What to look for in a protein powder?

Hello,

I am wondering if anyone has any suggestions as to what to look for/what makes a good protein powder? Also, if you have any suggestions on specific brands that would be great.

I have used whatever protein powder was on the shelf at the grocery store for awhile now, but I have a feeling that I could probably get better stuff online (and from what I have seen, cheaper as well). I tried going to GNC and looking around, but everything is so expensive, even the same brand as the grocery store was $14 more expensive.

whey isolate is very good. Protein is pretty much all the same, just with different labels and fancy advertising. Honestly A tall glass of milk is the ultimnate protein beverage.
A good sized glass has from 8-11 Grams plus calcium and D Vitamin.

Muscles need to be fed protein through out the day si its not just a one time thing like after workout drink a shake and that it. They need a constant supply throughout your day as well as rest days. Muscles usually take about 3-5 days to fully repair and recover after a good workout,

I love Optimum Nutrition Whey Protein for their cost and flavors.

If you want seriously healthy protein get some from www.jayrobb.com, it costs an arm and a leg though, if you can afford it, you won't be disappointed. Shit tastes amazing.

I've been readin' some damn good things about hemp protein. Gonna try some when my tub of whey expires.

I guess i am almost looking for more of a meal replacement/protein shake combo. I already get protein in my breakfast and lunch, and have been using the powder I have after lifting in the afternoon. I usually mix my shakes with 2% milk (mostly because it adds to the flavor, and the mix I have doesnt mix in water that well.)

I appreciate the input.

Isopure Protein drinks are excellent. There a very pure concentrated form of whey and the flavors are delicious. It comes in a glass bottle. Flavors like tea, lemonade, apple, ect.

MAXAMEYES;435379 said:

I've been readin' some damn good things about hemp protein. Gonna try some when my tub of whey expires.

Click to expand...

Yes! Hemp Protein is amazing! Here's an excerpt from an article regarding the nutritional values of Hemp.

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Even though it’s a plant, hemp is, unexpectedly, a complete protein. It consists of all twenty known amino acids, including those ten that are designated as essential for human health. Just to get our terminology right, a protein is considered complete when it not only contains the ten essential amino acids, but when those amino acids are in the correct quantity and proportion for the body to utilize them. So, in terms of complete protein, hemp is up there with the best.

But, it doesn’t just end there. Hemp also contains the essential fatty acids {EFA's} needed for good health in the perfect balance – that is one of Omega 3 to each three of Omega 6.

And, if that wasn’t enough, the insoluble fiber content of hemp organic protein powder works to keep your blood sugar level stable, as well as ensuring that your bowel movements are regular. If you look on the ingredient label, you’ll see that all the carb content is fiber, making it perfect for a low carb diet.

Source

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This is what I buy mainly these days since I am attempting to make the transition from industrial to completely organic in terms of diet and supplementation. However, it has been very costly because I utilize a body-building diet and the amount of food I take in is greater than your typical vegan/veggie/hipster that makes up the larger part of health food store's consumer base. Why do we have to PAY to be healthy? Seriously, nutriticide is a conspiracy!

http://www.amazon.com/Nutiva-Organi...81ZG/ref=sr_1_1?ie=UTF8&qid=1307198643&sr=8-1

As I mentioned earlier, I have also been a big supporter of Optimum Nutrition Whey, and have used their brand for many years. I just love their flavors, and my body seems to react well with daily supplementation of their products.

I usually buy ON Gold Standard Whey, and in the 2lb buckets, so I can regularly change flavors.

http://www.amazon.com/Optimum-Nutri..._1_cc_2?ie=UTF8&qid=1307199322&sr=1-2-catcorr

Girthtacular;435406 said:

I guess i am almost looking for more of a meal replacement/protein shake combo. I already get protein in my breakfast and lunch, and have been using the powder I have after lifting in the afternoon. I usually mix my shakes with 2% milk (mostly because it adds to the flavor, and the mix I have doesnt mix in water that well.)

I appreciate the input.

Click to expand...

I will always advocate staying away from as many processed supplements, drinks, "pre/post-workout" nutrition as possible. In my experience, most of this stuff is garbage, and has so many extra ingredients that your body doesn't even utilize, or need!

Most importantly, cow's milk is very unhealthy to ingest! I would recommend you make your own delicious carb filled smoothie/shake if you need to use it as a meal replacement. Something else to keep in mind, nothing can replace a real whole foods meal! However, I do understand the need to get calories in, and also find myself being forced into drinking a meal filler shake on occasion due to work or studies.

For a filler-inner-shake I would recommend adding some protein of your choice, 25-40g, and I suppose you will want the calories from Carb's (but I really don't know your diet), so you could go with ground up oats (coffee grinder), or fresh fruit (berries, for phytonutrients, etc.). Also, remember that when you add some raw nut or seed oil to your shake, it will help slow down the digestion and breakdown of your protein powder supplement; they digest rather quickly compared to whole food sources. Inasmuch, you can add other fillers that are relatively healthy for flavor, such as Carob powder.

My favorite home-made PRO/FAT shake is this.
4Tbs Organic Hemp Protein Powder
1Tbs Organic Raw Almond Butter
1Tbs Organic Coconut Butter
1Tbs Carob Powder
1C Almond Milk
Sprinkle of Cinnamon

And for a cum-blaster/horniness shake you can opt for some Maca Powder in there too!

I use Life-Flo brand Maca, and a 16oz jar lasts me a few months. Generally I take 3-6g/day and give myself 1-2 weeks off on occasion.

http://www.bodybuilding.com/store/lifeflo/macagold.html

Anyway, I've probably rambled on for too long already.

