Protein Slows Digestion? Nope.

By Jordan Feigenbaum MS, Starting Strength Staff, CSCS, HFS, USAW Club Coach

In response to this gem of an article. I answered this on the Starting Strength nutrition forum, but I thought I’d repost it here. The article’s claims are italicized and my responses are in bold. 

The food that we consume is absorbed and its nutrients are subsequently sent to different organs through the blood.

The food that we consume is absorbed and its nutrients are subsequently sent to different organs through the blood. Not really the case literally. Protein and carbohydrates get absorbed as amino acids and monosaccharides through the small intestine’s brush border> into the enterocyte (cell)> into the portal vein> to the liver first before going anywhere else, then they get distributed based on lots of factors.

Fats get absorbed as fatty acids directly into the enterocyte (cell) and packaged into the chylomicron (with cholesterol, phospholipids, etc.)> into the lymphatic system> into the venous circulation and then go to some tissues, but mainly those who express high levels of mitochondria for beta oxidation or peroxisomes for long chain fatty acid oxidation. Principally, these are the liver and skeletal muscle.

However, a slow or sluggish digestive system isn’t able to perform its assigned function effectively. That is why a person experiencing a bout of slow digestion is bound to feel extremely uncomfortable post lunch or dinner. Nausea, bloating and vomiting are the most common symptoms of sluggish digestive system that occur after having meals.

Notice they do not define a normal GI transit time for a mixed meal, a slow GI transit time for a “bad” meal, nor do they distinguish between a pathologically slow state like gastroparesis or ileus or obstruction and a “slow” transit time occurring due to a specific meal composition. Yes, there is a marked difference.

Constipation or common digestive problems like diarrhea and irritable bowel syndrome can make the digestive system sluggish.

Diarrhea is actually the GI contents moving too fast. IBS has physiological symptoms of a combination of diarrhea, constipation, abdominal pain, and abdominal bloating. Seems like it might not make the digestive system sluggish, right? Though if you’re constipated, sure (and fiber and/or some probiotics tend to improve symptoms by increasing motility and osmotic pressure in the intestine to propel the contents)

Although protein is good for health, excessively high amounts of protein in the diet can slow down the digestive health. This is because, the body has to really work to digest protein.

Not the case at all. Proteins are initially broken down via the acidic pH of the stomach (and further in the small intestine by pancreatic enzymes that are all part of our normal physiology) and are absorbed very rapidly into the portal circulation. Whey, for instance- spikes blood plasma levels of amino acids (digestive end products of protein) within 20 minutes of ingestion.

Mixed meals confound the “speed” component, i.e. what is the fat content (slows gastric emptying), fiber content (soluble slows, insoluble speeds), total kCal content (larger is slower), tonicity of the meal (isotonic empties faster than hypo or hyper tonic from the stomach to the small intestine), etc. In addition, the hormonal milieu at the time with respect to previous meals also influence gastric transit time. Ghrelin, for instance- increases when you’re hungry and increases the motility of the gut.

Don’t forget about existing food in the GI tract. See how this is quite complicated to talk about? Let’s not forget about drugs….

At any rate, Carbohydrate rich and protein rich foods empty at about the same rate, but normal gastric emptying following a meal is 2-6 hrs….so yea- perhaps this whole article is a bit silly, eh?

Unlike simple carbohydrates, proteins are heavy, hence are not easy to digest and so when its presence is alarmingly high in everyday meals, the consequence is a slow digestive system.

Now this is easy to see that this is wrong…

People with intestinal problems such as Crohn’s disease tend to have a sluggish digestive system besides bowel dysfunction (diarrhea or constipation), vomiting and stomach pain. In this condition the lining of the small and large intestine are inflamed. However, in most cases, the swelling infiltrates in the inner layers of the bowel tissue. This chronic inflammatory disease considerably slows down digestion as the food tends to move at a very slow pace through the intestine.

Fuark. Crohn’s is, currently, a dysregulation of inflammation in response to bacteria in the walls of the GI tract, which results in proinflammatory substances causing direct mucosal injury.

