascular inflammation; hypothesis-generating from animal data only.
ERK1-mediated posttranslational modifications, dependent on proteasome function and ROS, are essential for rapid LPS-induced priming of the NLRP3 inflammasome.
Shamaa et al. (2014) studied LPS-mediated NLRP3 inflammasome priming. LPS priming and ATP activation was evaluated on Caspase-1 activity and IL-18 release. LPS-mediated NLRP3 inflammasome priming is dependent on ERK1 phosphorylation and proteasome function, licensing the inflammasome for ATP-induced activation independent of new protein synthesis.
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