Processed foods are part of most people’s diet. They are packed with salt, sugar, fat and loads of additives. One of the most common additives is wheat, hidden in many different ingredients. This can make following a gluten-free diet impossible if you aren’t in the habit of reading labels. We have compiled a list of common places that wheat and gluten may be hiding in processed foods.
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Hidden Sources of Wheat
Breadings and coating mixes
Brown Rice Syrup (May contain malted barley)
Canned meats and fish in broth
Caramel Color (Usually corn-derived, but check)
Cheese products- Sauces and some shredded cheeses
Condiments (Carefully read condiment labels. Gluten is often used as a stabilizer or thickening ingredient in ketchup, mustards and Oriental sauces)
Deli Meats, breaded fish and meats, pre-packaged ground beef products and hot dogs
Dextrin (Usually corn-derived but always check)
Flavorings, food starches, seasonings, and malt are general and vague words to watch for on labels of packaged foods. These terms are often clues that the product may contain gluten. For example, “malt” vinegar and “malted” milk powder contain gluten.
Gravy Products (Dry products, bouillon cubes, and processed, canned products)
Hydrolyzed Vegetable Protein (HVP) and Texturized Vegetable Protein (TVP)
Imitation fish, meats and cheeses
Instant flavored coffee/cocoa mixes
Licorice candy (black and red)
Modified Food Starch
Mono and di-glycerides
Sauces, including soy sauce which is commonly made by fermenting wheat. (Check ALL processed sauce labels- From BBQ sauce to ice cream toppings, chili pepper products and tomato sauce products-all may contain gluten)
Self-basting poultry products including turkey with added “solutions”
Snack foods including flavored potato chips and corn chips
Soups, stocks and broth
Spice and herb blends (spices and herbs in their natural form do not contain gluten)
Rice products with seasoning packets
As you can see, the list is pretty long. Obviously, your best bet would be to avoid processed foods whenever you can but that’s not always possible. When you do have to rely on processed foods, do two things to protect yourself from gluten and other dietary bad actors: read the ingredients and take DigestShield® before you eat.
We mention “bad actors” frequently on our website because there are so many of them in the industrialized food supply. It is our goal to raise awareness about this fact so that we might contribute to improving your health. To better understand what these bad actors are and why they are a problem, keep reading.
Gluten is a blessing and a curse. It is responsible for giving bread and other baked goods their wonderfully chewy, elastic texture. However, recent evidence tells us that it is also very difficult to digest and responsible for immune activation and leaky gut in many individuals.
Gluten works in bread by forming an elastic web, which traps air and carbon dioxide during baking, leading to a fluffy, squishy lattice. This makes for fantastic texture in baked goods. Just think of a fresh-baked, still steaming roll.
Gluten works in your small intestine by binding to special receptors that signal a hormone to loosen the tight junctions between the cells there. This makes for less-than-fantastic opportunities for gluten and the other bad actors to trigger an immune response, causing damage to your cells. Just think of bloating, indigestion and gut pain.
The long-term effects of gluten exposure are worse than indigestion and gut pain, though. Researchers have theorized that repeatedly weakening the tight junctions of your gut by exposing it to gluten almost continually could be one of the steps to autoimmune diseases.
Plant lectins are a blessing for plants but a curse for all of us. Lectins are found in nearly 40% of the American food supply but wheat is the worst source. Plants evolved these lectins to work as deterrents to their predators. They are proteins that are really good at sticking to the sugars in our cells. After they are good and stuck, they can actually destroy the cells they are stuck to. Just like gluten, this creates opportunity for lectins and other bad actors to get past the wall and into the bloodstream
Again, researchers fear that over time and with repeated exposure, this weakening of the integrity of the gut wall could open the door for chronic inflammatory and autoimmune diseases. We call lectins ninjas because they have been secretly assassinating cells in our gut for a long time. The science shining a light on these ninjas is called lectinology and is relatively new. Lectinology has found that we can protect ourselves from these ninjas by using decoy sugars.
Bad Yeast and Bacteria
Our bodies are home to billions of bacteria and yeast all of the time. Most of the time, they are helping us by digesting things that we can’t, making vitamins, and boosting our immune system. Sometimes, however, certain yeast and bacteria can get out of control and cause problems. Think of the situation like a house party.
Lots of people are there and most of them are having a great time and improving the atmosphere with their jolliness and good mood. But there are always a few people at parties that just have to take it too far. They drink too much, they make too much noise, they go into parts of the house you asked them not to and sometimes they break stuff. Your gut is just like that – most of the yeast and bacteria are there having a great time and making the place better but there are a few of the party goers that will take it too far if given the chance.
A way to prevent this is by taking a high quality probiotic. The term probiotic is a fancy way of saying “good bacteria.” Probiotics are like a really well thought out party invite list. You’re putting only good, well behaved bacteria into your gut so that everyone has a great time and the environment is made better.
Undigested Fats, Carbohydrates, and Proteins
It is a little unfair of us to call these bad actors because they are just foods that are minding their own business but accidentally find themselves where they are not wanted. The immune system is not particularly understanding about things being where they are not supposed to be in the body. Undigested foods that stumble through the holes in a leaky gut get treated just like any other invader.
Fats, carbohydrates, and proteins need to be broken down into their building blocks before the body can use them. When gluten or lectins put holes in the wall, sometimes these foods slip through before they are small enough to be used and this can activate the immune system.
There are two good ways to minimize the risk of this happening: heal the gut wall and provide extra enzymes to more quickly break these foods down. Enzymes are chemicals that the body uses to break foods into small enough parts for absorption.
As you know, not all foods are created nutritionally equal. This applies to the digestibility of foods as well. We’ve covered how gluten and lectins are resistant to digestion but they are not the only ones: Lactose, the sugar found in dairy products, and phytate, the storage form of phosphorus in plants, can also be difficult to break down.
Dietary bad actors refer to things we eat which can cause digestive distress or illness. The things we eat were not created equal. Some are a benefit to us and others can be dangerous. There are some foods that contain what has become known as “anti-nutrients” that are always a problem and others that can become a problem in certain situations. We call these problematic foods dietary bad actors and they are the focus of our research at Shield Nutraceuticals. We developed DigestShield® to help mitigate the damage that these dietary bad actors can cause.
The term gluten refers to a compound of two storage proteins found in the endosperm of wheat, barley, and rye. The proteins glutenin and gliadin are bound together with starch inside the wheat germ. These proteins provide many functional properties when used in baking and are the main source of protein in those grains. (1)
Of the two proteins in gluten, glutenin is the most important for baking, having the greatest effect on elasticity and texture of the final product. (2) Gliadin is the protein fraction that causes problems during human digestion and the protein that triggers an immune response in the body after ingestion. (3)
Gliadin has been shown to produce both innate and adaptive immune responses and is thought to be involved with the pathogenesis of many autoimmune diseases. Most importantly to note, it has recently been shown that gliadin can promote an immune response in individuals with or without the genetic predisposition for reaction. (4)
In addition to an immune and inflammatory response, gliadin also contributes to the development of a condition known as leaky gut in which intestinal permeability is increased and molecules of inappropriate size are allowed through the intestinal wall.
