Loren Cordain, Colorado State University Professor and author of The Paleo Diet has a new book: The Paleo Answer. 7 Days to Lose Weight, Feel Great, and Stay Young.
Here is an interview with Loren from 2010, where he explains the biochemistry of why autoimmune diseases such as MS, arthritis and Type 1 diabetes might be made worse by grains, beans, dairy, and in some people, egg whites and tomatoes. In addition to the audio interview, this now includes a written transcript of the interview. Thanks to Sandy Grabowski for transcribing.
We started off with rheumatoid arthritis, that was our original model, and we’ve parlayed into a more universal understanding of all autoimmune disease. So with multiple sclerosis, we chose that because there is epidemiologic evidence that implicates diet in multiple sclerosis. We think that in order for the immune system to lose the ability to recognize self and non-self, which is what autoimmune disease is, there has to be peripheral antigenic stimulation, meaning that there has to be antigens or proteins that come in constant contact with the immune system that we believe enter into the immune system from the gut.
The gut normally is impervious to proteins. We normally break proteins down in our gut to the constituent amino acids. The proteins are broken into peptide fragments, and peptides are broken into amino acid sequences. So normally what we end up with are amino acid fragments that we absorb, and what we think is going on is, we think that these larger peptide fragments, as well as amino acid sequences that may be 10 to 15 bases long, can also get in. We think that this content leaking of antigenic peptides and proteins from the gut into circulation primes the immune system to do nasty things in certain generally predisposed individuals. Normally these large-size peptides and proteins simply would not be able to get through, so we’ve hypothesized that there’s one of three potential mechanisms whereby they can get through.
Two of the mechanisms aren’t unique to our group. Other people have suggested the same thing. One is what’s called the paracellular pathway, which is whereby these peptide fragments are leaking through the cell-to-cell connections. The gut cells are called enterocytes. These are called tight junctions. So the dimensions of the tight junctions actually increase, allowing for a larger molecule to get through.
And that happens when there’s more inflammation?
That’s right. Tight junctions loosen up with inflammation, when the gut is chronically inflamed. People who have rheumatoid arthritis tend to have inflammations of the joints occur at the same time the gut occurs. We don’t believe that this is serendipitous. In nature we believe that inflammation of the gut is associated with inflammation of other tissue.
The second mechanism is the transcellular pathway, where these elements are going through the cell itself. We think that this pathway with active transport is probably the way that it is happening. We believe that there are receptors in the gut that are acting as Trojan horses that are allowing these molecules to get through.
And this is the human epidermal growth factor receptor?
That’s right. This is an unusual receptor, because the way the body works its that when we secret hormones, hormones bind to receptors at cells, and that causes the cell to express genes and make proteins and do all kinds of things. So the crazy thing about the gut is, the inside of the gut that’s exposed to the food and so forth, is actually the outside of your body. So the question comes up, why, from an evolutionary perspective, would we ever find a receptor that is facing luminally or towards the outside? It faces the lumina of the gut, which is the outside of the body. In theory, there shouldn’t be any hormones there for it to bind to.
Turns out that in our saliva, we have the key to the lock. The receptor could be envisioned as a lock. The receptor itself is bound in what we call the glycocalyx of the gut. The glycocalyx is kind of this wavy series of carbohydrate molecules that prevent anything from binding this receptor. What happens is, when the gut becomes damaged, either through mechanical damage or through GI tract irritation or whatever, that information causes the glycocalyx to be shed and it allows the receptor to bind its normal ligand. The ligand is the word for a key. A ligand is like a key, a receptor is a lock. So it allows the key to bind the receptor, and the body’s endogenous key is epidermal growth factor. That’s found in our own saliva. So when we swallow our own saliva, if the receptor has been exposed at the glycocalyx, then the hormone, epidermal growth factor, the key, can bind it’s receptor, epidermal growth factor receptor, and when it does that, it causes tissues to be healed inside the gut.