Crohn’s usually presents with diarrhea, fatigue, weight loss, and crampy abdominal pain plus oral ulcerations, perianal fissures, perirectal abscesses, and malabsorption BECAUSE THE FOOD CAN’T BE ABSORBED BECAUSE IT’S MOVING at a normal speed but the mucosa can’t absorb it.

A point to note that although food is digested in the stomach, most of the digestion occurs inside the intestine. Experts say that the intestine is the place where nutrients are observed and eventually circulated in the bloodstream to various parts of the body. However if the food stays for longer time in the stomach, this can affect the digestion process. This condition is known as gastroparesis, in which the stomach takes more time to transfer the ingested food to the intestine. This happens because the stomach muscles that are assigned the task of pushing the food to the intestine, lose their ability to work efficiently. Gastroparesis is the result of malfunctioning of the vagus nerve that regulates movement of muscles lining the stomach wall.

Most common KNOWN causes of gastroparesis:

1) diabetes mellitus
2) idiopathic
3) post-surgical (especially if vagus nerve damaged)

Other causes:

-meds
-etoh and tobacco, weed
-surgery
-infection (mono, chagas, rotavirus)
-CNS injury like a tumor or cerebrovascular event
-PNS pathology (parkinson’s or guillan barre)
-other issues (cancers, hypothyroid, lupus, intestine obstruction, portal hypertension, HIV, stroke and migraines)

So…yea, protein is UNLIKELY to be the cause of “slowed” gi emptying….

-thefitcoach

7 Rules to Optimize Protein Intake

By Jordan Feigenbaum MS, CSCS, Starting Strength Staff, USAW CC, HFS

In general, I am not a fan of rules, dogma, or rigid guidelines. That being said, what follows are what I consider to be the most important variables when it comes to optimizing protein intake for anyone. While there are sure to be inter-individual variability, these “rules” are pretty spot on. Without further ado…..

1) You will eat enough protein each meal. Optimal protein intake per meal will be the amount of protein that yields ~3-4g of leucine, a branched-chain amino acid (BCAA). 3-4g of leucine per meal has been shown to maximize muscle protein synthesis. If it’s maximized, it can’t go any higher with additional protein, right? This is also, of course, assuming that the protein you’re consuming either contains all the essential amino acids (like all animal derived proteins do) or you have eaten a protein rich meal within the past 4-6 hours that had all of the EAA’s present in abundant amounts. Just to give an example, whey protein (the KING of all proteins) has ~3g of leucine per 20g serving whereas brown rice protein has 3g of leucine per 40g serving. While these two doses are equivalent in their potential to drive muscle protein synthesis, they are not equivalent in calories, which may be a consideration you wish to make if you’re calorie restricted. (Note: many protein manufacturers have different leucine/serving ratios but this is a fairly accurate estimate based on most protein supplements).
2) You will optimize meal frequency. Somewhere along the line people started espousing the mantra “eat every two hours to stoke the metabolism” or “so you don’t become catabolic”, with catabolism meaning breaking down– in this case skeletal muscle- to use their constituents elsewhere in the body.  Problem with these recommendations with respect to protein intake is that there is a known refractory period to muscle protein synthesis (MPS), which we can think about on a gross level as muscle growth/recovery/building. Every time a large enough dose of protein is ingested, i.e. one that provides enough leucine and EAA’s to push the MPS reaction over the edge, there’s a 3-5 hour refractory period that must transpire before another dose of protein (at a meal/shake/etc) will yield another bout of MPS. This means that if you ate a protein rich breakfast at 8am, then ate again at 10am, the meal at 10 am would contribute nothing to MPS and then, by definition- it would be stored away as energy -either glycogen or fat depending on other variables. Ultimately, we should be waiting longer between protein dosings to optimize our results. MPS is obviously important for the athlete, but it’s also important for the gen pop- particularly the aging population who is at risk for sarcopenia, decreased work capacity, and thus a host of other comorbidities (e.g. diabetes from decreased skeletal muscle buffering of blood glucose). The literature suggests that the aging population actually sees fantastic results with higher protein intakes and they even use whey protein shakes in many of their interventions.