Below is some information on Cow's Milk! Yuck! (And of course more info on WHEAT!)

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Brief Article:
http://www.celiac.com/articles/2158...uth-About-Wheat-Dairy-Corn-and-Soy/Page1.html

More in depth:

The proteins in dairy (casein) behave like gluten. So it triggers an autoimmune response and/or mimics endorphins to cause changes in perception, mood, and behavior. It is literally a drug, that is why people are so hooked up with dairy and gluten. But dairy also causes problems in other ways as well, it is reviewed in Detoxification and Healing, but here is the relevant part about gluten and casein:

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Quote from: Sydney Baker

"An average person and most doctors simply cannot believe that difficulty with the digestion and biochemical or immunological processing of the gluten found in these grains can cause substantial mischief.

Gluten intolerance affects approximately one out of a hundred people; if you look among sick people instead of in the general population, you will find a much higher incidence. If you have problems of just about any combination of symptoms you can name or even if you have been diagnosed with a disease and remain symptomatic, a brief avoidance of gluten in your diet will cover this base.

Gluten sensitivity is the protein in cereal grains such as wheat, rye, and barley. Sensitivity is not the same as an ordinary allergy.

Most sensitivity to foods involves delayed reactions and has to do with IgG antibodies. It is very easy to identify food allergies if you get an immediate reaction to them, for example if you get a rash after eating some strawberries. But it is very tricky to pin down a delayed food allergy because there is no clear-cut cause and effect. You may experience symptoms after two hours, but frequently they don’t show up until one day to three days after you eat the food in question. Further complicating matters, the symptoms wax and wane. You may eat gluten with impunity one day but get diarrhea from it the next three times you indulge. Or your symptoms may be cumulative, occurring only after you’ve eaten gluten a number of times or when you eat a particular combination of foods you’re sensitive to.

Delayed food allergies can cause just about any symptom, and chronic illness often involves a state of inappropriate immune vigilance in which food allergy gets involved even if it is no the cause of the problem. For some reason, your defense immune system can get stuck in a high vigilance alert and response, leading to chronic inflammatory symptoms that persist and even worsen long after the initial trigger has gone. When this happens, your immune system may develop an oddly aggressive attitude toward a variety of antigens or foreign substances in your body, including many found in the foods you eat.

Wheat and other gluten-containing foods and milk products may test positive on IgG food allergy testing but that, in you, produce effects that are not really allergic but are mediated by mechanisms that take weeks or months for alleviation after avoiding the foods.

Autistic children often improve enough on a gluten-free [Psyche: and dairy free diet, it is well documented] diet at to make it worth continuing. The diet avoids wheat, rye, barley, and all products containing even traces of the protein (gluten) found in these grains. Oats are still a matter of controversy; some studies show no negative effect in gluten-sensitive individuals, but other individuals report reactions to them. The majority of psychologists, physicians, teachers, neighbors, and parents reject the idea that anything as completely innocent as bread or spaghetti could make your lose your mind. More practitioners every day prescribe a gluten free diet for individuals with diseases such as schizophrenia and autism as top treatment instead of it being it a last resort. If you have any chronic symptom and you have not tried eliminating gluten from your diet for somewhere between three weeks and three months to see what different it may make.

Doctors are conditioned to think that each disease has a separate cause, and each produces a separate disease, so it is no surprise that they will find it difficult to believe that sensitivity to the protein wheat, rye, barley, and maybe, oats could produce such a diverse list of conditions such as headaches, fatigue, malaise, depression, any sort of chronic digestive problem including difficulty gaining weight, abdominal pain, diarrhea, constipation, irritable bowel, undigested food in stools, Sjögren’s syndrome (dry eyes), epilepsy associated with brain calcification, history of migraine headaches, or digestive problems; osteoporosis, infertility, complications of pregnancy such as miscarriage, low-birth-weight infants, intestinal lymphoma, esophageal cancer, diabetes, thyroid problems, schizophrenia, autism, dermatitis herpetiformis (a chronic skin condition with tiny blisters that resemble those of herpes virus infections).

There is substantial evidence of a causative association between gluten intolerance and these problems. And the list grows as case reports of dramatic cures produced by a gluten-free diet attract the attention of researchers.

There are blood tests and urine tests that may predict whether you will feel better by eliminating gluten from your diet, but no blood or urine test is completely decisive. Response to a change in diet will be decisive for you.

The original peoples of Northern Europe, who like the peoples of the Americas, Africa, and the Far East, had not adapted to the consumption of wheat because they were hunter-gatherers or because they practiced agriculture based on corn, millet, or rice, as well as tubers.

In order to understand gluten sensitivity, we must understand digestion of protein. A protein is an assembly of amino acids. Amino acids joined together are called peptides and when we have 100 or so amino acids joined together, we have a small protein. Most proteins have hundreds or thousands of amino acids, and they are folded into shapes that are kept permanent by bridges, usually made of sulfur. The strength of this assembly is quite strong, and so our digestive tracts are trusted with the task of disassembling the thousands of amino acids from our foods right down to individual amino acids, which then pass int our bloodstream to be then reassembled int our own very proteins. To be more precise, our digestive tracts uses stomach acids, and alkali juices from our intestines, combined with the digestive enzymes to do this job. Specific enzymes disassemble the proteins into peptides. Gluten intolerance has to do with a failure of a particular enzyme, a peptidase called DPP4.