So if you’ve ever noticed a dog licking wound, there’s method to the madness. When you lick an open wound, the hormone, epidermal growth factor, in the saliva promotes healing. We know that from animal studies in which we’ve prevented animals from licking their wounds, or we’ve taken their own saliva and swabbed it onto the open wound. It heals faster when saliva is there. So we believe that’s what’s going on in the gut, that the epidermal growth factor receptor is there on an evolutionary basis to help us heal our own wounds.
The luminal side of the intestine doesn’t have a whole lot of receptors that we know about. We know the epidermal growth factor receptor. There’s another receptor in the lower gut called the Thompson-Fridenright [?] receptor. But there’s very few receptors per se in the gut. And the way the gut actually makes the immune system aware of the contents of the gut, because the immune system needs to know that, is through what we call M cells. These are specialized cells that line Peyer’s patches in the gut, bumps that are found in certain parts of the gut, and within those Peyer’s patches are M cells. Their function is to sample tiny amounts of the bacteria and the pathogens and everything that’s in the gut so we can tell the immune system what’s going on.
But the M cells we don’t believe are exploited by dietary antigens and most of the bacterial gut pathogens.
They’re too little.
Right. They’re tightly controlled, too. The way that T and B cells operate in conjunction with these M cells is, the T and the M cells don’t allow much antigenic material to bypass the gut, or what we have is, we have another part of our immune system called the gamma globulins, and the gamma globulins form complexes that prevent any of these proteins from doing any damage to our system. So at least in theory, the M cells, combined with the gamma globulin system, prevent any of this from going on.
So our hypothesis is, the gut becomes damaged by certain dietary elements, which strips the glycocalyx, which exposes the epidermal growth factor receptor, which allows these certain dietary elements, along with these viral and bacteria peptides, to get into the bloodstream. The epidermal growth factor receptor is what we call a very promiscuous receptor. Most receptors have one or two endogenous ligands, but the way this thing work is what’s called a dimer. This dimer of a receptor has 10 or 12 endogenous ligands that it binds. So it binds this whole series of things, and it has to do with the structure of the receptor. Because it binds so many endogenous ligands, it has the potential for binding everything, and that’s the problem, that it has the potential to bind lots and lots of factors that at least in the Western diet are very, very common.
So one problem is that the foods that you’re implicating have an easy way, they tend to damage the glycocalyx. They tend to get at it through cooking. Stomach acids don’t break them down enough. When they get into the gut, they’re irritating.
That’s right. And what we’re talking about is dietary lectins. For instance, when you eat whole wheat, you eat a lectin called wheat germ agglutinin, WGA. We know that WGA, when it gets into the gut, causes the glycocalyx to be stripped, which opens the door to bind the epidermal growth factor. We know that WGA indeed binds the epidermal growth factor. How we know this is, there are animal models where we take insulin and we bind insulin to WGA, so we have a complex. We have an insulin WGA molecule, and what happens is, WGA, because it has an affinity for the epidermal growth factor receptor, binds that receptor, and in rats, it lowers the blood glucose. Normally you can’t get insulin into your system because it’s a large molecule. That’s why we have to inject ourselves with insulin. So when you bind it to WGA, you can actually lower blood glucose. But the problem is, WGA is like superglue. It doesn’t just bind the receptor and go on its merry way? Anything and everything that’s in the gut it will bind.
So it has a high affinity for bacterial cell wall proteins, and there’s a bacterial cell wall protein called LPS, lipopolysaccharide. We know that WGA binds lipopolysaccharide. In the gut, bacteria are just like proteins. They get busted up, too. So when you eat meat, that gets broken down into its peptides and amino acid components in the same way as the bacteria. So bacterial cell wall gets broken down, and if you have WGA in the gut, it binds these bacterial cell wall proteins, and it then binds the epidermal growth factor receptor, acting like a Trojan horse, and bringing WGA plus this antigenic bacterial molecule into plasma.
I’m picturing it like a sticky lollypop stick, and what it grabs to be the top of the lollypop is unfortunately quite often a bacteria.