tl;dr-Eat 3-5x per day tops, spread out 3-5 hours.
3) You will determine optimal protein intake by taking rules 1 and 2 into consideration with total calorie intake, age, and gender. It intuits well, given rules 1 and 2, that the optimal protein intake per day is initially based on how much protein a person needs per meal to maximize MPS multiplied by the number of meals they will have per day. Other factors that are taken into consideration to increase or decrease the protein prescription (new book title?) for an individual includes the following modifiers:
a)Gender- The more male someone becomes, the more sensitive to amino acids they are, in general. This would allow a male to need slightly less protein per pound than a weight and age-matched female. That being said, lean body mass weight also plays a role in the amount of leucine needed per meal to maximize MPS, but this is literally a variation of 0.5-1g tops for a range of bodyweights between 100lbs-300lbs, so we don’t take it into consideration and 3-4g is very safe.

b) Age- In general, the more someone ages the less sensitive they become to protein, so protein levels should go up over time slightly.

c) Dietary Preferences- As the quality of protein increases (based on bioavailability, protein digestibility amino acid corrected score, and amino acid profile) the total protein needed to optimize protein intake goes down. Similarly, the more vegan someone is, the more protein they require, i.e. the more calories from protein they require to get the same effect as their meat-eating, bone crushing, bacon frying counterparts. In short, the lower quality your protein sources are (lentils/rice/veggies/wheat/soy) the more protein you require for the same effect. This is an important consideration for those who are calorie restricted/limited.

4) You will not listen to bro’s who tell you that you only need x gram of protein/day. First off, we’re definitively NOT talking about protein needs here. Protein needs refers to what you NEED to not be deficient- not to optimize performance, aesthetics, or health but merely to survive. So yea, not what we’re talking about. Secondly, the amount of protein you actually need is a fairly complex answer based on everything we’ve discussed above. Do you really think the dude with the cut-off tee who maxes out on bench press every Monday and squats high (or more likely-leg presses) has taken all this into consideration before word vomiting his opinion to you while you foam roll? Doesn’t it make more sense that he noticed your new Lululemon yoga pants (if female) or is admiring your handsome combover (if male)? Seems more likely to me…

5) You will not listen to the bros who tell you that you can only absorb x gram of protein/meal. The poor bro, he can’t catch a break. So this oft-repeated nonsense goes around and around and just will not die…until TODAY. Let me be crystal clear, you absorb and use virtually 100% of everything that enters your gastrointestinal tract from your mouth. If you don’t, you’ll know it because you’ll be having watery diarrhea post-prandial (after a meal) since the undigested and unabsorbed food will act osmotically to draw water into the large intestine and then well, you know what happens after that. Look, we’ve done the tracer studies and know that when you eat any amount of protein at a meal it all gets absorbed. All of it. Actually 110-120% of it. Yep, MORE THAN 100%. That’s because the cells the line the  bowel, the enterocytes, make proteins themselves. These are called endogenous (made within the body) proteins and yep, they’re absorbed too. Yes Virginia, if you eat 100g of protein at a meal you’ll absorb it all. Yes, it will take longer than if you only ate 20g, but you’ll absorb the first 20g of protein from the 100g at the same rate as 20g on it’s own provided they have similar total fat content and fiber content within the entire meal. That being said, the time course to which a meal is absorbed matters little to anyone, unless they compete or train multiple times per day.