When the same enzyme is sticking out of a lymphocyte, a cell of our immune/defense system and apparently doing a different job within the body, it is called CD26. Because of the failure or insufficiency of DPP4, an undigested fragment of protein, or peptide, survives and it appears to cause mischief in at least two ways. First, this undigested peptide, looks familiar to the immune/defense system, in other words, it produces a mimicry which is based on digestive weakness among the descendants of peoples who have not been eating wheat long enough to adapt. This will cause symptoms caused by the triggering of an immune response against a suspicious-looking peptide which will resemble a virus to our defense/immune system. Because the gluten-derived peptide is similar to various disease-causing virus, it generates a complex defensive response on the part of the immune system, which does not then find a virus to kill. The next step is damage to tissues by the antibodies aimed at the peptide. This triangle of viral stimulus, immune response, and autoimmune damage is suspected to be a common theme in various illnesses, such as type I diabetes, multiple sclerosis, and autism. The immune response damages different tissues in different people.

The second way that undigested peptides from gluten cause trouble is by entering the bloodstream. Peptides released from gluten when there is a failure of DPP4 possess another kind of mimicry apart from their resemblance to peptides from viruses. These peptides look like opium and the family of drugs derived from opium: heroin, morphine, codeine, and other semisynthetic derivatives. This understanding is based on the finding of opioid peptides in the urine of individuals with autism and schizophrenia, also from the dramatic withdrawal symptoms that occur in some individuals when they come off gluten. The malaise and irritability strongly resemble a mild version of the kinds of symptoms seen in heroin withdrawal.

Most individuals with gluten-related symptoms will begin to experience relief a few days after excluding all gluten. It may take up between 3 weeks and 3 months.

Many doctors define the problem in terms of the lab test, the lab tests are meant to indicate celiac disease, which does not necessarily have a one-to-one correlation with all of the other problems associated with gluten sensitivity. Celiac disease is just one type of a broader spectrum of gluten sensitivity.

Everything that we had learned about gluten applies to casein, one of the main proteins in milk, the lack of DPP4, thus the peptides pass into the blood where they do harm because the evoke an autoimmune response and/or mimic endorphins to cause changes in perception, mood, and behavior.; but it is to say that milk can cause you problems in other ways as well."

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The lack of these enzymes (peptidase) is not only due to heritability, but it is also due to multiple factors including toxicity (for instance, heavy metal toxicity) which ends up impairing their function. Also, for a more thorough review on gluten, see Sayer Ji's articles here:

Source

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Opening Pandora's Bread Box: The Critical Role of Wheat Lectin in Human Disease

Sayer Ji
GreenMedInfo.com
Sun, 21 Mar 2010 02:39 CD

Now that celiac disease has been allowed official entry into the pantheon of established medical conditions, and gluten intolerance is no longer entirely a fringe medical concept, the time has come to draw attention to the powerful little chemical in wheat known as 'wheat germ agglutinin' (WGA) which is largely responsible for many of wheat's pervasive, and difficult to diagnose, ill effects. Not only does WGA throw a monkey wrench into our assumptions about the primary causes of wheat intolerance, but due to the fact that WGA is found in highest concentrations in "whole wheat," including its supposedly superior sprouted form, it also pulls the rug out from under one of the health food industry's favorite poster children.

Below the radar of conventional serological testing for antibodies against the various gluten proteins and genetic testing for disease susceptibility, the WGA "lectin problem" remains almost entirely obscured. Lectins, though found in all grains, seeds, legumes, dairy and our beloved nightshades: the tomato and potato, are rarely discussed in connection with health or illness, even when their presence in our diet may greatly reduce both the quality and length of our lives.

Although significant progress has been made in exposing the dark side of wheat over the past decade, gluten receives a disproportionate share of the attention. Given that modern bread wheat (Triticum Aestivum) is a hexaploid species containing three distinct sets of chromosomes capable of producing well over 23,000 unique proteins, it is not surprising that we are only now beginning to unravel the complexities of this plant's many secrets.1 What is unique about the WGA glycoprotein is that it can do direct damage to the majority of tissues in the human body without requiring a specific set of genetic susceptibilities and/or immune-mediated articulations. This may explain why chronic inflammatory and degenerative conditions are endemic to wheat-consuming populations even when overt allergies or intolerances to wheat gluten appear exceedingly rare. The future fate of wheat consumption, and by implication our health, may depend largely on whether or not the toxic qualities of WGA come to light in the general population.

Nature engineers, within all species, a set of defenses against predation, though not all are as obvious as the thorns on a rose or the horns on a rhinoceros. Plants do not have the cell-mediated immunity of higher life forms, like ants, nor do they have the antibody driven, secondary immune systems of vertebrates with jaws. They must rely on a much simpler, innate immunity. It is for this reason that seeds of the grass family, e.g. rice, wheat, spelt, rye, have exceptionally high levels of defensive glycoproteins known as lectins. Cooking, sprouting, fermentation and digestion are the traditional ways in which man, for instance, deals with the various anti-nutrients found within this family of plants, but lectins are, by design, particularly resistant to degradation through a wide range of pH and temperatures.

WGA lectin is an exceptionally tough adversary as it is formed by the same disulfide bonds that make vulcanized rubber and human hair so strong, flexible and durable. Like man-made pesticides, lectins are extremely small, resistant to break-down by living systems, and tend to accumulate and become incorporated into tissues where they interfere with normal biological processes. Indeed, WGA lectin is so powerful as an insecticide that biotech firms have used recombinant DNA technology to create genetically modified WGA-enhanced plants. We can only hope that these virtually unregulated biotech companies, who are in the business of playing God with the genetic infrastructure of Life, will realize the potential harm to humans that such genetic modifications can cause.

