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Cells must respond in an appropriate fashion to many complex signaling events. Extracellular signaling cues are organized into well defined signal transduction modules that control fundamental cellular behavior. Two prominent signaling modules that are among the best characterized are the p44/42 MAP kinase (ERK MAPK) and Akt signal transduction pathways. These signaling modules control cellular growth, proliferation, movement, survival, and death. The p44/42 MAPK is activated by a wide variety of extracellular signals including growth and neurotrophic factors, cytokiones, hormones, and neurotransmitters. p44/42 MAPK activation occurs through phosphorylation of theronine and tyrosine at the sequence T*EY* by a dual specificity kinase called MAP kinase kinase (MEK). The Akt protein kinase is generally activated in response to growth factor stimulation and phosphorylated on Ser473. Growth factor stimulation results in phosphorylation of S6 Ribosomal protein on Ser235/236, leading to an increase in protein synthesis and cell cycle progression. Phosphorylation levels of critical molecular switches such as MAPKs and Akt therefore serve as a reliable indicator of the activation state of the entire signaling module. The profiling of phosphorlation events using phospho-specific antibodies is now widely used to investigate diagnostic pathology (1,2). The PathScan® Signaling Nodes II 4-Plex Array Kit provides the researcher with means to profile numerous chemical compounds and obtain in-cell relative potency (3).
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