That’s right. So even if these bacterial peptides were to get past the gut, and even if they were to get into cells, cells have an enzyme called lysozyme. Lysozyme specifically acts on bacterial cell proteins to break them down. So even if you do get bacteria in your bloodstream, the lysozyme in the cells breaks it down and there’s not a problem. However, WGA is resistant to this enzyme lysozyme, so WGA, when it’s bound to the bacterial peptide, it’s like putting a Superman invulnerable shield around itself. The peptide remains intact, and then it can be transported to any other cell in the body that expresses the epidermal growth factor.
And as it gets transported, it also carries along whatever it stuck to it?
That’s right, it gets carried along whatever is stuck to it, and this is the universal mechanism. We started off using rheumatoid arthritis as the model. We now believe that this probably is a universal mechanism that acts in many types of autoimmune disease. If you don’t have a specific genetic makeup, this process won’t work.
Or at least the risk of it is significantly lower?
Is significantly, significantly lower. You have to have what we call an HLA haplotype. This is the human leucocyte antigen haplotype.
You don’t have to have that, it just increases your chances?
Right, it increases the probability. And we haven’t completely ironed all this out. When I say “we,” science in general. We believe there are multiple HLA haplotypes that can combine with multiple dietary lectins, which can combine with multiple gut antigens to express a disease.
What you’re describing is, some people happen to have the kind of DNA that looks more like these Trojan horses than other people? So the immune system is more likely to get confused?
All DNA does is code for a protein. And one of the proteins that it codes for is the HLA protein. And what an HLA molecule is, it’s just simply a little molecule that spans the cell membrane and it presents proteins from within the cell to circulating white blood cells, or T lymphocytes. When the circulating T lymphocytes see a molecule that’s foreign to the body’s own self, it mounts an attack on not just the molecule that it sees here, but any other place in the body where it encounters that foreign molecule, it will mount an attack. That’s how we get rid of infections. That’s how our body recognizes foreign material. What we believe is, through a process of three-way molecular mimicry, the T lymphocytes become confused. And how they become confused is through a process that we call monster molecules, these chimeric molecules, which you’ve called the lectins attached to the bacterial cell walls. We call those chimeric or monster molecules, and when they come in, they look a lot like the bacteria, but they also look a little bit like the tissue that’s being attacked.
The T lymphocytes lose the ability to recognize themselves in a foreign bacteria because the confirmation of what it sees is so similar to a foreign molecule and itself. It’s like you have somebody speaking English and somebody speaking Chinese and you have somebody in the middle that’s doing the translation. And the guy in the middle is the HLA molecule. What the HLA molecule does is, it sees that chimeric molecule that’s digested, and the HLA molecule then presents this monster molecule at its cell surface. The shape of the HLA molecule is determined by our genes. Everybody has a slightly different HLA makeup. That’s why we believe that people have a genetic susceptibility for autoimmune disease, because for those people that see this little monster molecule, it’s slightly changed by our middleman, our translator. So the HLA molecule slightly changes the confirmation this monster molecule, and when it does that, it totally confuses the immune system, and the immune system loses the ability to recognize self and non-self. That’s the underlying concept.
This sounds like Homeland Security going after terrorists.
[laughs] Well, I don’t know if that’s an apt analogy, but the immune system is the most complex part of our genetic makeup. The HLA system is what’s called a polymorphic molecule, and there’s more than 3,000 different versions of this. It’s a very, very complex system. It’s designed that way. A more apt analogy is cops and radar systems. Cops are trying to catch speeders, and the companies that build radar detectors build a better radar detector, they build a better radar gun, and there’s this one-ups-manship. The same thing has happened over the course of hundreds of millions of years with the immune system. We have this one-ups-manship, and that’s why the system is so polymorphic. There are so many multiple versions of this thing along the way.
You’ve described WGA as bad, bad, bad every step of the way. Cooking it doesn’t stop it. Stomach acids don’t stop it.
Lysozymes within cells don’t stop it.