Lectins are glycoproteins, and through thousands of years of selectively breeding wheat for increasingly larger quantities of protein, the concentration of WGA lectin has increased proportionately. This, no doubt, has contributed to wheat's global dominance as one of the world's favored monocultures, offering additional "built-in" pest resistance. The word lectin comes from the same etymological root as the word select, and literally means "to choose." Lectins are designed "to choose" specific carbohydrates that project off the surface of cells and upon which they attach. In the case of WGA the two glycoproteins it selects for, in order of greatest affinity, are N-Acetyl Glucosamine and N-Acetylneuraminic acid (sialic acid).

WGA is Nature's ingenious solution for protecting the wheat plant from the entire gamut of its natural enemies. Fungi have cell walls composed of a polymer of N-Acetylglucosamine. The cellular walls of bacteria are made from a layered structure called the peptidoglycan, a biopolymer of N-Acetylglucosamine. N-acetylglucosamine is the basic unit of the biopolymer chitin, which forms the outer coverings of insects and crustaceans (shrimp, crab, etc.). All animals, including worms, fish, birds and humans, use N-Acetyglucosamine as a foundational substance for building the various tissues in their bodies, including the bones. The production of cartilage, tendons, and joints depend on the structural integrity of N-Acetylglucosamine. The mucous known as the glycocalyx, or literally, "sugar coat" is secreted in humans by the epithelial cells which line all the mucous membranes, from nasal cavities to the top to the bottom of the alimentary tube, as well as the protective and slippery lining of our blood vessels. The glycocalyx is composed largely of N-Acetylglucosamine and N-Acetylneuraminic acid (also known as sialic acid), with carbohydrate end of N-Acetylneuraminic acid of this protective glycoprotein forming the terminal sugar that is exposed to the contents of both the gut and the arterial lumen (opening). WGA's unique binding specificity to these exact two glycoproteins is not accidental. Nature has designed WGA perfectly to attach to, disrupt, and gain entry through these mucosal surfaces.

It may strike some readers as highly suspect that wheat - the "staff of life" - which has garnered a reputation for "wholesome goodness" the world over, could contain a powerful health-disrupting anti-nutrient, which is only now coming to public attention. WGA has been overshadowed by the other proteins in wheat. Humans - not Nature - have spent thousands of years cultivating and selecting for larger and larger quantities of these proteins. These pharmacologically active, opiate-like proteins in gluten are known as gluten exorphins (A5, B4, B5, C) and gliadorphins. They may effectively anesthetize us, in the short term, to the long term, adverse effects of WGA. Gluten also contains exceptionally high levels of the excitotoxic l-aspartic and l-glutamic amino acids, which can also be highly addictive, not unlike their synthetic shadow molecules aspartame and monosodium glutamate.1In a previous article on the topic,The Dark Side of Wheat: New Perspectives on Celiac Disease and Wheat Intolerance2, we explored the role that these psychotropic qualities in grains played in ushering in civilization at the advent of the Neolithic transition 10,000 BC. No doubt the narcotic properties of wheat are the primary reason why suspicions about its toxicity have remained merely speculation for thousands upon thousands of years.

WGA is most concentrated in the seed of the wheat plant, likely due to the fact that the seeds are the "babies" of these plants and are invested with the entire hope for continuance of their species. Protecting the seed against predation is necessarily a first priority.WGA is an exceedingly small glycoprotein (36 kilodaltons) and is concentrated deep within the embryo of the wheat berry (approximately 1 microgram per grain). WGA migrates during germination to the roots and tips of leaves, as the developing plant begins to project itself into the world and outside the safety of its seed. In its quest for nourisHydromaxent from the soil, its roots are challenged with fungi and bacteria that seek to invade the plant. In its quest for sunlight and other nourisHydromaxent from the heavens the plant's leaves become prey to insects, birds, mammals, etc. Even after the plant has developed beyond the germination and sprouting stages it contains almost 50% of the levels of lectin found in the dry seeds. Approximately one third of this WGA is in the roots and two thirds is in the shoot, for at least 34 days.3

Each grain contains about 1 microgram of WGA. That seems hardly enough to do any harm to animals our size. Lectins, however, are notoriously dangerous even in minute doses and can be fatal when inhaled or injected directly into the bloodstream. According to the U.S. Centers for Disease Control it takes only 500 micrograms (about half a grain of sand) of ricin (a lectin extracted from castor bean casings) to kill a human. A single, one ounce slice of wheat bread contains approximately 500 micrograms of WGA, which if it were refined to its pure form and injected directly into the blood, could, in theory, have platelet aggregating and erythrocyte agglutinizing effects strong enough to create an obstructive clot such as occurs in myocardial infarction and stroke. This, however, is not a likely route of exposure and in reality the immediate pathologies associated with lectins like ricin and WGA are largely restricted to the gastrointestinal tract where they cause mucosal injuries. The point is that WGA, even in small quantities, could have profoundly adverse effects, given suitable conditions. Ironically, WGA is exceptionally small, at 36 kilodaltons (approximately the mass of 36,000 hydrogen atoms) and it can pass through the cell membranes of the intestine with ease. The intestines will allow passage of molecules up to 1,000 kilodaltons in size. Moreover, one wheat kernel contains 16.7 trillion individual molecules of WGA, with each molecule of WGA having four N-Acetylglucosamine binding sites. The disruptive and damaging effects of whole wheat bread consumption are formidable in someone whose protective mucosal barrier has been compromised by something as simple as Non-Steroidal Anti-Inflammatory Drug (NSAID) use, or a recent viral or bacterial infection. The common consumption of both wheat and NSAIDs may suggest the frequency of the WGA vicious cycle. Anti-inflammatory medications, such as ibuprofen and aspirin, increase intestinal permeabilty and may cause absorption of even larger than normal quantities of pro-inflammatory WGA. Conversely, the inflammation caused by the absorption of WGA lectin is the very reason there is a great need for the inflammation-reducing effects of NSAIDs.