It has long been understood that gliadin produced an immune response in those with celiac disease (5) but recently researchers have discovered that gliadin also produces an immune response in healthy individuals. (6) The immune response is not uniform among individuals and a differing severity of response is not well understood. Most likely, as with all immunity, it is based upon a variety of factors including genetic susceptibility, intestinal permeability, environmental factors, gut flora, and overall health.
Though it is still not well understood, it has been shown that gliadin can trigger a response from the innate immune system and cause intestinal and extra-intestinal symptoms in non-celiac individuals. (6-8) In individuals with celiac disease, the innate immune system trigger is a precursor to adaptive immunity involvement. A large part of gliadin’s ability to elicit a response from the innate immune system is based upon its resistance to degradation (9) by the digestive process and its ability to cross the epithelial wall relatively intact. This allows gliadin, as a macromolecule, access to areas where many innate immune cells are found and the interaction is inevitable. Once this interaction occurs, gliadin shows the ability to activate undifferentiated immune cells that then proliferate while simultaneously producing pro-inflammatory hormones. This hormone production results in several downstream inflammatory responses. (10)
Though the adaptive immune system does not appear to play a role in the deleterious effects that gluten has on healthy, non-celiac individuals, gliadin very demonstrably activates the adaptive immune response in genetically susceptible individuals. (5) The immune response triggered in celiac individuals is varied and aggressive. It includes activation of T-cells, and eventually the autoimmune targeting of tissue transglutaminase in the body’s cells. (11)
The potentially greater threat posed by gluten is the role that it plays in intestinal permeability. For reasons not yet understood, gliadin has the ability to bind to receptors in the intestine that signal for the release of a hormone, which promotes the tight junctions of the epithelial cells to be degraded. Once these tight junctions are opened gliadin, as well as other pathogens, can bypass the physical barrier of the gut and interact directly with immune cells. (12)
Lectin is a broad term for a class of proteins found in all plants and animals. We have lectins in our bodies that serve a wide variety of functions including regulation of serum protein levels, removal of glycoproteins from the circulatory system, and mediation of important immune functions. (13) However, many of the plants that are part of our food supply contain lectins with a very different and specific function: defense. Lectins are the defense mechanism against predators, including fungi, that seek to eat the plant. Lectins are designed to cause digestive distress to keep predators away.
Lectins are found in the greatest concentration in grains (especially wheat), legumes such as soy, nuts, and seeds, and nightshade vegetables. It has been estimated that there are concentrated sources of lectins in 30-40 percent of the American diet (14) though that figure is more than likely higher as the survey of foods it is based on was done in 1980 and our food supply has become more filled with wheat, soy, and potato based processed foods since then.
Much like gluten, lectins have been shown to be resistant to cooking and the digestive process. (15) Because they are not degraded by the human digestive process, many lectins reach the gut intact where they perform their defensive attack on the epithelial cells that line the small intestine. Though lectins may play a role in the pathogenesis of many autoimmune diseases just like gluten, the likely mechanisms are different. Unlike gluten, lectins directly damage the cells that they attach to. At first, this means epithelial cells but once a leaky gut has been created and the lectins are able to enter the bloodstream, they may attach to any of the tissues in the body. (16)
Lectins increase intestinal permeability by directly binding to and destroying epithelial cells. (17) Once through the epithelial barrier, not only do lectins bind to and destroy cells in other parts of the body, but they may also lead to an autoimmune response through cellular mimicry. (19) In addition to their own damaging effects, the leaky gut they create may allow for other pathogens to bypass the body’s first line of defense. (20)
Another outcome of damaged epithelia is impaired nutrient absorption. Even before the damage is done, lectins have been shown to bind to the receptors in the epithelia thereby preventing nutrients from being absorbed and reducing the digestibility of proteins in the diet. (21, 22)
Aside from increase the opportunity for autoimmune disease pathogenesis through the degradation of tight junctions, lectins also present autoimmune activation potential themselves. Lectins have been shown to stimulate class II HLA antigens on the pancreatic islet and thyroid cells.(23) Lectins have been heavily implicated in the pathogenesis of rheumatoid arthritis, an autoimmune disease, as well. (24-26)
Bacteria and Yeast
There are trillions of microorganisms living within us at all times and not all of them are beneficial. (27) Though we do not yet understand the entirety of the vast interplay between the human microbiota and health, researchers have identified many strains that play either a primary or opportunistic role in negative health outcomes. (28) Gut dysbiosis, or out of balance gut bacteria, has been implicated in a variety of disease states and is believed to be a necessary condition for the development of inflammatory bowel disease. (29)
Opportunistic bacteria and yeast are not damaging when present in small amounts but can lead to disease states when over-abundant and are also the cause of common ailments. Gastric and duodenal ulcers are caused when the bacterium H. pylori is able to over-colonize these areas and erode the protective mucosal layer. (30) Another well-documented example of this is overgrowth by the fungal species Candida albicans. Candida is the fungus responsible for the ailment commonly referred to as yeast infection, vaginal and in other parts of the body. (31)
Partially Digested Foods
Finally, foods that have not been fully digested can cause problems in a variety of ways. Nutrient uptake is dependent upon sufficient breakdown of foods into constituent parts of specific particle size.(5) There are primarily two situations in which incompletely digested nutrients become a problem; If we lack or have a deficiency of the enzyme required to degrade a food and if intestinal permeability is increased and allows macromolecules through the epithelial border.
Many individuals do not have sufficient lactase production to properly digest the amount of lactase found in the typical American diet. This causes incompletely digested lactose, the sugar found in dairy products, to cause intestinal discomfort in those affected. (31) Additionally, everyone lacks the full amount of enzymes required to hydrolyze the protein gliaden found in wheat, barley, and rye. (4)
Depending on the individual, this can lead to gluten-containing products causing symptoms everywhere from mild discomfort to debilitating illness, while causing increased gut permeability. (4)
The degradation of the tight junctions forming the physical barrier of the epithelium allows particles to cross this border at an inappropriately large size. (33) The immune reaction occurs when any molecule is recognized as inappropriate for the area it is in. This, of course, includes incompletely digested fats, proteins, and carbohydrates. (34)
Shewry, P., Halford, N., Belton, P., & Tatham, A. (2002). The structure and properties of gluten: an elastic protein from wheat grain. Philosophical Transactions Of The Royal Society B: Biological Sciences, 357(1418), 133-142. doi:10.1098/rstb.2001.1024
Wheat Protein Composition and Properties of Wheat Glutenin in Relation to Breadmaking Functionality. (2015).Critical Reviews In Food Science And Nutrition.
