The receptor TK activity of EGFR can be activated by multiple ligands, such as EGF.
Dynamin activity has been shown to be activated by multiple phosphoinositides, including PI(3 P, PI(4 P and PI 4,5 P2, in vitro (Yarar et al, 2008).
Although the level of pERK, an upstream activator of pCREB, was reduced in the present study, CREB can be activated by multiple signal pathways including PI3K/Akt and Ca/CaM/CaMK IV signalling [ 37, 38].
SRC can be activated by multiple classes of membrane receptors, such as G protein-coupled receptors, cell adhesion molecules, and integrins.
Although individual STAT proteins may be activated by multiple ligands, certain cytokines preferentially activate particular STATs.
In turn, SpkK1 can be activated by multiple stimuli as IGF-1 signaling [ 14].
PI3-K itself is activated by multiple mechanisms, including the activation of growth factor receptor tyrosine kinases [ 5, 6] and G protein-coupled receptors [ 7, 8], integrin-mediated cell adhesion [ 7, 8], and the actions of oncogene products such as Ras [ 9, 10] and hormones such as estrogen [ 11- 13].
Similarly, the transcriptional activity of the NF-κB complex is activated by multiple stresses, including oxidative, shear, ER, and hypoxic stress [ 47- 51], and is predicted to have increased activity in three of the four data sets: hypoxia, OxPAPC, and hyperoxia.
Stress-activated protein kinase/c-Jun N-terminal kinase is activated by multiple forms of stress including UV, radiation, inflammatory cytokines, and has been implicated as a mediator of stress-induced apoptosis (Davis, 2000).
AMPK itself is activated by multiple mechanisms including phosphorylation by the tumor suppressor LKB1/STK11 kinase in response to increased AMP or ADP levels in the cell11, 12.
The transcription factor Stat3 is activated by multiple cytokines, including leptin and those signaling through the gp130 receptor.