It gets through the gut barrier and lysozymes don’t stop it. Not only that, but it’s an adjuvant. What is an adjuvant?
When we were first trying to make vaccines to prevent diseases, like the polio vaccine that Jonas Salk won the Nobel Prize for back in the ’40s or ’50, they tried to simply get the virus and make a weakened version of the virus, dry it out, whatever, inject it into the body’s system. What they wanted to do was to build an immune response so that the T cells and the B cells and the rest of the system would mount an attack on this weakened version of the polio virus. But the problem is, the immune system was smart, and the immune system says—it’s like going fishing. “I’m not going to go for that, because it just doesn’t look like a problem.” So what they have to do it, they have to tack on what’s called an adjuvant molecule. When the adjuvant molecule is tacked onto the weakened virus or bacteria, that adjuvant serves like red pepper. It totally inflames the immune system, and now the immune system will make an immunologic response to that antigen.
So WGA by itself, as do other dietary lectins, act as adjuvants. We believe then that this adjuvant response promotes autoimmunity in certain individuals.
So the WGA on its own increases inflammation and irritation inside the body, but when it’s stuck to something like a bacteria that happens to look like one of the body’s cellular components, it makes the immune system more likely to be fiercely attacking that kind of bacteria and also human cells that remind it of them?
We don’t have in vivo data because this is such a new concept, meaning that in humans, does this actually happen within their body? The best evidence that we have is what’s called in vitro data. What we take are little Petri dishes and we put in white blood cells, and then we also put in WGA. If we put WGA into a Petri dish with white blood cells, the white blood cells, which are called macrophages, elicit an inflammatory response. The inflammatory response occurs because they secrete localized hormones called cytokines. These are inflammatory cytokines. We know then if you put WGA into a Petri dish with white blood cells, the inflammatory response is even greater than if you would put bacterial cell walls, this LPS protein I talked about. It’s 30% to 40% greater than what would occur with a bacteria.
That’s a good response. When a bacteria gets into your system, you want an inflammatory response to get rid of it. When a dietary antigen gets into your system, it’s causing a low level of inflammation, and that’s not a good thing, to have chronic low-level inflammation.
Some fans of Sally Fallon and Weston Price asked me to ask you what about fermenting grains? Does that flatten out the WGA lectins enough that they don’t cause a problem?
What we do know about fermentation is that the bacteria that are responsible for fermenting dairy foods and other foods, beans and so forth—
And how about wheat?
—and even wheat, they reduce another antinutrient called phytate or phytic acid. The phytic acid content is reduced with fermentation. In WGA, fermentation has little or no affect upon the appearance of lectins. As a matter of fact, if you take dry kidney beans and boil them for two or three hours, there’s still physiologically significant lectins after boiling for two or three hours. The only way that you can remove lectins, because of their molecular confirmation, they are such sturdy molecules the way they’re built, that they’re resistant to not only proteases that are found in these bacteria that cause fermentation, they are resistant to heat. The only way you can get rid of them is to pressure cook them. If you pressure cook them for an hour or so, then you will degrade all the WGA. But frequently we eat our legumes and beans from the dried form, we just soak them and boil them, and they are still significant sources of WGA.
If you buy canned legumes, part of the process of preventing horrible bacterial contamination is to pressure cook them, so most canned foods are pressure cooked, and if you’re eating beans you don’t have to worry about it if they are canned, typically.
Bread is cooked at a very high temperature.
Not even close. The WGA that’s found in cooked bread or even roasted peanuts is the same concentration as what you find in raw, uncooked.
And sourdough bread, the bread that was traditionally done in Switzerland where they left it out for a week before they cooked it so it fermented a great deal, that doesn’t affect lectins?
The information that we have is that the fermentation process does not significantly reduce the lectin content of bread. What does do it is that the WGA that we find in bread is primarily found in the germ and the bran. So if you look at the concentration of WGA in whole wheat, it is significantly higher than what it is in white bread. So white bread, even though it’s not necessarily a good food because of the high glycemic load, has a lower lectin content.