Caio, G., Volta, U., Tovoli, F., & De Giorgio, R. (2014). Effect of gluten-free diet on immune response to gliadin in patients with non-celiac gluten sensitivity. BMC Gastroenterol, 14(1), 26. doi:10.1186/1471-230x-14-26
Drago D., Asmar R., Di Pierro M., et al. (2006) Gliadin, zonulin and gut permeability: Effects on celiac and non-celiac intestinal mucosa and intestinal cell lines. Scan J. of Gastro. 41(4)
Mahan, L. Kathleen., Escott-Stump, Sylvia., Raymond, Janice L.Krause, Marie V. (Eds.) (2012) Krause’s food & the nutrition care process /St. Louis, Mo. : Elsevier/Saunders
Verdu, E., Armstrong, D., & Murray, J. (2009). Between Celiac Disease and Irritable Bowel Syndrome: The “No Man’s Land” of Gluten Sensitivity. Am J Gastroenterol, 104(6), 1587-1594. doi:10.1038/ajg.2009.188
Hadjivassiliou, M., Sanders, D., Grünewald, R., Woodroofe, N., Boscolo, S., & Aeschlimann, D. (2010). Gluten sensitivity: from gut to brain. The Lancet Neurology, 9(3), 318-330. doi:10.1016/s1474-4422(09)70290-x
Sapone, A., Lammers, K., Casolaro, V., Cammarota, M., Giuliano, M., & De Rosa, M. et al. (2011). Divergence of gut permeability and mucosal immune gene expression in two gluten-associated conditions: celiac disease and gluten sensitivity. BMC Medicine, 9(1), 23. doi:10.1186/1741-7015-9-23
Hausch, F., Shan, L., Santiago, N., Gray, G., & Khosla, C. (2002). Intestinal digestive resistance of immunodominant gliadin peptides. American Journal Of Physiology-Gastrointestinal And Liver Physiology, 283(4), G996-G1003. doi:10.1152/ajpgi.00136.2002
de Punder, K., & Pruimboom, L. (2013). The Dietary Intake of Wheat and other Cereal Grains and Their Role in Inflammation. Nutrients, 5(3), 771-787. doi:10.3390/nu5030771
van Heel, D. (2006). Recent advances in coeliac disease. Gut, 55(7), 1037-1046. doi:10.1136/gut.2005.075119
M G Clemente, A. (2003). Early effects of gliadin on enterocyte intracellular signalling involved in intestinal barrier function. Gut, 52(2), 218.
Maverakis E, Kim K, Shimoda M, Gershwin M, Patel F, Wilken R, Raychaudhuri S, Ruhaak LR, Lebrilla CB (2015). “Glycans in the immune system and The Altered Glycan Theory of Autoimmunity”. J Autoimmun57 (6): 1–13.
Nachbar, M., & Oppenheim, J. (1980). Lectins in the United States diet: a survey of lectins in commonly consumed foods and a review of the literature. The American Journal Of Clinical Nutrition,33(11), 2338-2345.
Pusztai, AP. Chemistry and pharmacology of natural products: plant lectins. Cambridge University Press, Cambridge; 1991
Kelsall, A., FitzGerald, A., Howard, C., Evans, R., Singh, R., Rhodes, J., & Goodlad, R. (2002). Dietary lectins can stimulate pancreatic growth in the rat. International Journal Of Experimental Pathology, 83(4), 203-208. doi:10.1046/j.1365-2613.2002.00230.x
Wang, Q., Yu, L., Campbell, B., Milton, J., & Rhodes, J. (1998). Identification of intact peanut lectin in peripheral venous blood. The Lancet, 352(9143), 1831-1832. doi:10.1016/s0140-6736(05)79894-9
Miyake, K., Tanaka, T., & McNeil, P. (2007). Lectin-Based Food Poisoning: A New Mechanism of Protein Toxicity. Plos ONE, 2(8), e687. doi:10.1371/journal.pone.0000687
Cordain L, e. (2015). Modulation of immune function by dietary lectins in rheumatoid arthritis. – PubMed – NCBI .Ncbi.nlm.nih.gov.
A, V. (2015). Lectins, agglutinins, and their roles in autoimmune reactivities. – PubMed – NCBI. Ncbi.nlm.nih.gov.
Pusztai A, et al. Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins. Br J Nutr. 1993; 70(1): 313-21
Vasconcelos I. Oliveira J. Antinutritional properties of plant lectins. Toxicon 2004; 44(4): 385-403
Freed, D. (1999). Do dietary lectins cause disease? : The evidence is suggestive—and raises interesting possibilities for treatment . BMJ : British Medical Journal,318(7190), 1023.
Cordain L, et al. Modulation of immune function by dietary lectins in rheumatoid arthritis. Br J Nutr 2000;83:207-217.
Braun J & Sieper J. Rheumatologic manifestations of gastrointestinal disorders. Curr Opin Rheumatol 1999;11:68-74.
Hoss VK, Raabe G, Muller P. Lectin arthritis: a new arthritis model. Allerg Immunol (Leipz) 1976;22:311-316
Eckburg, P. (2005). Diversity of the Human Intestinal Microbial Flora.Science, 308(5728), 1635-1638. doi:10.1126/science.1110591
Gaurner F. Malagelada J-R. Gut flora in health and disease. Lancet 2003: 361 (9356): 512-519
C P Tamboli, J. (2004). Dysbiosis as a prerequisite for IBD. Gut, 53(7), 1057.
Graham, D. (1992). Effect of Treatment of Helicobacter pylori Infection on the Long-term Recurrence of Gastric or Duodenal Ulcer . Annals Of Internal Medicine,116(9), 705. doi:10.7326/0003-4819-116-9-705
M. Huppert, J. (1953). PATHOGENESIS OF CANDIDA ALBICANS INFECTION FOLLOWING ANTIBIOTIC THERAPY I. : The Effect of Antibiotics on the Growth of Candida albicans. Journal Of Bacteriology, 65(2), 171.
Human digestion starts at the mouth and ends at the anus. There are several mechanisms in the mouth that immediately begin to break down the foods we eat and prepare them for the rest of the digestive process. Through the process of mastication, or chewing, we are physically breaking the food into smaller pieces, which will help it travel more easily through the rest of the digestive system as well as increase the surface area available for the chemical agents in our body to bind to and break down the food.
Glands under the tongue secrete saliva, a mixture of water, mucus, proteins, mineral salts and the enzymes lingual lipase and salivary amylase. Saliva moistens the food and begins to break down the fats and carbohydrates while the teeth and tongue combine the food into a mushy ball.
As we swallow, this ball, now referred to as a bolus, is pushed to the back of the oral cavity and into the esophagus. A flap of muscle known as the epiglottis closes over the trachea, or windpipe, preventing any swallowed solids or liquids from entering the lungs.
Once in the esophagus, the bolus is moved into the stomach via a process called peristalsis, which is a downward wave of muscle contraction. Peristalsis continues through most of the digestive system and is the primary mechanism that moves foods through the digestive tract. This action is also referred to as a “housecleaning wave”.
