Extracellular signal‐regulated kinases (ERKs) are key genes in activating survival pathways (Roskoski, 2012), and their transient activation plays an important role in memory‐related processes (Costa & Silva, 2002).
Previous work indicated that hemolytic GBS strains activate the NLRP3 inflammasome in mouse dendritic cells (Costa et al, 2012) and recently, RNA was implicated in hemolysin-mediated NLRP3 activation (Gupta et al, 2014).
The mechanisms underlying the cell death response of cancer cells following withdrawal of oncogene-addicting signals are complex but appear to result in part from activation of the pro-apoptotic proteins BIM and PUMA (Costa et al., 2007; Gong et al., 2007; Bean et al., 2013).
Because NLRP3 activation occurs only in the presence of hemolytic GBS (Costa et al, 2012; Gupta et al, 2014), we aimed to understand how the purified GBS pigment activates the inflammasome, induces cell death, and establish the consequence on fetal injury.
Our group has previously identified JNK activation as being necessary for Fas-mediated apoptosis in DU 145 cells (Costa-Pereira et al, 2000; Curtin and Cotter, 2002).
There are less crowded resorts on the Costa de la Luz, the Costa Tropical and Costa de Almería.
Additional analysis identified activation of the stress kinase JNK as an integral event in this process (Costa-Pereira et al, 2000).
Our group has previously demonstrated that JNK activation is sufficient to sensitise DU 145 cells to Fas receptor-mediated apoptosis (Costa-Pereira et al, 2000; Curtin and Cotter, 2002).
The activation of JNK using chemotherapeutic drugs or anisomycin was sufficient to sensitise these cells to Fas (Costa-Pereira and Cotter, 1999; Costa-Pereira et al, 2000; Curtin and Cotter, 2002).
Activation of the stress kinase JNK was found to be essential in potentiating Fas mediated apoptosis (Costa-Pereira et al, 2000).
