Glutamine

So a really good point that you bring up.

I will say that cancer metabolism is absolutely essential to sustain only in the presence of glucose and glutamine.

But that is not the case for methionine, alanine, other gluconeogenic amino acids however methionine uh as you can use in a radio labeled methionine scan uh that what the cancer does it uses methionine for biosynthesis and it uses alanine for by and also tyrosine and and tryptophan uh but for fuels if we're just talking about energetic fuels methionine Glutamine is by far, like far, far more important for the fuel for cancer than any other amino acid.

It's also more available, like, you know, in circulation, most abundant.

So by that, you know, and there's no...

So you've got to be a little bit careful with that.

But there are other ways to target glutamine.

Glutamine, one way would just do, you know, moderate protein, do a lower protein ketogenic diet with the two things that I mentioned and exogenous ketones.

Okay, now here's the third one I opened with.

Glutamine is mechanistically one of the most heavily studied amino acid dependencies in cancer metabolism.

Almost all cell lines and a couple of tumors are described in the literature as genuinely glutamine-addicted, using it to fuel both energy production and biosynthesis.

And yet, glutamine restriction is essentially never appearing as a real dietary intervention in serious clinical research.

Why? For a simple, unavoidable biological reason.

Glutamine is a non-essential amino acid.

Unlike methionine, which the body cannot manufacture and must obtain from food, healthy human cells, including liver and muscle tissue, synthesize their own glutamine continuously, and they will simply increase that internal production to compensate for anything cut from your diet.

You cannot starve a tumor of glutamine by adjusting what you eat, because your body actively works around the restriction.

Now, remember the transporters, SLC38A2.

Glutamine is taken up by that transporter, and that facilitates a nutrient-sensitive production of a protein complex.

Protein complex, I also have mentioned just briefly, that's the FLCN FNIP2 complex.

Now, why that's important, I'm not going to give you the detail of that complex right now, only in that it inhibits the transcription factor, okay? And the transcription factor here is TFEB.

You have to have them in the diet, whereas other amino acids can be created within our body.

Glutamine is an interesting amino acid.

It's the most abundant amino acid in our bloodstream.

So a glutamine dominates all the other amino acids.

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The brain's moment-to-moment function depends on maintaining an optimal balance between excitatory, glutamate-driven, and inhibitory GABA-mediated neurotransmission.

Glutamine, derived from dietary protein and synthesized endogenously, serves as the precursor for both glutamate and, through the glutamine-glutamate-GABA cycle, for gamma-aminobutyric acid, GABA.

the brain's main inhibitory neurotransmitter.

Glycine and serine, both nonessential amino acids synthesized from other amino acids and carbohydrates, co-act at NMDA receptors to regulate synaptic plasticity, the brain's ability to form, strengthen, and prune synaptic connections essential for learning and memory.

This forms the barrier to your immune system deeper inside, but your intestinal cells are very hungry for glutamine.

In fact, out of all the glutamine, they hog like 30% of it for themselves.

Glutamine is very important in producing ATP energy.

Glutamine fuels the intestinal layer of the cells as well as the mucosal layer where all the good bacteria hang out.

And glutamine supports tight junctions.

You see, I originally talked about this gut being a source of inflammation, but I didn't describe exactly what's occurring.