Where the esophagus attaches to the stomach, there is a valve called the lower esophageal sphincter that regulates the movement of material from the stomach. In normal circumstances, it stays closed except when allowing a bolus to pass from the esophagus into the stomach. It typically takes roughly 10 seconds for food to pass from the top of the esophagus to the stomach.
The stomach is essentially a bag made of three layers of muscle. Because of this muscled composition, the stomach is capable of contraction and expansion. It can expand to accommodate roughly a liter of food and liquid at once before any distention pressure is felt. It is also this ability to expand and contract that allows the stomach to mix, grind and churn the bolus. Additionally, 1.2 to 1.5 liters of gastric juice is secreted per day into the stomach.
Gastric juice is a mixture of water, hydrochloric acid, electrolytes (sodium, potassium, calcium, phosphate, sulfate, and bicarbonate), mucus and enzymes. This juice is highly acidic due to its hydrochloric acid content and contains enzymes, both to break the bolus down further and make it more soluble in preparation for absorption to occur in the small intestine. At this point, the semisolid mixture created from the bolus is called chyme. While in the stomach, some absorption can occur though not very much. Small amounts of fluid (such as water and alcohol) can be absorbed from the stomach as well as some simple sugars like glucose and some amino acids. Many pharmacological agents are absorbed here as well.
The time that the chyme stays in the stomach depends on the chemical and physical composition of the meal as well as the specific physiology of the individual. Fluids empty the most rapidly followed by carbohydrate, protein, and fat in that order.
After an average of 2 to 4 hours in the stomach, when the food particles in the chyme have been reduced sufficiently in size and are at the appropriate level of solubility, the chyme will move through the valve at the base of the stomach, called the pyloric sphincter into the first section of the small intestine called the duodenum. (doo-oh-dee’-num)
The small intestine is roughly 20 to 25 feet long and about 2 inches in diameter. It is the longest section of the digestive system and is divided into three sections. The first section, where the stomach meets the small intestine is called the duodenum. The duodenum is roughly 9 to 11 inches in length and contains the duodenal papilla where pancreatic juice and bile flows into the small intestine. When the chyme enters the duodenum, special cells in the walls produce the hormones secretin and cholecystokinin.
These hormones signal for the pancreas to deliver pancreatic juice, which contains the enzymes trypsinogen, chymotrypsinogen, elastase, carboxypeptidase, pancreatic lipase, nucleases, and amylase as well as bicarbonate. The bicarbonate concentration neutralizes whatever stomach acid comes with the chyme so that the enzymes are able to work and the small intestinal wall is not damaged by the hydrochloric acid.
Cross section of the small intestine at increasing magnification.
Cholecystokinin and secretin also signal for the sphincter of Oddi, a valve at the base of the common bile duct to relax, releasing bile into the duodenum. Bile is a brownish yellow liquid that is continuously produced by the liver. It is composed of water, bicarbonate, phospholipids, bile salts, emulsifying agents, cholesterol, and bile pigments. It is stored and concentrated in the gallbladder until release into the duodenum for digestion. Bile serves important functions in fat digestion, coating fat particles from food and allowing greater surface area for pancreatic lipase to work.
The combination of enzymes and bile acids serves to further reduce the particle size and increase the solubility of the chyme. This allows for the nutrients within the food to pass through the walls of the small intestine and be carried throughout the body for use. Enzymes within the walls of the small intestine carry out any final breakdown of nutrients as the chyme travels toward the large intestine.
The remaining length of the small intestine is divided into the jejunum and ileum. These sections are much longer than the duodenum. The jejunum is the middle section and is roughly 8 feet long while the ileum, the final section of the small intestine, is nearly 12 feet long. The chyme travels along the length of these sections and the useable nutrients are slowly absorbed as it completes its journey to the bowel.
The total estimated surface area of the small intestine is approximately 5,400 square yards. This incredible surface area is provided by the unique structure of the cells that line the interior of the small intestine, which is arranged in a series of concentric folds that take the shape of transverse ridges along its length. These folds, called plicae circulares or valves of Kerckring are present in almost the entire small intestine with the exception of the first few inches near the stomach and the last few inches near the large intestine.
Villi & Microvilli
The surface area of the small intestine is also increased by the tiny projections called villi that make up the mucosal barrier. Inside of the villi is a loose structure of connective tissue containing a network of blood vessels, a central lacteal, and muscle tissue. There are specialty cells called goblet cells scattered among these villi that secret mucin, the primary constituent of mucus.
At the base of these villi, there are depressions referred to as intestinal glands or Lieberkuhn’s glands. In the bottom of these depressions are epithelial cells called cells of Paneth that are filled with enzymes that are toxic to bacteria and immunoglobins.
Additionally, there are undifferentiated cells, more goblet cells, and endocrine cells located in the Lieberkuhn’s glands. The undifferentiated cells serve to replace losses of other types of cells as they can undergo changes in structure as appropriate. Endocrine cells release hormones from the endocrine system into the small intestine to modulate multiple physiological functions including release of enzymes, release of hormones and control of intestinal motility.
The mucosal villi are additionally covered in tiny, hair-like projections called microvilli. They are small enough that each villus may be covered with as many as 1000 microvilli. These microvilli make up the primary site of nutrient absorption in the body referred to as the brush border.
Water and other solutes pass through the pores in these microvilli via active transport and drag caused by differences in osmotic gradient between the lumen and cytoplasm. The size of these pores differs along the length of the small intestine. This pore size difference in combination with receptor specificity along the length of the small intestine is why different nutrients are absorbed in different sections. The microvilli also secrete the digestive enzymes disaccharidase and peptidase that hydrolyze sugar and protein molecules respectively.
Enterocytes here are joined near their apex by strands of proteins connecting them in what are known as tight junctions. These tight junctions serve to keep larger molecules out of the bloodstream and it is thought that they are modulated as part of the immune system.
The juncture of the small intestine and large intestine is the ileocecal valve. Whatever remains of the chyme will pass from the ileum into the cecum, the first section of the large intestine, here.
The large intestine, also called the colon, is the last part of the digestive system. It is roughly 5 feet long and 2.5 inches wide. The large intestine is divided into four sections, moving from the small intestine to the rectum: the cecum, ascending colon, descending colon, and sigmoid colon. Structurally it is similar to the small intestine with the exception of the villi and microvilli. The muscle fibers making up the large intestine are arranged such that the interior of the colon forms circular furrows of varying depths called haustra. There is a small pouch connected to the cecum known as the vermiform appendix or just appendix. Though it is surrounded by a concentration of immune cells, it was long believed to be a useless evolutionary vestige. New evidence indicates that the appendix may serve as a reserve of healthy bacteria to help repopulate the gut after a colony destroying illness.
Functionally, the large intestine absorbs water and electrolytes from the chyme and packages the remains, along with dead bacteria and cells, into feces. The feces are stored in the large intestine until they can be removed via defecation. Factors that determine the composition and liquidity of feces include overall hydration status, fiber, and other indigestible food solids, and the composition of the bacterial colonization in the large intestine.
