Ludwig 3.0 Activation Keyl 👑

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Ludwig 3.0 Activation Keyl

Presumably, the classical translation coupling mechanism, in which PI3K phosphorylates Akt at threonine 308 and serine 473, leads to increases in protein synthesis ( Figure 2 ). The currently accepted mechanism by which the insulin-dependent increase in cell growth induced by Akt-dependent phosphorylation of the eukaryotic translation initiation factor 4E binding protein 1(4EBP1) confers the effects on protein synthesis, involves inactivation of the forkhead box O1 (FoxO1) transcriptional repressor, and resultant activation of the metabolic gene transcription factor, nuclear factor of activated T cells (NFAT), which results in the transcription of genes required for protein synthesis. The activated FoxO1 is sequestered by 14-3-3 into the nucleus and 4EBP1 is translationally repressed.

Second, insulin-mediated activation of Akt in the CNS results in the expected alterations in protein synthesis in the short term (5 minutes) in a large number of different animal models of obesity, stress, and circadian alterations in SNA, all of which can be reversed by inhibiting PI3K with LY294002 (see Table 3 ). On the other hand, the activation of NFAT is thought to result in protein synthesis in the long term (hours to days) and requires the involvement of protein synthesis independent factors, such as transcriptional cofactors (101). The second alternative might suggest that the insulin-mediated increase in cell growth, measured by increases in DNA synthesis, does not result from Akt-mediated activation of the metabolism gene transcription factor, NFAT, and that insulin-mediated stimulation of protein synthesis as measured by increases in protein synthesis result from the activation of a separate pathway. However, as shown in Table 2, an inhibitor of SGK would block the alterations in protein synthesis.

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