Mike Arnold
Board Sponsor
- Awards
- 3
Can Today's EAA Products Activate Muscle Growth?
When it comes to growing muscle tissue, essential amino acids are the most effective product on the market, but how do they work? Aside from providing the building blocks for muscle growth, they are known for activating of one of the body's most powerful growth regulators, mTOR. Leucine is the major player here, and for this reason we saw BCAA products (a combination of leucine, isoleucine, and valine) dominate the market for years. But recently, research has shown that having all 9 EEAs present (which includes the BCAAs) is a much more effective option.
But what if this wasn't the most effective option? What if EAAs actually weren't able to activate mTOR by themselves? Impossible, right? Wrong. As it turns out, EAAs can NOT activate mTOR without first being exposed to "priming" amino acids. This 2-step process, known as priming & activation, is critical for mTOR-mediated muscle growth to occur.
The take home message here is simple.
If your amino acid product does not contain one or more of these "priming" amino acids, it cannot stimulate mTOR-mediated muscle growth. The body MUST have one or more of these amino acids present in order for EAA products to do their job. If you're already have adequate quantities of these aminos circulating in your bloodstream, you're covered. If not, you're screwed. What does this mean for people who use EEA products prior to training in the morning...or at any other time they haven't eaten for a while? It means they aren't able to activate mTOR, which means they can't effectively activate protein synthesis, which means they can't effectively stimulate muscle growth.
The solution? Make sure your EAA product contains these priming aminos.
Below you will find one of many studies explaining this reality.
Amino Acids Regulate mTORC1 by an Obligate Two-step Mechanism
Julia Dyachok 1 2 3, Svetlana Earnest 1, Erica N Iturraran 1 2, Melanie H Cobb 1, Elliott M Ross 4 2
Affiliations expand
- PMID: 27587390
- PMCID: PMC5077182
- DOI: 10.1074/jbc.M116.732511
Erratum in
- Correction: Amino acids regulate mTORC1 by an obligate two-step mechanism.
Dyachok J, Earnest S, Iturraran EN, Cobb MH, Ross EM.J Biol Chem. 2020 Jun 26;295(26):8868. doi: 10.1074/jbc.AAC120.014360.PMID: 32591444 Free PMC article. No abstract available.
The mechanistic target of rapamycin complex 1 (mTORC1) coordinates cell growth with its nutritional, hormonal, energy, and stress status. Amino acids are critical regulators of mTORC1 that permit other inputs to mTORC1 activity. However, the roles of individual amino acids and their interactions in mTORC1 activation are not well understood. Here we demonstrate that activation of mTORC1 by amino acids includes two discrete and separable steps: priming and activation. Sensitizing mTORC1 activation by priming amino acids is a prerequisite for subsequent stimulation of mTORC1 by activating amino acids. Priming is achieved by a group of amino acids that includes l-asparagine, l-glutamine, l-threonine, l-arginine, l-glycine, l-proline, l-serine, l-alanine, and l-glutamic acid. The group of activating amino acids is dominated by l-leucine but also includes l-methionine, l-isoleucine, and l-valine. l-Cysteine predominantly inhibits priming but not the activating step. Priming and activating steps differ in their requirements for amino acid concentration and duration of treatment. Priming and activating amino acids use mechanisms that are distinct both from each other and from growth factor signaling. Neither step requires intact tuberous sclerosis complex of proteins to activate mTORC1. Concerted action of priming and activating amino acids is required to localize mTORC1 to lysosomes and achieve its activation.