One way to gauge just how pervasive the adverse effects of WGA are among wheat-consuming populations is the popularity of the dietary supplement glucosamine.In the USA, a quarter billion dollars' worthof the glucosamine is sold annually.The main source of glucosamine on the market is from the N-Acetylglucosamine rich chitin exoskelotons of crustaceans, like shrimp and crab. Glucosamine is used for reducing pain and inflammation. We do not have a dietary deficiency of the pulverized shells of dead sea critters, just as our use of NSAIDs is not caused by a deficiency of these synthetic chemicals in our diet. When we consume glucosamine supplements, the WGA, instead of binding to our tissues, binds to the pulverized chitin in the glucosamine supplements, sparing us from the full impact of WGA. Many millions of Americans who have greatly reduced their pain and suffering by ingesting glucosamine and NSAIDs may be better served by removing wheat, the underlying cause of their malaise, from their diets. This would result in even greater relief from pain and inflammation along with far less dependency on palliative supplements and medicines alike.

To further underscore this point, the following are several ways that WGA depletes our health while glucosamine works against it:

WGA may be Pro-inflammatory

At exceedingly small concentrations (nanomolar) WGA stimulates the synthesis of pro-inflammatory chemical messengers (cytokines) including Interleukin 1, Interleukin 6 and Interleukin 8 in intestinal and immune cells.4 WGA has been shown to induce NADPH-Oxidase in human neutrophils associated with the "respiratory burst" that results in the release of inflammatory free radicals called reactive oxygen species5 WGA has been shown to play a causative role in patients with chronic thin gut inflammation.6

WGA may be Immunotoxic

WGA induces thymus atrophy in rats7and may directly bind to, and activate, leukocytes.8 Anti-WGA antibodies in human sera have been shown to cross-react with other proteins, indicating that they may contribute to autoimmunity.9 Indeed, WGA appears to play a role in the pathogenesis of celiac disease (CD) that is entirely distinct from that of gluten, due to significantly higher levels of IgG and IgA antibodies against WGA found in patients with CD, when compared with patients with other intestinal disorders. These antibodies have also shown not to cross-react with gluten antigens.10,11

WGA may be Neurotoxic

WGA can pass through the blood brain barrier (BBB) through a process called "adsorptive endocytosis"12 and is able to travel freely among the tissues of the brain which is why it is used as a marker for tracing neural circuits.13 WGA's ability to pass through the BBB, pulling bound substances with it, has piqued the interest of pharmaceutical developers who are looking to find ways of delivering drugs to the brain. WGA has a unique binding affinity for N-Acetylneuraminic acid, a crucial component of neuronal membranes found in the brain, such as gangliosides which have diverse roles such as cell-to-cell contact, ion conductance, as receptors, and whose dysfunction has been implicated in neurodegenerative disorders. WGA may attach to the protective coating on the nerves known as the myelin sheath14 and is capable of inhibiting nerve growth factor15 which is important for the growth, maintenance, and survival of certain target neurons. WGA binds to N-Acetylglucosamine which is believed to function as an atypical neurotransmitter functioning in nocioceptive (pain) pathways.

WGA may be Cytotoxic

WGA has been demonstrated to be cytotoxic to both normal and cancerous cell lines, capable of inducing either cell cycle arrest or programmed cell death (apoptosis).16

WGA may interfere with Gene Expression

WGA demonstrates both mitogenic and anti-mitogenic17 activities. WGA may prevent DNA replication18 WGA binds to polysialic acid (involved in post translational modifications) and blocks chick tail bud development in embryogenesis, indicating that it may influence both genetic and epigenetic factors.

WGA may disrupt Endocrine Function

WGA has also been shown to have an insulin-mimetic action, potentially contributing to weight gain and insulin resistance.19 WGA has been implicated in obesity and "leptin resistance" by blocking the receptor in the hypothalamus for the appetite satiating hormone leptin. WGA stimulates epidermal growth factor which when upregulated is associated with increased risk of cancer. WGA has a particular affinity for thyroid tissue and has been shown to bind to both benign and malignant thyroid nodules.20 WGA interferes with the production of secretin from the pancreas, which can interfere with digestion and can cause pancreatic hypertrophy. WGA attaches to sperm and ovary cells, indicating it may adversely influence fertility.

WGA may be Cardiotoxic

WGA induces platelet activation and aggregration. 21 WGA has a potent, disruptive effect on platelet endothelial cell adhesion molecule-1, which plays a key role in tissue regeneration and safely removing neutrophils from our blood vessels.22

WGA may adversely effect Gastrointestinal Function

WGA causes increased shedding of the intestinal brush border membrane, reduction in surface area, acceleration of cell losses and shortening of villi, via binding to the surface of the villi. WGA can mimic the effects of epidermal growth factor (EGF) at the cellular level, indicating that the crypt hyperplasia seen in celiac disease may be due to the growth-promoting effects of WGA. WGA causes cytoskeleton degradation in intestinal cells, contributing to cell death and increased turnover. WGA decreases levels of heat shock proteins in gut epithelial cells leaving these cells less well protected against the potentially harmful content of the gut lumen.23

