Pro-tip: Plants have feelings too, they didn’t want to be eaten.
This is a little motif that can be carried out in regards to food and evolution in general; nothing evolves for the purpose of satiating another being’s belly.
In order to live, plant and humans need similar nutrients; in effect we are stealing theirs via consumption. In order to survive, plants will create defenses to prevent being eaten.
Some of the most successful plants have physical defenses (thistles) or chemical defenses (hemlock) that prevent predators, for the most part, from eating them. Except some highly adapted or stupid predators.
Some plants suck at it though. Broccoli has created glucosinolates that have a bitter taste (which has not stopped us from eating it), and Cocoa has developed a potent insecticide which was later discovered to be a nice stimulant and has become the world’s favorite drug. (I speak of caffeine here, the reason caffeine exists is due to it’s insecticidal effect)
Other compounds, such as will be discussed below, are kind of half way. These compounds aren’t going to kill you straight like hemlock, but they are not necessarily harmless either. This includes compounds like gliadin and phytohaemagglutinin.
Lectins, by definition, are proteins which bind to sugars and are highly specific to the sugars that they bind to. I want to point out that this definition (the true definition of lectins) is not inherently bad. It seems the media is taking smaller and negative compounds that belong to this category and defiling the category by association.
A gluten is part lectin, hence why it follows it up; ‘gluten’ is not one compound, but a word used to describe a union between two subunits. Gluten units by nature are mostly insoluble in water.
Glutens are made up of two subunits, the first is called a Glutelin subunit (of which the most common is glutenin from the Triticum family) and also of a Prolamin subunit (of which the most common is gliadin). The last buzzword is the one to actually remember.
Take-away: Glutens are made up of two subunits and and the word ‘Gluten’ is a classification, not a single compound.
The gluten is found in the endosperm of the cereal grain, so it exists in both white and whole wheat bread. It could be removed for the most part via processing with either fatty acid bases or saline solutions (since it’s mostly fat soluble), but cold water is the cheapest method and most widely used (which doesn’t affect gluten levels much). [x]
It’s found in wheat, barley, rye, and malt grains. Oats are essentially gluten free, but have another allergen in them (more on that later). Oats, in stead of gluten, have Avenin. Avenin serves the same mechanical functions as gluten, but does not seem to be an intestinal dilemma like glutens (except in sensitive individuals). [x]
Rice seems to have minimal gluten content. [x]
Shit’s evil bro
In regards to how gluten acts, it seems to do this via it’s prolamin subunit (most common and the one of concern is gliadin).Gliadin is a lectin. If we recall the definition of a lectin, it is a protein compound with a high affinity for specific sugar moieties, meaning it is looking for a sugar ‘marker’ to bind on to. The sugar that gliadin responds best to is called ‘N-Acetylglucosamine’.
Gliadin specifically has 12 binding sites of which can adhere to N-Acetylglucosamine and other sugars, so it is not a 1:1 ratio of damage. This is the main reason some experts hypothesize that lectins can cause agglutination in the body (via using multiple binding sites to attract multiple cells and cause cellular ‘clumping’)
(I should note that this section uses the biochemicular definition of sugar, so it expands beyond the dietary definition of sugar which only includes, in a practical sense, sucrose/glucose/fructose/maltose/lactose/galactose)
The most common methods of gliadin general fuck-uppery in the human body are:
- An enzyme in the gut called tissue Transglutaminase has this sugar marker. This enzyme exists to bind some amino acids to others and start building resistant tissue for the body (such as collagen or mucosal wall lining), this enzyme and gliadin react together because of the sugar marker on the outside of the enzyme. The two form a complex which no longer allows the enzyme to act as it normally does, and this complex creates an auto-immune reactions. [x] (Unfamiliar compound in the body of large enough size means that the bodies immune system will try to fight it).
- Some mucosal cells of the small intestine also have sugar markers on them, of which gliadin can adhere to and cause mechanical damage.
- After sufficient damage is done to the gut wall, these complexes (that were once too big to leave the gut) can get into systemic circulation. Gliadin is pro-inflammatory and it’s presence in systemic circulation has been hypothesized to be the reason behind grain-sensitive arthritis as the sugar marker, N-Acetylglucosamine, is highly active and prominent around chondrocytes (connective tissue cells) [x] [x]
The act of forming a complex, initiating an auto-immune response, and then breaking through the intestinal wall are the three reasons Gluten (via it’s gliadin content) is an irritant to those with sensitive guts. What is important to note is that although salient symptoms are seen in sensitive individuals (Irritable Bowel Syndrome, Coeliac Disease), the mechanisms by which gliadin acts do not require these disease states to work. They act in asymptomatic individuals, and this has recently been noted as well in academia. [x] It has not been established to be a concern in healthy individuals, but the mechanisms are theoretically possible (so take that for what its worth).
What if I want grains, but not lectins, and don’t want to process my own foods?
There is one method of preventing gliadin and other potential harmful lectins from acting. Competitive Inhibition.
Keep in mind that the roles of lectins are ‘to bind to their highly specific sugar substrates/moieties, in most scenarios cells or nutrients are tagged with certain sugars such as mannose/glucose, N-acetylglucosamine, or N-acetylgalactosamine to name a few. We already discussed how gliadin acts on mostly N-acetylglucosamine earlier.
(The tagging of cells with sugars is an important function in the body, as it is one of the methods cells communicate with each other via intrinsically produced lectins and other signaling molecules that confer no significant harm)
It will bind to it’s sugar moiety, but if there are two compounds which have the same sugar on it; lectins will bind to the one which is more electronegatively favorable (gives less resistance). Generally this is smaller compounds, although some proteins are made for each other and have high affinity.