So white sourdough French bread might be OK for some people?
The concentration of WGA in white flour is about 3 to 4 milligrams per 100 grams, whereas in whole wheat it’s 10 times that, it’s an order of magnitude higher. But at physiologic levels, we’re only talking nanogram concentrations in bloodstreams. We know from tissue studies, these in vitro studies, that cells respond at nanogram concentrations, so nanogram concentrations can easily be achieved by consuming 4 to 7 milligrams per 100 grams.
It sounds like if somebody actually has a sensitivity or a vulnerability to this WGA, it may be an all-or-nothing food for them.
If you have celiac disease, we know that gliadin proteins have been complicated in celiac disease. How they specifically get through the gut is not completely clear, but those individuals can’t have any wheat.
For some people with autoimmune diseases, your guess is that it might be the same thing?
That’s right. In animal models, we can induce type 1 diabetes by simply feeding wheat.
And not very much wheat?
You have to go back and look at the literature. In the animal models where it’s been done, it’s been done at typically higher values in which ___ wheat comprises 20% to 30% or more for the energy.
But once somebody’s sensitized, once their immune system is hypervigilant for this protein, it may not take very much.
Right, memory cells become attuned or agitated to these peptides, so it doesn’t take much.
You have also been looking at other foods besides wheat that you say, “Watch out for these if you have an autoimmune disease.” What’s on the list?
Legumes, like kidney beans, contain a lectin called phytohemagglutinin, PHA. We think that people should definitely stay away from legumes. Soybeans as well contains a lectin SBA. Animal models tell us that these legume lectins get across the gut very easily, just like wheat germ agglutinin. We currently have conducted an experiment here at CSU where we fed wheat germ agglutinin into humans as well as peanut agglutinin to humans, and we’re in the process of measuring blood concentrations of these lectins to see if it gets through. We’re working with a group in Austria, Franz Gabor [?], and we’re working with a group at the University of California at Davis in their plant physiology laboratory that are measuring the lectin concentrations in the human plasma. So we hope to have this information shortly, and this will represent the first human studies to show that these lectins get through.
And that’s the very first step, to show definitively that in healthy, normal people without gut disease, which is what our subjects were, that with the consumption of these foods, we see lectin appear in the bloodstream. And after that, then hopefully in the ensuing years we’ll be able to measure this inflammatory response that we see in vitro, in tissue models, we want to do it in vivo, to show that if we give people a big dose of lectin from kidney beans or wheat germ, that it causes an in vivo inflammatory response, and then the next step is to do what are called Elisas , a kind of an immune-type way of looking at these complexes, so we can identify these molecules to see if they are actually getting in the bloodstream as well.
How about dairy?
Dairy goes back to this whole notion of this receptor that is willing to bind just about anything. This gut receptor, the epidermal growth factor receptor. The problem with dairy is that dairy doesn’t contain lectins per se, so you would think that if this is how lectins are dragging these gut molecules through, dairy shouldn’t be a problem. But dairy contains something else, the body’s own endogenous ligand for the epidermal growth factor.
That means it sticks to things?
A ligand is a key, a receptor is a lock. The ligand binds the receptor, it’s like binding a lock, and opens the door. We think about milk as being a perfectly harmless white substance that’s got a lot of calcium and a lot of healthy nutrients for us. But it also contains a profile of many of the hormones that circulate in a cow’s blood, because milk is essentially filtered blood. Most of the hormones that are in a cow’s blood are also found in a cow’s milk. Most of the hormones have very, very rapid half-lives, like any other hormones, so by the time the cow’s milk is pasteurized and process, three days later it appeared on the grocery shelf, most of the hormones are degraded.