WGA may share pathogenic similarities with certain Viruses

There are a number of interesting similarities between WGA lectin and viruses.Both viral particles and WGA lectin are several orders of magnitude smaller than the cells they enter, and subsequent to their attachment to the cell membrane, are taken into the cell through a process of endocytosis.Both influenza and WGA gain entry through the sialic acid coatings of our mucous membranes (glycocalyx) each with a sialic acid specific substance, the neuriminidase enzyme for viruses andthesialic acid binding sites on the WGA lectin.Once the influenza virus and WGAlectin have made their way into wider circulation in the host body they are both capable of blurring the line in the host between self-and non-self.Influenza accomplishes this by incorporating itself into the genetic material of our cells and taking over the protein production machinery to make copies of itself, with the result that our immune system must attack its own virally transformed cell, in order to clear the infection.Studies done with herpes simplex virus have shown that WGA has the capacity to block viral infectivity through competitively binding to the same cell surface receptors, indicating that they may effect cells through very similar pathways.WGA has the capability of influencing the gene expression of certain cells, e.g. mitogenic/anti-mitogenic action,and like other lectins associated with autoimmunity, e.g. soy lectin,and viruses like Epstein-Barr Virus,WGA may be capable of causing certain cells to exhibit class 2 human leukocyte antigens (HLA-II), which mark them for autoimmune destruction by white blood cells.Since human antibodies to WGA have been shown to cross react with other proteins, even if WGA does not directly transform the phenotype of our cells into "other," the resulting cross-reactivity of antibodies to WGA with our own cells would result in autoimmunity nonetheless.

Given the multitude of ways in which WGA may disrupt our health, gain easy entry through our intestine into systemic circulation, and remain refractory to traditional antibody-based clinical diagnoses, it is altogether possible that the consumption of wheat is detracting from the general health of the wheat-consuming world and that we have been, for all these years, "digging our graves with our teeth."This perspective may come as a great surprise to the health food industry whose particular love affair for whole wheat products has begun to go mass market. The increasingly hyped-up marketing of"whole wheat," "sprouted grain," and "wheat germ" enriched products, all of which may have considerably higher levels of WGA than their processed, fractionized, non-germinated and supposedly "less healthy" equivalents,may contribute to making us all significantly less healthy.

It is my belief that a careful study of the wheat plant will reveal that, despite claims to the contrary, man does not have dominion over nature. All that he deems fit for his consumption may not be his inborn right. Though the wheat plant's apparently defenseless disposition would seem to make it suitable for mass human consumption, it has been imbued with a multitude of invisible"thorns," with WGA being its smallest and perhaps most potent defense against predation. While WGA may be an uninvited guest at our table, wheat is equally inhospitable to us. Perhaps the courteous thing to do, having realized our mistaken intrusion, is to lick our wounds and simply go our separate ways. Perhaps as the distance between man and his infatuation with wheat grows, he will grow closer to himself and will discover far more suitable forms of nourisHydromaxent that Nature has not impregnated with such high levels of addictive and potentially debilitating proteins.

Notes

1 Desmond S. T. Nicholl, An Introduction to Genetic Engineering,3rd Edition ISBN-13: 9780521615211
2 Ji, Sayer "The Dark Side of Wheat - New Perspectives on Celiac Disease & Wheat Intolerance." Winter, 08', Journal of Gluten Sensitivity
3 Distribution of Wheat Germ Agglutinin in Young Wheat Plants. Plant Physiol. 1980 Nov;66(5):950-955. PMID:16661559
4 Effects of wheat germ agglutinin on human gastrointestinal epithelium: insights from an experimental model of immune/epithelial cell interaction.Toxicol and Applied Pharmacology 2009 Jun 1;237(2):146-53. Epub 2009 Mar 28. PMID 19332085
5 Wheat germ agglutinin induces NADPH-oxidase activity in human neutrophils by interaction with mobilizable receptors. Infection and Immunity.1999 Jul;67(7):3461-8. PMID 10377127
6 Lectin glycosylation as a marker of thin gut inflammation. The FASEB Journal. 2008;22:898.3
7 Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins.The British Journal of Nutrition 1993 Jul;70(1):313-21. PMID: 8399111
8 Lectinlike properties of pertussis toxin. Infection and Immunity1989 Jun;57(6):1854-7.PMID:2722243
9 Natural human antibodies to dietary lectins. FEBS Lett.1996 Nov 18;397(2-3):139-42. PMID: 8955334
10 Antibodies to wheat germ agglutinin in coeliac disease. Clin Exp Immunol. 1986 January; 63(1): 95 - 100. PMID: 3754186
11 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. 1995 May;6(2):98-102. PMID: 7581728
12 Transcytotic pathway for blood-borne protein through the blood-brain barrier. Proceedings from the National Academy of Sciences U S A. 1988 Jan;85(2):632-6. PMID:2448779
13 Transsynaptic transport of wheat germ agglutinin expressed in a subset of type II taste cells of transgenic mice. BathmateC Neuroscience. 2008 Oct 2;9:96. PMID: 18831764
14 Distribution of concanavalin A and wheat germ agglutinin binding sites in the rat peripheral nerve fibres revealed by lectin/glycoprotein-gold histochemistry. The Histochem Journal.1996 Jan;28(1):7-12.PMID:8866643
15 Wheat germ agglutinin, concanavalin A, and lens culinalis agglutinin block the inhibitory effect of nerve growth factor on cell-free phosphorylation of Nsp100 in PC12h cells. Cell Struct and Function 1989 Feb;14(1):87-93. PMID:2720800
16 Wheat germ lectin induces G2/M arrest in mouse L929 fibroblasts. J Cell Biochem.2004 Apr 15;91(6):1159-73.PMID:15048871
17 Wheat germ agglutinin and concanavalin A inhibit the response of human fibroblasts to peptide growth factors by a post-receptor mechanism. J Cell Physiol. 1985 Sep;124(3):474-80. PMID:2995421
18 DNA replication in cell-free extracts from Xenopus eggs is prevented by disrupting nuclear envelope function. J Cell Sci. 1992 Jan;101 ( Pt 1):43-53.PMID:1569128
19 Effects of wheat germ agglutinin and concanavalin A on the accumulation of glycosaminoglycans in pericellular matrix of human dermal fibroblasts. A comparison with insulin. Acta Biochim Pol. 2001;48(2):563-72. PMID:11732625
20 Analysis of lectin binding in benign and malignant thyroid nodules. Arch Pathol Lab Med.1989 Feb;113(2):186-9. PMID:2916907
21 Further characterization of wheat germ agglutinin interaction with human platelets: exposure of fibrinogen receptors.Thromb Haemost.1986 Dec 15;56(3):323-7.PMID:3105108
22 Wheat germ agglutinin-induced platelet activation via platelet endothelial cell adhesion molecule-1: involvement of rapid phospholipase C gamma 2 activation by Src family kinases. Biochemistry. 2001 Oct 30;40(43):12992-3001.PMID:11669637
23 Decreased levels of heat shock proteins in gut epithelial cells after exposure to plant lectins. Gut. 2000 May;46(5):679-87.PMID:10764712

