At a concentration of 100 micromolar, leucine produces the maximum possible increase in insulin-driven GSK3β phosphorylation and glycogen synthesis in human muscle cells; higher concentrations up to...
Mechanism
Synthesis from 1 study
Leucine helps insulin turn on a signal that shuts down a blocker of sugar storage. Once enough leucine is present to fully shut down that blocker, adding more doesn’t help because the system is already working at its maximum capacity.
Most probable mechanism
When leucine is present at a certain level, it helps insulin work more effectively to turn on a key signal that shuts off a brake on sugar storage. Once this brake is fully released, adding more leucine doesn’t help any further because the system is already running at full capacity.
Leucine pre-exposure primes the insulin signaling pathway to amplify the activation of AKT in response to insulin binding
Amplified AKT phosphorylation at Ser473 leads to maximal phosphorylation and inactivation of GSK3β at Ser21/9
Inactivated GSK3β no longer suppresses glycogen synthase, allowing glycogen synthase to remain active and catalyze glycogen synthesis at its maximum rate
At leucine concentrations above 100 μM, no further increase in AKT or GSK3β phosphorylation occurs, indicating the system has reached saturation
Evidence from Studies
Supporting (1)
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Leucine modulates dynamic phosphorylation events in insulin signaling pathway and enhances insulin-dependent glycogen synthesis in human skeletal muscle cells
Contradicting (0)
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