The majority of the microbes living in the body are found in the large intestine. These large numbers of bacteria synthesize niacin (nicotinic acid), thiamin (vitamin B1), and vitamin K, vitamins that are essential to several metabolic activities as well as to the function of the central nervous system. Additionally, they ferment otherwise indigestible chyme remnants into forms usable by the body. These monosaccharides can be absorbed in the large intestine as well. A byproduct of the fermentation, (cellular respiration) occurring in the bowel, is gas production.
The gas, referred to as flatus, is mostly composed of non-fragrant gases: nitrogen, oxygen, carbon dioxide, and methane. Only 1% of the compound’s inflatus is responsible for its distinctive odor. These are volatile sulfur compounds and are a combination of hydrogen sulfide, methyl mercaptan, dimethyl sulfide, and dimethyl trisulfide.
Once the rectum reaches a certain volume of feces and/or flatus, signals are sent for the urge to defecate. The anus is voluntarily relaxed and feces are pushed out of the body.
This completes the digestive process.
Mahan, L. Kathleen., Escott-Stump, Sylvia., Raymond, Janice L.Krause, Marie V. (Eds.) (2012) Krause’s food & the nutrition care process /St. Louis, Mo. : Elsevier/Saunders
Barrett, Kim E. Gastrointestinal Physiology (Lange Physiology Series). 1st ed. New York: McGraw-Hill Medical, 2005
After reading hundreds of articles and research papers, we started to come across several papers and theories that seemed like the pieces of a puzzle whose image was hidden. After several years and much effort, the pieces finally started fitting together to reveal a compelling picture.
Digestive Health – it’s as much about the journey as the destination.
The following is our interpretation of what may be behind the increase in autoimmune and food-related disorders:
Though it is a complicated, poorly understood, and controversial condition, we believe that leaky gut syndrome is highly relevant and may play a crucial role in the development of celiac disease, Crohn’s disease, ulcerative colitis, rheumatoid arthritis, asthma, chronic fatigue syndrome, psoriasis and much more.
We understand that leaky gut syndrome is a widely debated condition and that not all health professionals believe it to be related to (or a direct cause of) disease. As research progresses, many doctors, dietitians, and researchers are becoming aware of the condition and seek ways to test for and treat it.
If you haven’t heard of leaky gut syndrome, please read below:
Leaky gut syndrome is the easier-to-say term for increased intestinal wall permeability. It just means that gut wall is easier to cross than it should be. The gut wall begins to be more porous and develop holes. Basically, your gut is leaking things it shouldn’t into your bloodstream.
Leaky gut is thought to be caused or worsened by certain components of foods (more on that later), cytotoxic drugs, NSAIDS (non-steroidal anti-inflammatory drugs), irradiation of food, antibiotics, unbalanced gut flora, excessive alcohol consumption and compromised immunity.
How It Works
The intestinal lining is on the front lines of our immune system. We like to think of it as castle wall – we let the drawbridge down for visitors we know (like food and resource deliveries) but we leave it up to keep out invaders.
The other layers of this sophisticated defense is called the epithelium. A single layer of epithelial cells normally stay connected together by tight junctions. These tight junctions are how the passage of nutrients is regulated in the digestive tract. The epithelial cells in the gut are tipped with finger-like projections called villi. When food is digested, villi absorb the nutrients and transport them through the epithelial cell into the bloodstream.
When the digestive process is functioning normally, the tight junctions stay closed and only nutrients are allowed to pass through into the blood stream. When something goes wrong, the tight junctions become permeable or “open” and allow un-screened molecules through the border and into the bloodstream. Examples of things that can get through in this situation are bacteria, pathogens, yeast, incompletely digested food, lectins and more. That’s why we call it a leaky gut.
As this process continues over time, the intestinal lining can become damaged and even leakier, allowing even more “undesirables” through the intestinal wall and directly into the bloodstream.
Typically, this increase in offenders in the blood will make the liver and kidneys work that much harder to filter it all out. As the gut becomes increasingly damaged, the liver or kidneys may not be able to keep up with the constant flow of bacteria, pathogens, yeast, undigested macro-nutrients and waste products escaping through the gut lining.
As more invaders get through, overworking and overwhelming liver and kidneys, they are able to wreak havoc systemically (throughout the body).
When these offenders attach to the cells lining the gut, an immune response is triggered which can lead to collateral damage of healthy cells. This can lead to another chain of events in which the immune system begins to recognize certain molecules from food as invaders, calls for an immune response whenever you eat those foods, which can then cause even more collateral damage. This collateral damage can be experienced as bloating, cramps, diarrhea, inflammation, joint pain, skin rashes, headaches, malabsorption and more.
As the result of continuous immune response and corresponding collateral damage, the gut becomes more and more damaged. If you are frequently eating foods that it recognizes as an invader – it has no time to heal. Healthy cells are destroyed and those microvilli we talked about earlier are not able to do their job, which prevents your body from getting all the nutrients that you need, which in turn leads to all sorts of problems such as a weakened immune system or nutritional deficiencies.
To make matters worse, as your immune systems weakens, you become more susceptible to illness from the stream of junk (toxins, bacteria, pathogens, etc.) flowing through your leaky gut.
If this vicious cycle continues for weeks or months or years, you body may ultimately end up fighting itself, potentially leading to the initiation of autoimmune diseases such as as Crohn’s disease, ulcerative colitis, multiple sclerosis, type 1 diabetes, lupus, rheumatoid arthritis, chronic fatigue syndrome, fibromyalgia, vasculitis, urticaria (hives), alopecia areata, polymyalgia rheumatica, Raynaud’s syndrome, vitiligo, thyroiditis, and Sjogren’s syndrome.
With me so far? Great!
Let’s go deeper and talk about the probable triggers that start off this awful process.
The Hidden Causes
Some of the most interesting emerging research regarding digestion and autoimmune disease has to do with a few factors that could be triggers for opening the draw bridge (tight junctions) of the gut. A few key factors that appear to be the likely causes of leaky gut are zonulin, gluten (the gliadin portion), and some lectins.
Zonulin is a protein that modulated the permeability of the tight junctions in the gut. So far, it is the only “key” that we know the human body produces. Zonulin upregulation has been implicated in the pathogenesis of several autoimmune diseases including celiac and type 1 diabetes. Zonulin is currently being studied as a potential target for celiac treatment.
Gliadin (1/2 of the protein complex we commonly refer to as gluten) has been shown to active (upregulate) zonulin signaling in everyone, regardless of celiac status, leading to the opening of tight junctions in the gut and leading to increased gut permeability. Gliadin is found in wheat, barley, rye, and triticale, which are all grains found nearly everywhere in our modern food supply. There are three main types of gliadin (α, ϒ, and ω), and they all produce an immune response in those with celiac disease.