6) You will not get lured into buying expensive protein with sub optimal amino acid profile. People, if you’re paying more than ~10 dollars/lb of protein you’re getting duped, as the manufacturer is preying on your ignorance. Whey is the king protein, period. It’s better than the 100 dollar fish protein from a certain manufacturer who is big in the land of shirtless dudes and vibram 5 finger clad women. Why? Because its amino acid profile is better, i.e. it has more BCAAs (leucine/isoleucine/valine) and a higher concentration of essential amino acids. Also, it’s cheaper…so that seems to be a good point in and of itself. Whey trumps casein on satiety, MPS rates, and time that it keeps plasma (blood) amino acid levels elevated. In other words, all the nonsense the bro at GNC regurgitates about casein being a slow digesting protein that is good to take at night because it slowly releases amino acids from the GI tract is BS. Well, to be fair to him (bro) or her (bra?), it [casein] does more slowly release amino acids into the blood stream from the gut, but it’s TOO SLOW to actually raise blood amino acid levels high enough to effectively drive muscle protein synthesis unless you dose it much higher than whey, which is the king of proteins. Also, whey keeps you fuller, longer (satiety) than casein, and it’s CHEAPER. Yep, whey is better than egg protein, beef protein, hemp protein (sucks), rice protein (sucks), pea protein (double sucks), and soy protein (double sucks). Whey protein concentrate, one of the cheapest options out there is where everyone should start for whey supplementation. If it doesn’t upset your GI tract, then stay there and never look back. If it does- and it will in some who are sensitive to an amino acid fraction (beta lactalbumin) – switch to whey protein isolate, which has this fraction removed. Whey protein concentrate (WPC) might actually be superior to whey protein isolate (WPI) because b-lactalbumin is a very concentrated source of leucine- so I prefer WPC in those who can tolerate it. No Virginia, WPI doesn’t always mean better and as you just learned- more expensive is not always better.

7) You will not fall into the trap of megadosing protein, because gainzZz? So far we’ve described why it’s hard to put a firm number on optimal protein intake based on numerous variables. That being said, there is definitely an upper limit- though not for the reason your doctor will try to justify. Most physicians, PA’s, nurses, etc. will all try to recite the urea cycle and scream stuff about ammonia at you whilst telling you that your kidneys and/or liver will fail with high levels of protein intake. I think every time they do this an angel gets its wings because it occurs too frequently and is so far removed from what actually happens in vivo (in the body) that I assume it’s just a religious ritual that all health care providers learn in school and pay homage to periodically. While I do not have time to layout the entire metabolic pathway for ammonia and urea, the two  toxic byproducts of protein metabolism that supposedly build up an will harm your kidney and/or liver, I will briefly state that in a healthy person- there is no upper limit for protein intake, as the excretion (removal) rate of these toxins is massively upregulated in an adaptive way that is not harmful, but is a response to a hormetic stressor, i.e. something that disrupts our homeostasis. There is no evidence of any kidney or liver damage when the excretion pathways upregulate either. Similarly, in end stage renal disease, those who ate a “very low protein diet” had worse outcomes than those who ate either a “moderate protein” or “low protein” (but higher than very low) diet. This indicates, to me at least, that protein and its metabolism is not harmful to the kidney- even if it’s function is reduced. More data continues to accrue exposing other harmful factors to the kidney, namely elevated blood sugar in those patients who don’t deal with glucose very well….perhaps because they haven’t optimized their protein intake yet 🙂

I say all this sort of tongue-in-cheek, as I do think there is an actual upper limit to useful protein intake, i.e. there is an inflection point where increased protein dosing does not yield improvements in performance, muscle protein synthesis, aesthetics, etc. This point is obviously different for many people, but I could make a pretty strong argument to avoid intakes in excess of 300g or so for anyone who is under 350lbs. Think about the 200lb bro- replete with cut off tank- who eats 400g of protein per day. While only a fraction (maybe half- depending on sources, age, etc.) will actually contribute to MPS, the other half is getting burnt (oxidized) or converted to carbohydrates and/or fat for storage. These processes are all controlled by enzymes, who will adapt (of course) to the stress imposed upon them. If/when these enzymes upregulate, i.e. increase in number and activity, the body becomes more efficient at using protein for fuel (oxidation to yield energy) and/or converting it to carbohydrates and fat. Similarly, such a robust protein intake concomitantly decreases intake of other substrates to a degree, i.e. carbohydrate and fat intake will be lower in a person who eats 400g of protein than if that same person only ate 200g of protein. This all sums to create a situation where a person is very good at breaking down protein as fuel and, God forbid, should his protein level ever significantly drop below 400g for an extended period of time- like if he were to spend a week at the Jersey Shore and only consume 100-150g of protein/day- then theoretically protein turnover would continue to be elevated since the body’s enzymatic ability to break down protein is so upregulated. Just some food for thought.