However, there’s an exception to this, and there’s a very, very stubborn hormone called betacellulin, which is the body’s own endogenous ligand for the receptor. Remember we said that the epidermal growth factor receptor is very promiscuous. It has 10 different ligands. One of the most powerful ligands for the receptor is betacellulin. It causes downstream signaling greater than epidermal growth factor itself. So when you drink cow’s milk, even pasteurized, processed cow’s milk, even cheese, that goes through this entire process of degrading and everything else, cheese contains betacellulin. Three months later there’s very high concentrations of betacellulin in cheese. So when you drink milk, whether it’s been pasteurized, processed, whether it’s goat’s milk, cow’s milk or anything, you’re get a big shot of betacellulin, which then has the capacity to bind the epidermal growth factor receptor. And betacellulin also binds the casein fractions of milk. Not only does betacellulin get in, these other peptide fragments that are found in the casein fragment, the whey side of milk, they also get through as well.
It sticks to these big monster milk proteins and brings them through?
That’s right. And then if you throw WGA into the mix, you can get even potentially more of these monster molecules.
If somebody eats yogurt that’s been drained of the whey, does that get rid of all this nasty stuff in milk?
At least in theory. One of my colleagues, Pedro Bastos from Portugal, is the man to talk to about that, but apparently there are different ways in which the whey is separated from the rest of the milk proteins. The separation process has to do with whether or not betacellulin ends up in there. I don’t know that we have any experiments to date that show what the betacellulin content is of these various separation processes.
That might be another one where if somebody has an autoimmune disease, maybe no dairy products, not even strained yogurt?
That’s kind of the approach we would take. It’s a lot like elimination diet. These are the most likely candidates that cause this three-way molecular mimicry and peripheral antigenic stimulation in the gut. Our idea is that people with autoimmune disease, there’s a variety of foods that they ought to eliminate initially and then carefully monitor their symptoms. With a disease like multiple sclerosis, basically there’s different versions of it, but the most common version is relapsing and remitting, where people have these symptoms that come on and go off, come on and go off. At least to date, it seems somewhere serendipitous how it happens, although there’s an association once again with inflammation. So when they get viral diseases or bacterial diseases, they seem to have a flare-up of their symptoms. So we believe that these dietary antigens also potentially can cause flare-ups in relapsing and remitting MS patients.
Let’s go through the whole list of foods. Tomatoes. You don’t like tomatoes either for people with an autoimmune disease. Why not?
Of the two known lectins that have been shown in human plasma, the first is peanuts. That was show in 1998 by the ___ group in English. So we know that peanut lectin gets into plasma. We’re replicated that study as we speak. The second lectin that we know gets into human plasma is tomato lectin. Tomato lectin in 1972 was shown, when they labeled tomato juice with a radioactive isotopic tracer, a person drank tomato juice, and a half hour later the isotope was in their bloodstream. So we know that tomato lectin also gets through.
But the thing about tomato lectin is that if you put it in these little Petri dishes with white blood cells, it doesn’t cause an inflammatory response. WGA and PHA cause inflammatory response. Tomato lectin doesn’t. We know from epidemiologic studies that people who eat tomatoes have reduced incidents of cancer and heart disease and so forth. So on paper it looks like tomato ought to be a very, very healthy lectin. But once again, tomato lectin doesn’t just nicely bind the receptor, shut the door, and go in. Anything that’s in the gut, just like WGA, can be drug through with tomato lectin.
It’s sticky, that’s right. And so we believe that if tomato lectin binds specific antigens in the gut, then those antigens can gain access. And once again, we have this monster molecule formed by tomatoes. We don’t have any direct evidence that any of these things cause autoimmune disease. We have circumstantial evidence. What we do have is a dietary trial going on right now in Ireland where people are going on diets that are wheat-, grain-, dairy-free. They’re not tomato- or egg white-free yet, because we’ve just identified those. And they are having amelioration of symptoms. This has not been published, and this is anecdotal at this point. We don’t believe that this is a cure-all for everybody, but we think that in certain people, dependent upon how long they’ve had the disease, they can improve the symptoms. The longer they’ve had the disease, they may stabilize, but the less likely it is they will ever regain function. If they have had the disease for a short period, within one to three years, there’s a good chance that they can go into complete remission, not all people, but some people, and many people can have an improvement of symptoms.