The term lectin refers to a specific class of proteins that bind to carbohydrate moieties. They are found in almost all plants and animals but the variety that we are most interested in are concentrated in certain plants and some dairy products. These lectins bind to glycoproteins and glycolipids (sugar-coated proteins and fats) found on the surface of human and other animal cells. This binding allows for agglutination (clumping) and sometimes can produce an immune response. They can cause agglutination of blood cells and they can bind to the cells that line the small intestine. Nasty business.
The most interesting research I’ve seen in this area came from Alessio Fasano, M.D. and his team. Dr. Fasano is a world-renowned pediatric gastroenterologist, the W. Allan Walker Chair of Pediatrics at Harvard Medical School, Vice Chair of Basic, Translational, and Clinical Research and Division Chief of Pediatric Gastroenterology and Nutrition at the MassGeneral Hospital for Children in Boston and really fun to watch lecture.
He proposes that altering or upregulating (as gluten does) zonulin pathways can cause autoimmune and inflammatory disorders. More interestingly, he thinks that these diseases can be all but reversed by reestablishing the zonulin-dependent tight junctions of the intestine.
Here’s the Abstract from Dr. Fasano’s paper:
The primary functions of the gastrointestinal tract have traditionally been perceived to be limited to the digestion and absorption of nutrients and to electrolytes and water homeostasis. A more attentive analysis of the anatomic and functional arrangement of the gastrointestinal tract, however, suggests that another extremely important function of this organ is its ability to regulate the trafficking of macromolecules between the environment and the host through a barrier mechanism. Together with the gut-associated lymphoid tissue and the neuroendocrine network, the intestinal epithelial barrier, with its intercellular tight junctions, controls the equilibrium between tolerance and immunity to non-self antigens. Zonulin is the only physiological modulator of intercellular tight junctions described so far that is involved in trafficking of macromolecules and, therefore, in tolerance/immune response balance. When the finely tuned zonulin pathway is deregulated in genetically susceptible individuals, both intestinal and extraintestinal autoimmune, inflammatory, and neoplastic disorders can occur. This new paradigm subverts traditional theories underlying the development of these diseases and suggests that these processes can be arrested if the interplay between genes and environmental triggers is prevented by reestablishing the zonulin-dependent intestinal barrier function. This review is timely given the increased interest in the role of a “leaky gut” in the pathogenesis of several pathological conditions targeting both the intestine and extraintestinal organs.
So zonulin is the “key” that opens the tight junctions of the intestine and when the finely tuned zonulin pathway is disrupted, autoimmune, inflammatory, and neoplastic (tumor-related) diseases can occur. The worst part is that once the body mounts a defense against any particular protein that escapes, it becomes trained to react to those proteins every time they appear which can lead to chronic inflammation.
So far, the only triggers that we have found for the zounlin pathways are certain gut bacteria in the small intestine and gluten. Dr. Fasano’s research indicates that gliadin increases zonulin levels in everyone, regardless of celiac status. As zonulin levels rise, the tight junctions of the gut get less and less…tight. This allows bacteria, pathogens, and macromolecules of undigested food to pass directly into the bloodstream.
In conclusion, Dr. Fasano states:
The classical paradigm of inflammatory pathogenesis involving specific genetic makeup and exposure to environmental triggers has been challenged recently by the addition of a third element, the loss of intestinal barrier function. Genetic predisposition, miscommunication between innate and adaptive immunity, exposure to environmental triggers, and loss of intestinal barrier function secondary to the activation of the zonulin pathway by food-derived environmental triggers or changes in gut microbiota all seem to be key ingredients involved in the pathogenesis of inflammation, autoimmunity, and cancer. This new theory implies that once the pathological process is activated, it is not auto-perpetuating. Rather, it can be modulated or even reversed by preventing the continuous interplay between genes and the environment. Since zonulin-dependent TJ dysfunction allows such interactions, new therapeutic strategies aimed at reestablishing the intestinal barrier function by downregulating the zonulin pathway offer innovative and not-yet-explored approaches for the management of these debilitating chronic diseases.
Dr. Fasano’s team has also found evidence that gluten may be responsible for the pathogenesis of all autoimmune disease (not just celiac disease) due to the upregulation of zonulin and the subsequent loosing of tight junctions. It also suggests that this process plays a role in inflammatory diseases such as Chron’s and rheumatoid arthritis.
Check out his piece in Scientific American or read the abstract below:
Little is known about the interaction of gliadin with intestinal epithelial cells and the mechanism(s) through which gliadin crosses the intestinal epithelial barrier. We investigated whether gliadin has any immediate effect on zonulin release and signaling.
MATERIAL AND METHODS:
Both ex vivo human small intestines and intestinal cell monolayers were exposed to gliadin, and zonulin release and changes in paracellular permeability were monitored in the presence and absence of zonulin antagonism. Zonulin binding, cytoskeletal rearrangement, and zonula occludens-1 (ZO-1) redistribution were evaluated by immunofluorescence microscopy. Tight junction occludin and ZO-1 gene expression was evaluated by real-time polymerase chain reaction (PCR).
When exposed to gliadin, zonulin receptor-positive IEC6 and Caco2 cells released zonulin in the cell medium with subsequent zonulin binding to the cell surface, rearrangement of the cell cytoskeleton, loss of occludin-ZO1 protein-protein interaction, and increased monolayer permeability. Pretreatment with the zonulin antagonist FZI/0 blocked these changes without affecting zonulin release. When exposed to luminal gliadin, intestinal biopsies from celiac patients in remission expressed a sustained luminal zonulin release and increase in intestinal permeability that was blocked by FZI/0 pretreatment. Conversely, biopsies from non-celiac patients demonstrated a limited, transient zonulin release which was paralleled by an increase in intestinal permeability that never reached the level of permeability seen in celiac disease (CD) tissues. Chronic gliadin exposure caused down-regulation of both ZO-1 and occludin gene expression.
Based on our results, we concluded that gliadin activates zonulin signaling irrespective of the genetic expression of autoimmunity, leading to increased intestinal permeability to macromolecules.
To summarize, this research indicates that gluten (gliadin) causes an enormous release of zonulin. Zonulin opens the tight junctions of the intestinal epithelial cells and creates the opportunity for systemic inflammation and autoimmune response. Most interestingly, this process does not appear to happen only in those with celiac disease. Gluten is a danger to everyone.
INFLAMMATORY TRIGGER FOODS
All right, that covers gluten and zonulin pretty well. Let’s talk the sneakiest of the bunch: lectins. As I said before, lectins are a class of proteins that bind onto the carbohydrates in our cell walls.
Lectins are present in about 30-40% of the American diet but they are especially concentrated in grains (wheat is the worst), seeds, nuts, legumes (soy is the worst), nightshade plants (potatoes, tomatoes, eggplant, peppers, etc), and dairy. Importantly, lectins are not fully degraded by heat or by digestion, which means they often reach the small intestine more or less intact.
Some ingested lectins will make it through the gut wall by a process called endocytosis, which may allow them access to the blood and lymph system. From here, they may enter the liver, pancreas or other organs. Experts believe that about 5 percent of ingested lectins will enter the bloodstream and, depending on the individuals specific glycoconjugates (what type of sugar is bound to their cell walls), bind to various tissues in the body such as nervous tissue or connective tissue or even the bladder.