-strengthmd

The Truth About Gluten

By Jordan Feigenbaum MS, CSCS, HFS, USAW CC, Starting Strength Staff

Unless you’ve been living under a rock or living off the grid for some time, chances are you’ve at least heard about gluten and gluten-free diets. There is good reason for this as gluten and similar nutrients have been the subject of a flurry of recent research efforts and clinical observations. To begin, let’s talk about what gluten is and why we’re even bringing it up.

Gluten is a protein that’s found in all products containing wheat, barley, rye and other foods as a binding agent and even in some prescription drugs. Gluten generally increases elasticity of the dough and improves its texture to aid in palatability. It lets bread rise and maintain its shape as well.

Gluten is made up of what we call prolamin proteins. This essentially means that gluten is made of constituents rich in proline (prol-) and glutamine (-amin) and in wheat’s case, these prolamin proteins are gliadin and glutenin [1]. The prolamin proteins in barley, rye, and corn are: hordein, secalin, and zein, respectively. Oats also contain a prolamin protein known as avenin, although this is a rather minor constituent in comparison to the others.

I will detail how these prolamin proteins interact with our bodies later on in this article, but for now we can say that these proteins resist being broken down in the small intestine by the usual proteases and peptidases [2]. Proteases and peptidases are enzymes that help the body break down proteins from food we ingest for absorption in the small intestine. We can intuit that this might possibly be a bad thing as I’ll discuss later.

As mentioned before, gluten is a hot topic these days. Using the Google search engine and typing in “gluten free” results in over 82 million hits. Originally the topic of gluten intolerance or using a gluten free diet was limited to those suffering from celiac sprue disease. However, the number of those diagnosed with celiac disease has been increasing steadily in recent times, affecting approximately 1 in 133 Americans and countless undiagnosed people. It is important to understand that this disease commonly goes undiagnosed, for almost 11 years in most cases [3]. The issue isn’t a lack of a formidable test to diagnose celiac or gluten intolerance, the test exists and it is very specific, however it is not very sensitive- or at least not as sensitive as some clinicians would prefer. At any rate we cannot deny that “gluten” and “gluten-free” are buzzwords in today’s health and fitness world.

Consider this, in 2003 there were approximately 135 “gluten-free” food products were introduced to the market and in 2008 alone there were 832 introduced. The growth in the gluten-free food sector has recently been estimated to be 15-25%. Then there’s the bevy of research coming out of the medical field.

A New England Journal of Medicine (NEJM) article catalogued 55 diseases associated with gluten intake including : osteoporosis, irritable bowel syndrome, anemia, cancer, fatigue, canker sores, rheumatoid arthritis, lupus, multiple sclerosis, numerous autoimmune diseases, anxiety, depression, schizophrenia, dementia, migraines, epilepsy, neuropathy, and autism [4]. Government agencies associated with Celiac disease also report a decrease in symptoms for patients going on a gluten free diet with the following diseases: rheumatoid arthritis, Parkinson’s disease, neuromyelitis, Down’s syndrome, peripheral neuropathy, multiple sclerosis, seizures, ataxia and late-onset Freidreich ataxia, brain fog, osteoporosis, type 2 and type 1 diabetes mellitus, and anemia [5].

There are many reasons to believe that some people have become more intolerant of gluten as the generations go by. Celiac disease prevalence is increasing and reports of increasing sensitivity to gluten have also come to light. Plausible causes of this include the genetic manipulation of wheat and other grains, increased exposure to gluten, prolamin proteins in more and more food products at higher concentrations, and increased public knowledge of gluten intolerance or celiac itself[6].