So we’re not trying to provide false hope in that we have a panacea for all MS patients. When we’re saying is that we have a potential mechanism where a percentage of people can improve.
You went by egg whites pretty fast. What’s wrong with egg whites?
We talked about lysozyme. In the body’s own cells, it has these very, very powerful enzymes that bind bacteria and destroy them. For instance, if you look at your conjunctiva, if you look at the tissues that line your eye, the eye is constantly exposed to bacteria in the air, so we’ve got this open, as it were, reservoir that can potentially get infected every day of your life. But what happens is that the tears in your eye contain a very, very high concentration of lysozyme. Lysozyme busts up these gram-positive bacteria, as well as gram-negative bacteria, and it destroys them. The bacteria don’t have any way to counter lysozyme. Lysozyme is something we build ourselves, and it shouldn’t be problematic, because we’ve got it in every cell of our body.
But what happens with egg white is, egg white contains very, very high concentrations of lysozyme, and guess what lysozyme binds? It binds our promiscuous epidermal growth factor receptor. Now remember, what lysozyme does is attack bacterial cell walls. When we put high concentrations of lysozyme in our gut, it busts up these bacteria. When it busts them up, it forms these fragments of lysozyme, because lysozyme is resistant to the gut’s proteases, it forms these complexes of lysozyme plus bacteria. Because lysozyme can bind the epidermal growth factor receptor, then lysozyme, just like tomato lectin, even though in vivo it doesn’t do anything by itself, when it’s drawn through the gut, it can potentially cause an immune reaction.
Let me get this straight. So lysozyme doesn’t stick to things, it just busts them up?
That’s a good point. A lectin agglutinates—the older definition of a lectin is that it agglutinates red blood cells. So lysozyme does not agglutinate human red blood cells. But lysozyme does stick to bacteria. When it sticks to bacteria, it forms a complex, the lysozyme can bind that receptor, and then it can drag this stuff through.
Another monster molecule?
Potentially a monster molecule. Having spoken with multiple sclerosis patients who have come into remission on a wheat- and a dairy-free-type diet, a couple of them have told me that egg whites exacerbate their symptoms. I said eggs, not egg whites. But that kind of was the stimulus for this thought. And having gone through the biochemistry of lysozyme to see how it actually works, lysozyme in theory has the potential to act like a lectin and get into circulation.
Now, none of this has been shown in humans as of yet, except for the tomato and the peanut agglutinin. We are replicating those studies as we speak.
And you’re also showing in the laboratory the mechanisms for why you think these things might be a problem?
That’s right. Well, we haven’t gotten to the laboratory stage yet. We’re still at the theoretical stage, because the epidemiology studies point towards that. If you look at the epidemiology of milk-drinking and multiple sclerosis, for the last 30 or 40 years we know that there’s a very good epidemiologic association. You drink more milk, it increases the risk of multiple sclerosis.
And go ahead and add some of the other autoimmune diseases that you increase the risk for if you drink milk.
Type 1 diabetes. With type 1 diabetes, we not only have epi studies, we also have animal studies, just like those little rats where we fed them increased wheat diets and they had and increased incidence of type 1 diabetes, the same thing is true. My colleague Frazier Scott in Canada has shown that if you feed them more milk, they also have an increased incidence of type 1 diabetes.
Do you sometimes think that if you look closely enough at any food, you would find some nasty lectin or lysozyme or something that would bind with the epidermal growth factor receptor hormone and cause a monster molecule to get through? Is all food suspect?
Absolutely not. And the reason for it is because we need to look at the foods that were traditionally in the human diet. Milk was not ever traditionally in the human diet. Milk is a very recent newcomer. Milk has only been around for 6,000, and if a human generation is 30 years, we’re looking at a very, very small time for milk to be in the human diet. The same way with wheat and whole grains. Even though we call them the staff of life and the staple of all civilizations, on an evolutionary time scale, they’ve only recently been domesticated and adopted. The same thing with legumes. They were never traditionally a staple in the human diet.
