In adults aged 74 on average, a protein bar with 16 grams of protein and 1.5 grams of added leucine produces the same essential amino acid exposure in the bloodstream as a meal with 32 grams of...
Mechanism
Synthesis from 1 study
The extra leucine tells the muscles to start building protein right away, which stops the body from breaking down the other amino acids too fast. This lets the small amount of protein in the bar last as long in the blood as a much bigger meal would.
Most probable mechanism
When a small amount of protein with extra leucine is eaten after a low-protein meal, the free leucine quickly enters the blood and signals the body to hold onto all essential amino acids instead of breaking them down, making the small protein dose act like a much larger one.
Free leucine is rapidly absorbed from the gastrointestinal tract into systemic circulation, achieving plasma concentrations exceeding 500 µM within one hour after ingestion.
Elevated plasma leucine binds to Sestrin2 in skeletal muscle, relieving inhibition of the mTORC1 complex and triggering its activation.
Activated mTORC1 increases phosphorylation of p70S6K and 4E-BP1, enhancing ribosomal translation initiation and stimulating muscle protein synthesis.
Increased muscle protein synthesis creates a metabolic sink that reduces the catabolism of essential amino acids, prolonging their systemic availability and elevating net exposure.
Evidence from Studies
Supporting (1)
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Consumption of High-Leucine-Containing Protein Bar Following Breakfast Impacts Aminoacidemia and Subjective Appetite in Older Persons
Contradicting (0)
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