Source

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The Dark Side of Wheat - New Perspectives on Celiac Disease and Wheat Intolerance

Sayer Ji
GreenMedInfo.com
Sat, 20 Mar 2010 15:29 CDT

The globe-spanning presence of wheat and its exalted status among secular and sacred institutions alike differentiates this food from all others presently enjoyed by humans. Yet the unparalleled rise of wheat as the very catalyst for the emergence of ancient civilization has not occurred without a great price. While wheat was the engine of civilization's expansion and was glorified as a "necessary food," both in the physical (staff of life) and spiritual sense (the body of Christ), those suffering from celiac disease are living testimony to the lesser known dark side of wheat. A study of celiac disease may help unlock the mystery of why modern man, who dines daily at the table of wheat, is the sickest animal yet to have arisen on this strange planet of ours.

The Celiac Iceberg

Celiac disease (CD) was once considered an extremely rare affliction, limited to individuals of European origin. Today, however, a growing number of studies1 indicate that celiac disease is found throughout the US at a rate of up to 1 in every 133 persons, which is several orders of magnitude higher than previously estimated.

These findings have led researchers to visualize CD as an iceberg2. The tip of the iceberg represents the relatively small number of the world's population whose gross presentation of clinical symptoms often leads to the diagnosis of celiac disease. This is the classical case of CD characterized by gastrointestinal symptoms, malabsorption and malnourisHydromaxent. It is confirmed with the "gold standard" of an intestinal biopsy. The suBathmateerged middle portion of the iceberg is largely invisible to classical clinical diagnosis, but not to modern serological screening methods in the form of antibody testing3. This middle portion is composed of asymptomatic and latent celiac disease as well as "out of the intestine" varieties of wheat intolerance. Finally, at the base of this massive iceberg sits approximately 20-30% of the world's population - those who have been found to carry the HLA-DQ locus of genetic susceptibility to celiac disease on chromosome 6.4

The "Celiac Iceberg" may not simply illustrate the problems and issues associated with diagnosis and disease prevalence, but may represent the need for a paradigm shift in how we view both CD and wheat consumption among non-CD populations.

First let us address the traditional view of CD as a rare, but clinically distinct species of genetically-determined disease, which I believe is now running itself aground upon the emerging, post-Genomic perspective, whose implications for understanding and treating disease are Titanic in proportion.

It is not the genes, but what we expose them to

Despite common misconceptions, monogenic diseases, or diseases that result from errors in the nucleotide sequence of a single gene are exceedingly rare. Perhaps only 1% of all diseases fall within this category, and Celiac disease is not one of them. In fact, following the completion of the Human Genome Project (HGP) in 2003 it is no longer accurate to say that our genes "cause" disease, any more than it is accurate to say that DNA is sufficient to account for all the proteins in our body. Despite initial expectations, the HGP revealed that there are only 30,000-35,000 genes in human DNA (genome), rather than the 100,000 + believed necessary to encode the 100,000 + proteins found in the human body (proteome).

The "blueprint" model of genetics: one gene → one protein → one cellular behavior, which was once the holy grail of biology, has now been supplanted by a model of the cell where epigenetic factors (literally: "beyond the control of the gene") are primary in determining how DNA will be interpreted, translated and expressed. A single gene can be used by the cell to express a multitude of proteins and it is not the DNA itself that determines how or what genes will be expressed. Rather, we must look to the epigenetic factors to understand what makes a liver cell different from a skin cell or brain cell. All of these cells share the exact same 3 billion base pairs that make up our DNA code, but it is the epigenetic factors, e.g. regulatory proteins and post-translational modifications, that make the determination as to which genes to turn on and which to silence, resulting in each cell's unique phenotype. Moreover, epigenetic factors are directly and indirectly influenced by the presence or absence of key nutrients in the diet, as well as exposures to chemicals, pathogens and other environmental influences.

In a nutshell, what we eat and what we are exposed to in our environment directly affects our DNA and its expression.