While going gluten-free hasn’t been established as a weight-loss protocol in and of itself, anecdotal evidence disputes this with many people seeing weight loss as a nice byproduct of utilizing this diet. Some experts postulate that this is because without gluten in the diet overall calorie intake is decreased, while others claim it’s because gluten drives one to consume more palatable food. I tend to agree with this sentiment.

There is little certainty whether or not gluten is directly correlated to weight loss or gain, except in celiac patients that is. celiac patients often present with nutritional deficiencies stemming from malabsorbtion of digested food in the gut. When they switch to a gluten-free diet, however, their gut lining is repaired and they absorb more nutrients. So we could imagine that if a celiac patient ate a similar amount of food before and after the switch to a gluten free diet and now they are absorbing more nutrients than before, they might potentially gain some weight.

Interestingly enough, gliadin, which is found in gluten, exhibits what’s known as an ­insulin-mimetic effect. Gliadin mimics insulin’s effect on fat cells, that is, it attaches to the same receptor that insulin does on fat cells and causes it to incorporate glucose from the bloodstream into the tissue and store it as fat, just like insulin does. Insulin normally has a negative-feedback loop that keeps it in check. So when insulin levels rise more and more blood glucose is shuttled into the fat tissue and when blood sugar has been returned to a normal level insulin levels fall as the hormone (insulin) no longer interacts with its receptor. Gliadin, however, does not exhibit this negative-feedback loop and stays attached to the receptor and continues to exert its effect [7]. Also gliadin interacts with digestive hormones such as cholecystokinin (CCK), which is involved in regulating appetite control. This gliadin exerts a negative effect essentially blocking appetite control and potentially causing storage of fat via its insulin-mimetic effect [7].

With all that out the way let’s delve in to what foods contain gluten, how gluten and prolamin proteins interact with the body, and what, if anything, we should do about it! Gluten, as mentioned before, is in all products made of wheat, processed with wheat, or anything that uses wheat, barley, rye, or modified food starch. These foods include:

-beers, breads, candies, cakes/pies, cereals, cookies, crackers, croutons, gravies, imitation meats, pastas, processed lunch meats, salad dressings, sauces (including soy sauce), self-basting poultry, soups, maybe oats during production, modified food starch, medications/vitamins may use gluten as a binding agent, play dough

Foods that don’t contain gluten include:

– corn, gluten-free flour, polenta, rice, tapioca, fresh meat, fruits, most dairy, potatoes, vegetables, wine/liquor/cider/spirits

When we take in any food it’s usually through the mouth (hopefully) and digestion, but not absorption, starts immediately. From the mouth the food is compacted into a bolus as it moves down the esophagus and to the stomach. In the stomach some digestion takes place but it and all the previous digestion pales in comparison to what is to come, digestion-wise, in the small intestine. After passing through the stomach the partially digested food enters the small intestine which is about 21 feet long and comprised of three different parts listed here from beginning to end: the duodenum, jejunum, and ileum.

Digestion primarily occurs in the duodenum, whereas absorption primarily occurs in the jejunum and ileum. We can think about the small intestine as a long tube with finger-like projections known as villi. The layer of cells covering the inside of this digestive tube are called enterocytes and these cells interact with any and all of the digested food particles including gluten and its components gliadin and glutenin. Enterocytes are sealed off between each other by what’s known as a tight junctions (zonula occludens), which is made up of three distinct proteins: cadherins, zonulins and occludins. We can generally think of the tight junctions in the gut as being impermeable or resisting the transmission of any molecule, substance, or compound between the cells. In a healthy person this would mean that absorption of nutrients happens directly across the enterocyte (transcellular) and not in between them (paracellular).

We already know that gliadin and gluttenin are not digested by the enzymes in the small intestine, via proteases and peptidases, and as such they interact with the enterocytes directly [2]. When these prolamin proteins interact with enterocytes they cause a disruption of the tight junctions of the small intestine. They do this by binding to a zonulin receptor on the enterocyte which causes a release of zonulin, which was previously bound tightly, and a subsequent remodeling of the enterocyte’s structure and a loss of occludin. So we no longer have zonulin and occludin doing their job binding tightly to one another and we get an opening in the small intestinal wall, or permeability of the digestive tube [8].