Some lectins that we consume in everyday foods can bind to the sugars in the cell walls of the gut or in the blood. This can cause an immune response, leading to inflammation, intestinal damage, altered gut flora, malabsorption, decreased cellular repair, cellular death, and eventually disease.
Now, that’s in HEALTHY GUT. Let’s just think about how much worse it can be in a leaky gut. In a leaky gut situation, more complete lectins can flow directly into the bloodstream and bind to tissues throughout the body potentially causing autoimmune mayhem. As discussed earlier, this could lead to chronic inflammation or disease.
The effect of lectins on those with an established autoimmune disease such as Crohn’s or celiac could be even worse. The epithelial cells of the small intestine are renewing at a faster rate and immature cells are more glycosylated than mature cells making them more susceptible to lectin binding.
Though the area is still being researched, studies have shown that lectins are linked to many autoimmune disorders like Crohn’s, ulcerative colitis, arthritis, celiac disease, and more. The correlation between intestinal lining damage, gut permeability, and chronic autoimmune response is very compelling.
For example, in wheat, gliadin, a component of gluten and an iso-lectin of wheat germ agglutinin (WGA), is capable of activating NF kappa beta proteins which, when up-regulated, are involved in almost every acute and chronic inflammatory disorder including neurodegenerative disease, inflammatory bowel disease, infectious and autoimmune diseases.
There is also good evidence that lectins like WGA can initiate allergic reactions in the gut causing the release of IL-4, IL-13, and histamine from human basophils producing noticeable allergic symptoms. Additionally, WGA has been shown to interfere with protein digestion and increase gut permeability.
Lectins found in peanuts, kidney beans, and soybeans are all capable of attaching to various bodily tissues and having deleterious effects. Of course, it is not as simple as that. Our individual genotype (the genes we have) and phenotype (how those genes are expressed) play a role in how lectins affect any of us. Almost everyone tested so far have antibodies to some dietary lectins in their bloodstream meaning that their immune systems have mounted a defense against those lectins at some point. In fact, many allergists agree that most of what we call food allergies are actually immune responses to the lectins in the foods we eat.
Now, it’s almost impossible to avoid eating lectins because they are in just about every plant and animal to varying degrees (even if you try to avoid them you’ll still end up eating small amounts given their omnipresence in nature). However, lectins are definitely more concentrated in some sources than others.
I said it earlier but it is worth repeating; Here is a list of foods with a high concentration of lectins: All grains (wheat is the worst offender), dairy, nuts, legumes (soy is the worst offender), and nightshade plants (potatoes, tomatoes, eggplant, tamarios, tomatillos, pepinos, pimentos, paprika, cayenne, and peppers of all kinds except black pepper).
BRINGING IT HOME
All of this evidence leads to the conclusion that it is probable that all types of autoimmune diseases, many inflammatory diseases, and possibly neoplastic diseases share a common thread: leaky gut syndrome. That is not to say that leaky gut syndrome is causing these disease, but it does seem to be a necessary condition for them to occur.
Here is a scenario that demonstrates how one can go from a healthy state to a disease state after eating certain foods:
1. First, let’s suppose that you are genetically predisposed (which means you were probably “born with it”) to suffer from certain (or multiple) diseases which are activated by diet.
2. You eat gluten or other foods containing wheat and or lectins (legumes, nightshade vegetables, etc.).
3. You are exposed to a variety of environmental toxins in addition to the naturally occurring compounds found in what you eat.
4. Over time, that exposure causes leaky gut syndrome.
5. Once the gut becomes “leaky”, toxins, bacteria, pathogens, lectins, incompletely digested nutrients, and waste products flow from the gut directly into the bloodstream.
6. This can wreak havoc on the systems of the body (affecting different people in different ways.)
7. The immune system scrambles to deal with these “invaders.”
8. Immune-response damages your own cells in the process of attacking the invaders.
9. Because the invaders are attached to your own cells, the body begins to recognize these cells as bad guys and attacks healthy cells. (That’s why it is called “autoimmune.”)
10. This process is repeated over the course of weeks or years eventually leading to the pathogenesis of an autoimmune disease, chronic inflammatory disease, or neoplastic disorder.
(Please look at our references for this article to gain a deeper understanding of these concepts and theories)
1. Fasano, A. Leaky gut and autoimmune diseases. Clinical Reviews in Allergy & Immunology, Feb;42(1):71-8. doi: 10.1007/s12016-011-8291-x.
2. Fasano, A. Zonulin and Its Regulation of Intestinal Barrier Function: The Biological Door to Inflammation, Autoimmunity, and Cancer. Physiol Rev January 1, 2011 vol. 91 no. 1 151-175
3. Fasano, A. Gliadin, zonulin and gut permeability: Effects on celiac and non-celiac and non-celiac intestinal mucosa and intestinal cell lines. Scandinavian Journal of Gastroenterology, 2006; 41: 408 Á/419
4. Pusztai A, Ewen SW, Grant G, Brown DS, Stewart JC, Peumans WJ, Van Damme EJ, Bardocz S. Antinutritive effects of wheat germ agglutinin and other N-acetylglucosamine-specific lectins. Br J Nutr. 1993 Jul;70(1):313-321.
5. Jones, David S., ed.. Textbook of Functional Medicine. Gig Harbor:The Institute for Functional Medicine, 2005, 303.
6. Watzl B, Neudecker C, Hansch GM, Rechkemmer G, Pool-Zobel BL. Dietary wheat germ agglutinin modulates ovalbumin-induced immune responses in Brown Norway rats. Br J Nutr. 2001 Apr;85(4):483-90.
7. Eur. J. Immunology. 1999. Mar;29(3):918-27.
8. Falth-Magnusson K., et al. Elevated levels of serum antibodies to the lectin wheat germ agglutinin in celiac children lend support to the gluten-lectin theory of celiac disease. Pediatr Allergy Immunol. May 1995; 6(2): 98-102.
9. Hollander D, Vadheim CM, Brettholz E, Pertersen GM, Delahunty T, Rotter JI. Increased intestinal permeability in patients with Crohn’s disease and their relatives. A possible etiologic factor. Ann Intern Med, December 1986; 105(6):883-85.
10. Gut 1999. May; 44(5):709-14
11. J Cell Physiol. 2001 Feb;186(2):282-287.
12. Pusztai A. Dietary lectins are metabolic signals for the gut and modulate immune and hormonal functions. Eur J Clin Nutr. 1993 Oct; 47(10):691-699 ( Pusztai A Rowett Research Institute, Bucksburn, Aberdeen, UK.
Gluten sensitivity plagues a huge number of people around the world and that number is on the rise. Because it so difficult to diagnose, we do not know the exact number but researchers estimate as many as 18 million in America alone. Until recently, the only way for people with gluten sensitivity to find relief was with a gluten-free diet. What does that mean, exactly?