In theory, co-ingesting a compound with a higher affinity for the lectins than the enzyme tissue Transglutinimase or the intestinal cells should competitively inhibit the lectin from adversely acting on those cells and subsequently getting into systemic circulation. This has been seen in patients with Coeliac disease; note the line [x]
In all cases, lectin binding was specifically inhibited by the lectins’ competitive saccharides
Gliadin’s binding sites seem to be highly specific to the sugars ‘N-Acetylglucosamine’, as well as ‘Mannose’ [x]
This was also noted in another study in which N-Acetylglucosamine, mannose, and triacetylchitotriose directly inhibited the activity of gliadin on intestinal cells; it was also able to reverse already presently-bound complexes, which indicate a much higher affinity for these substrates than the cells. Sadly it’s an in vitro study though (Vitro studies are done in the lab, Vivo studies done in people). This reversing effect has been replicated as well in rats, so it’s not wholly an in vitro theory [x] [x]
Of course, there are many studies on the macro effects of N-Acetylglucosamine in human in the following section; so despite those two studies on the actual actions, this is not a wholly in vitro/rats situation.
N-Acetylglucosamine Supplementation for…Gut health?
An acetylated version of the most popular joint health supplement (glucosamine), N-Acetylglucosamine is a relatively small molecule with a very high affinity for gliadin. If they coexist, they will bind; if another molecule comes along with an even higher affinity for the lectin, who cares? The intestinal cells and enzymes are still fine.
Recall earlier that we stated that gliadin has 12 N-Acetylglucosamine binding sites, so we need 12 N-Acetylglucosamine molecules to prevent gliadin from acting on intestinal cells via competitive inhibition.
This study found that the gliadin content of foods varied significantly, ranging from 1.2-3.3% of dry matter. Dry matter is the weight after the water content has been factored out. Gliadin content is highest in durum and wheat grains, with a much lesser amount in barley and oats. According to the study, there was minimal detection of prolamins in rice. The molecular mass of gliadin also varies considerably, which is mentioned because of the following calculations. [x] [x] [x]
As for the actual math, I learned that it goes over most readers heads; I’ll give the summary only. Assuming 50g of wheat bread is ingested, you only need 1g of N-Acetylglucosamine to competitively inhibit all the gliadin content.
All calculations were done assuming wheat products with the highest gliadin content noted, so the N-Acetylglucosamine dose covers that and anything below it. The dose should protect against any foods containing N-Acetylglucosamine binding lectins, at any normally consumed human dose. (The calculations were done with 50g, but there is still a plethora of N-Acetylglucosamine left over after a 50g wheat load is neutralized).
So, knowing this we can safely say that the preventative dose of N-Acetylglucosamine is fairly low. Low enough that, after a 1g dose is administered, the N-Acetylglucosamine left over is not significant enough to cause an pancreatic cell damage that everybody has been concerned with lately. (Abstract is here, the dose is many folds higher than a single gram that is mostly used in in the intestines). N-Acetylglucosamine can interchangeably convert into glucosamine in the body after being taken up by the gut (in regards to the above study), but intestinal uptake of N-Acetylglucosamine is relatively poor, so that’s another detraction away from possible harm from this supplement.
And here’s a great thing to add. The main lectin found in legumes, phytohaemagglutinin (PHA), also preferentially binds to Mannose and N-Acetylglucosamine sugars, similar to Gliadin. N-Acetylglucosamine supplementation should also work with legumes. Although more PHA exists in 50g of legumes (especially kidney beans) when compared to 50g of wheat’s gliadin content, there are less binding sites. 1g of N-Acetylglucosamine should also work in this scenario, regardless of legume dose.
Research makes the above molecule very sexy
(Closing note: I have mentioned Mannose many times, and it should theoretically work as well. N-Acetylglucosamine is just more popular, easy bought, and has been used in the past over mannose in regards to intestinal lectin binding; hence my choice of NAG over Mannose)
But I want grains and legumes, and don’t want to make my own grains with saline, and don’t want to buy NAG, and don’t want lectins in my gut.
I added this section in since I know people will ask.
There was a study that I linked above that showed symptoms in healthy individuals, cited again here. [x]
From this, we have suspicion that gliadin does act in healthy people. It’s a relatively new field of study, so we do not know how much damage these lectins could possibly induce. All we are left is that there are visible markers of said lectins acting in healthy people.
Judging from this, use NAG if you want to eat lectin containing foods without worry. If you don’t want to buy NAG, either avoid lectin containing foods or make the conscious decision to accept the these specific lectin’s negative actions on your body.
We know gliadin/phytohaemagglutinin have bad actions, and we know these actions affect healthy people. We do not know whether these bad actions will make a significant digestive difference in healthy people over a long period of time. Anecdotes say yes; Science hasn’t formulated a conclusion yet.
Meaning, they are bad, but we do not know if they are bad enough that the body can not fight back against them and repair itself; thus avoid damage over time (low-grade toxins sometimes do not affect the body over long periods of time, due to the body repairing the damage to meet or exceed the induced damage; a concept known as Hormesis)
You can try to consume a ton of berries alongside lectin containing foods (as berries have a higher mannose content than most foods), but there is no evidence to suggest this would work; just conjecture.
Also, you can just buy gluten free breads for a higher price.
(Other potentially toxic compounds will be discussed in a future article or article series, dependent on amount of toxins to cover. Compounds such as Avena Sativa, Coumarin, Acrylamides, Solanine, Jacalin, Peanut agglutinin and Concavalin A; amongst others. there’s a lot of them)
(Credit to http://motherblissmunchies.blogspot.com/ for the first bread picture)