Chronic exposure to gliadin from gluten or similar substances can cause a down-regulation in production of zonulin and occludin, which further increases small intestine permeability [8]. This permeability allows molecules and substances to move freely into the body’s circulation or blood stream. Now these things are foreign and wherever these particles end up are recognized by the body’s immune system and this is bad news.

With this permeability other gliadin, glutenin, and prolamin proteins initiate an immune response, both the innate and cell-mediated immune cascade to be exact. The innate immune response causes the body’s inflammatory cells to be attracted to wherever these foreign materials end up. The innate immune response also ends up signaling inflammatory chemicals to be released to help destroy the invading foreigner. An enzyme called transglutaminase helps modify gliadin and gluttenin so that it more effectively stimulates the immune system [8]. We could envision a situation where all this inflammation in remote areas that these foreign substances have relocated could cause some serious damage and it’s not hard to see why the New England Journal of Medicine has associated 55 diseases with gluten intake and reactions.

With a permeable gut due to faulty tight junction functioning we get antigenic materials into our circulation. Some clinicians refer to this as leaky-gut syndrome, although it’s not widely recognized in Western medicine. Gut permeability has been linked to allergy induced autism, nutritional deficiency, increased absorption of toxins, liver inflammation, infection, rheumatoid arthritis, asthma, multiple sclerosis, vasculitis, Crohn’s disease, colitis, Addison’s disease, lupus, thyroiditis, chronic fatigue syndrome, and fibromyalgia [9].

So what do we make of all this? The research and anecdotal evidence seems to suggest eliminating gluten and similar prolamin protein-rich foods from the diet is probably a good idea. Eliminating wheat products, barley, rye, and other potential trouble sources like corn and oats is not very difficult to do, just don’t eat the products and use grass-fed meats, wild-caught fish, vegetables, nuts, fruits, roots, tubers, and seeds to make up your diet. By committing to 30 days of this elimination diet you will be able to accurately assess what effect, if any, these foods have on you. Do you feel better, look better, perform better at the end of this period of time?

After the elimination period you can try and revisit one of the eliminated foods to see what happens. Does it make you feel sick, gassy, or bloated? If so, you might be better off without it. Essentially you are drawing a line in the sand and setting a baseline for your own nutrition. By establishing a “normal” level of digestive health you can tweak the parameters to fit your own goals. If fat loss is the goal avoiding the wheat products might be smart due to the insulin-mimetic effect, their potential hyperpalatability, as well as avoiding processed foods in general. If you are looking to put on some size then you should also think about optimizing your ability to absorb the foods you eat so perhaps taking in potentially noxious food stuffs isn’t a good idea. Hopefully you liked this article! Please share it with friends, family, and coworkers if you did!

-thefitcoach

References

1) http://www.celiac.com/articles/8/1/What-is-gluten-What-is-gliadin/Page1.html

2) Lammers KM, Lu R, Brownley J, et al. (July 2008). “Gliadin induces an increase in intestinal permeability and zonulin release by binding to the chemokine receptor CXCR3”. Gastroenterology 135 (1): 194–204.e3. doi:10.1053/j.gastro.2008.03.023. PMC 2653457. PMID 18485912.

3) http://www.celiac.com/

4) http://www.nejm.org/doi/full/10.1056/NEJMra010852

5) http://www.glutenfree-diet.org/benefits.htm

6) http://www.huffingtonpost.com/david-katz-md/gluten-free-diet_b_907027.html

7)  http://intelegen.com/nutrients/lectins_their_damaging_role.htm

8)  S. Drago et. al Gliadin, zonulin and gut permeability: Effects on celiac and non-celiac  intestingal mucosa and intestinal cell lines. Scandinavian Journal of Gastroenterology, 2005; 41: 408-419

9) http://www.ei-resource.org/illness-information/environmental-illnesses/leaky-gut-syndrome-(lgs)/