At first, it seems like this would a simple concept: a gluten-free diet is a diet that does not include gluten. While that is true, following a gluten-free diet is a little bit more complicated in practice. Because food companies have been using flour as a filler and binding agent in so many processed foods, there is gluten found in many surprising places. Pasta sauces, salad dressings, hot dogs and sausages, canned soups and some chocolates have all been contaminated with gluten by the food industry. This means that following a gluten-free diet is not as simple as avoiding bread and pasta. You have to learn what sneaky ways that gluten may be listed on an ingredients label (hydrolyzed wheat protein, modified wheat starch, brewer’s yeast), read the label for every food item you purchase, have long conversations with all of the servers you interact with, and interrogate friends and family members at potlucks. Not so simple.
A Better Way
If you suffer from non-celiac gluten sensitivity but don’t want to give up the foods you love there is now a better way to get relief. DigestShield® is a synergistic blend of enzymes, probiotics and more than 200 milligrams of our proprietary prebiotic, chitosan. It breaks down gluten, dairy, carbohydrates, fat and protein plus re-tunes the gut to help you get back to feeling great. If you suffer ANY distress after eating, reach for DigestShield®before you eat. It is the only product on the market that can shield against gluten and other negative influences in our diet such as lectins. If you’re looking for a smart solution for all of your digestive needs, DigestShield® is the answer. Designed by doctors, our proprietary blend of ingredients is safe, effective and GUARANTEED to work.
The history of the gluten-free movement is both interesting and relevant to more and more people every day. Most likely, gluten sensitivity and celiac disease have been with humans ever since our ancestors started eating grains. The first record of the symptoms of celiac disease comes from 100 AD when the Greek physician, Aretaeus the Cappadocian, known as Galen, described the characteristic stool of celiac patients. Anthropologists recently found the bones of a young Roman woman who appears to have died from chronic malnutrition due to celiac disease.
There are “bread-crumbs” to follow from ancient to modern times indicating that people have more or less always suffered from ingestion of gluten. What is less clear is what has happened in the last couple of decades that has increased the prevalence of celiac disease and non-celiac gluten sensitivity. There has been a four-fold increase in the diagnosis of celiac disease between 1990 and 2012 and it is believed that two-thirds of celiac cases go undiagnosed.
It is hard to make statements on the prevalence of non-celiac gluten sensitivity but it is easy to see that it has increased since it was not a recognized condition as recently as 10 years ago. There is, however, evidence to suggest that it may affect as many as 1 in 20 Americans.
Where does this increase come from?
Before we look at the factors that led to this increase, check out this infograph of great moments in the gluten-free movement’s history:
There are many theories and explanations floating around but no consensus. As with most things in this world, the answer lies in the interaction between people and their environment. People are changing their behaviors and their environment is changing faster than ever before. Let’s take a look at these two areas and the factors within them.
More testing being performed
Because celiac disease presents in so many ways, it is not easy to diagnose. Until a few decades ago, it was generally believed that celiac disease only produced a handful of very uniform symptoms: stomach cramping, chronic diarrhea, bloating, and weight loss. In the past 10-15 years, we have learned that celiac disease produces a much wider array of symptoms than previously believed. We now believe that symptoms of celiac disease may also include chronic headaches, malnutrition, arthritis, skin rashes, osteoporosis, infertility, anxiety, depression, and even epilepsy in rare cases. This leads physicians to consider and test for celiac disease more often than they previously would have.
The tests themselves are better as well. In the past, tests relied on multiple intestinal biopsies, which required an individual to eat a gluten-containing diet for several weeks or longer. The tests would not necessarily catch cases of “silent celiac” in which extra-intestinal issues were the main problem. Though we still do not have a standard for testing, the options available to practitioners include genetic tests and a variety of blood and stool biomarkers that are more accurate and less invasive. So the combination of more tests being performed and those tests catching the illness more often may be playing a role in the increased diagnosis of celiac disease. Of course, these factors alone cannot explain the increase in celiac disease and gluten spectrum disorders.
In addition to the people being diagnosed by physicians, there are scores more who “self-diagnose” with gluten issues. “Gluten-free” has become popular so more people are trying it and, while not all of those people really need to avoid gluten, many of them find that they feel better after eliminating wheat from their diet. What may have started out as an experiment based on popularity becomes a real change for the better in many people’s lives.
Of course, our environment plays a big role in our behavior. There is a theory that part of the increase in gluten sensitivity spectrum disorders is due to increased consumption of gluten along with industrialized processing practices. (Wheat is often sprayed with herbicide just prior to harvest to increase yields and to act as a desiccant for drying.)
Speaking of processing, this is another way that we are getting exposed to more gluten than ever before. Because the food industry uses wheat and isolated gluten as filler in many products – things like soups, sauces, dietary supplements, even white pepper – we are often unknowingly consuming more gluten than just what we find in baked goods.
There is an interesting theory that certain types of bacteria that can colonize our gut have an effect on the risk of developing gluten intolerance. This is a perfectly feasible theory as our gut bacteria perform many functions in digestion, immunity, hormone regulation, and even behavior. We do not yet have a complete understanding of all species of gut bacteria and what they are capable of.
What Does the “Gluten-Free” Future Hold?
Though we can not say for certain why there has been such a huge increase in the number of people diagnosed with celiac disease and the number of people feeling the effects of non-celiac gluten sensitivity, we know that a rise in awareness has been a boon to those suffering from gluten issues.
There are more gluten-free products available than ever before for those with celiac disease who must be on an entirely gluten-free diet. Correspondingly, there has been a significant increase in the amount of research being done into celiac disease and non-celiac gluten intolerance. This means that more solutions are being introduced to the market and a greater understanding is developing within the healthcare community.
Because of the way our food supply is currently structured, gluten will remain in our lives for decades to come and “gluten-free” will continue its meteoric rise in public awareness. The smartest thing we can do is to find ways to reduce the risk that not being gluten-free poses to us.
How to Protect Yourself From Gluten
Even if you do not experience acute symptoms, there is good evidence that the gluten in your diet produces an immune response every time you eat it. This means that damage is being done to the lining of your gut on a repeated basis if you are eating wheat. If you are very healthy and lucky, your gut may heal quickly and you may never have a problem from this repeated insult. However, it is just as likely that this continual source of inflammation could lead to the development of more serious problems over time.
To stop this cycle of inflammation, you could try to stop eating gluten-containing foods entirely. There are an ever-increasing number of products on the market that are gluten-free versions of common foods. However, these are usually more expensive and, in our experience, not quite as good as the foods they replace.
A more cost-effective and easier way to heal your gut and protect against gluten is with a combination of enzymes and high-quality probiotics. Certain enzymes such a DPP-IV (Dipeptidyl Peptidase IV) aid in the breakdown of gluten so that your body does not mount an immune response in the small intestine. High quality probiotics will ensure that your gut is populated with the right kind of bacteria to aid in the digestion of gluten-containing products. DigestShield® is our answer to this need.