And I suppose eggs were only a seasonal food.
That’s right. Eggs were a seasonal food, as were all plant foods. So even if you had the susceptibility haplotype and you started to get the disease, then the exposure was very, very short, whereas in the modern world, we eat grains and legumes and dairy products almost every single day. So we are exposing ourselves on a daily basis. We believe, then, that these are diseases of civilization, these autoimmune diseases, had they been present two and a half million years ago, natural selection would have weeded them out by now, and that’s why they haven’t been weeded out, because they have such short exposure to the human genome. The human genome would normally, through negative selection, get rid of these things, because they’re killing us at a younger and younger age. Multiple sclerosis attacks young women in their prime reproductive years. Had that been going on for hundreds of thousands or millions of years, we would no longer have multiple sclerosis, or we would have it at a very, very low percentage of the population.
You also implicate a deficiency in vitamin D.
Animal studies, human studies, epidemiologic studies also point to the role of vitamin D. And vitamin D really isn’t a vitamin, it’s a hormone, because it acts in every cell of the body. We also believe that it’s a potent hormone that influences hormone function. And once again, from animal models, there’s an animal model of a multiple sclerosis EAE that can be prevented simply by dosing the animals on high levels of vitamin D before implication of the disease.
Here in Colorado we don’t get much sunshine compared to the tropics.
Here in Fort Collins, we get more days of sunshine than they do in San Diego, but what’s important is the height of the sun relative to the latitude, because in the tropics, you get direct sunlight, and the direct exposure of UV causes a greater synthesis of vitamin D. So in terms of the blood concentrations of vitamin D, we are significantly lower here in Colorado than we would be in the tropics.
The foods that you’re choosing to say are problems are ones that have been traditionally chosen also by naturopathic physicians, by acupuncturists, by people who study those alternative fields. Does that make sense to you?
I think that people that are in the trenches, making careful observations with naturopaths and some of these others, they see hundreds if not thousands or tens of thousands of patients, and they have at least anecdotal evidence from their experience that there’s something going on. But in support of these folks are part of the medical community that are concerned with allergies, particularly food allergies. If you look at the scientific peer review journals in the allergy field, the same picture is painted: milk, wheat, corn, dairy, tomatoes, and so forth often are the same foods that are allergenic. And we have in the allergy community IGG responses, which are considered more valid than an IGA response. So we have these IGG complexes to these food allergens.
So I think that if you triangulate it, and you look at the evolutionary perspective, we seem to be focusing in on these same types of foods. These are the foods that have been recently introduced into the human diet. And even though they seem like staples and they seem like everybody eats them and there’s no problems with it, if you look at the incidence of celiac disease, we know now the roughly 1 in 100 people have celiac disease in the U.S. We know that from blood bank studies. So if we go into blood banks and get a huge random sampling of blood, and we measure specific antibodies, we find 1 in 100. That’s three million people in America who shouldn’t be eating wheat. That’s an enormous amount. And I suspect that when we finally do, maybe not in my lifetime, I’m getting to be old here, I would suspect in maybe the next generation that we will see autoimmune disease unlocked. We will find out what the chain of environment events and genetic events is that cause it. This disease has been going on probably for at least 10,000 years, maybe longer. That disease knows exactly how it’s doing it. Humans just haven’t unraveled this complex disease.
Do you get a little bored or frustrated by how much money goes into drug treatments for autoimmune diseases while this other area is somewhat overlooked?
We need novel thought. We need to think outside the box. People, when they look at autoimmune disease or any other disease, they look at an allopathic treatment. Cure the symptoms, don’t cure the cause. And from a fundamental perspective to understand the disease processes, we can perhaps build better drugs, if that’s an option, but perhaps it’s better to use the system the way it was designed genetically, and that’s my bias. If the system is genetically designed to operate under these conditions, maybe that’s what we should be doing if it’s practical rather than continuing to try to operate it under conditions under which the genome wasn’t selective.