Within the scope of this new perspective even classical monogenic diseases like Cystic Fibrosis (CF) can be viewed in a new, more promising light. In CF many of the adverse changes that result from the defective expression of the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) gene may be preventable or reversible, owing to the fact that the misfolding of the CFTR gene product has been shown to undergo partial or full correction (in the rodent model) when exposed to phytochemicals found in turmeric, cayenne, and soybean.5 Moreover, nutritional deficiencies of seleniun, zinc, riboflavin, vitamin e, etc. in the womb or early in life, may "trigger" the faulty expression or folding patterns of the CFTR gene in Cystic Fibrosis which might otherwise have avoided epigenetic activation.6 This would explain why it is possible to live into one's late seventies with this condition, as was the case for Katherine Shores (1925-2004). The implications of these findings are rather extraordinary: epigenetic and not genetic factors are primary in determining disease outcome. Even if we exclude the possibility of reversing certain monogenic diseases, the basic lesson from the post-Genomic era is that we can't blame our DNA for causing disease. Rather, it may have more to do with what we choose to expose our DNA to.

Celiac disease revisited

What all of this means for CD is that the genetic susceptibility locus, HLA DQ, does not determine the exact clinical outcome of the disease.7 Instead of being the cause, if the HLA genes are activated, they are a consequence of the disease process.8 Thus, we may need to shift our epidemiological focus from viewing this as a classical "disease" involving a passive subject controlled by aberrant genes, to viewing it as an expression of a natural, protective response to the ingestion of something that the human body was not designed to consume.9

If we view celiac disease not as an unhealthy response to a healthy food, but as a healthy response to an unhealthy food, classical CD symptoms like diarrhea may make more sense. Diarrhea can be the body's way to reduce the duration of exposure to a toxin or pathogen, and villous atrophy can be the body's way of preventing the absorption and hence, the systemic effects of chronic exposure to wheat.

I believe we would be better served by viewing the symptoms of CD as expressions of bodily intelligence rather than deviance. We must shift the focus back to the disease trigger, which is wheat itself.

People with celiac may actually have an advantage over the apparently unafflicted because those who are "non-symptomatic" and whose wheat intolerance goes undiagnosed or misdiagnosed because they lack the classical symptoms and may suffer in ways that are equally or more damaging, but expressed more subtly, or in distant organs. Within this view celiac disease would be redefined as a protective (healthy?) response to exposure to an inappropriate substance, whereas "asymptomatic" ingestion of the grain with its concomitant "out of the intestine" and mostly silent symptoms, would be considered the unhealthy response insofar as it does not signal in an obvious and acute manner that there is a problem with consuming wheat.

It is possible that celiac disease represents both an extreme reaction to a global, species-specific intolerance to wheat that we all share in varying degrees. CD symptoms may reflect the body's innate intelligence when faced with the consumption of a substance that is inherently toxic. Let me illustrate this point using Wheat Germ Agglutinin (WGA), as an example.

WGA is glycoprotein classified as a lectin and is known to play a key role in kidney pathologies, such as IgA nephropathy. In the article: "Do dietary lectins cause disease?" the Allergist David L J Freed points out that WGA binds to "glomerular capillary walls, mesangial cells and tubules of human kidney and (in rodents) binds IgA and induces IgA mesangial deposits," indicating that wheat consumption may lead to kidney damage in susceptible individuals.10 Indeed, a study from the Mario Negri Institute for Pharmacological Research in Milan Italy published in 2007 in the International Journal of Cancer looked at bread consumption and the risk of kidney cancer. They found that those who consumed the most bread had a 94% higher risk of developing kidney cancer compared to those who consumed the least bread.11 Given the inherently toxic effect that WGA may have on kidney function, it is possible that in certain genetically predisposed individuals (e.g. HLA-DQ2/DQ8) the body - in its innate intelligence - makes an executive decision: either continue to allow damage to the kidneys (or possibly other organs) until kidney failure and rapid death result, or launch an autoimmune attack on the villi to prevent the absorption of the offending substance which results in a prolonged though relatively malnourished life. This is the explanation typically given for the body's reflexive formation of mucous following exposure to certain highly allergenic or potentially toxic foods, e.g. dairy products, sugar, etc? The mucous coats the offending substance, preventing its absorption and facilitating safe elimination via the gastrointestinal tract. From this perspective the HLA-DQ locus of disease susceptibility in the celiac is not simply activated but utilized as a defensive adaptation to continual exposure to a harmful substance. In those who do not have the HLA-DQ locus, an autoimmune destruction of the villi will not occur as rapidly, and exposure to the universally toxic effects of WGA will likely go unabated until silent damage to distant organs leads to the diagnosis of a disease that is apparently unrelated to wheat consumption.

Loss of kidney function may only be the "tip of the iceberg," when it comes to the possible adverse effects that wheat proteins and wheat lectin can generate in the body. If kidney cancer is a likely possibility, then other cancers may eventually be linked to wheat consumption as well. This correlation would fly in the face of globally sanctioned and reified assumptions about the inherent benefits of wheat consumption. It would require that we suspend cultural, socio-economic, political and even religious assumptions about its inherent benefits. In many ways, the reassessment of the value of wheat as a food requires a William Boroughs-like moment of shocking clarity when we perceive "in a frozen moment....what is on the end of every fork." Let's take a closer look at what is on the end of our forks.

Our biologically inappropriate diet

In a previous article12, I discussed the role that wheat plays as an industrial adhesive (e.g. paints, paper mache', and book binding-glue) in order to illustrate the point that it may not be such a good thing for us to eat. The problem is implicit in the word gluten, which literally means "glue" in Latin and in words like pastry and pasta, which derives from wheatpaste, the original concoction of wheat flour and water which made such good plaster in ancient times. What gives gluten its adhesive and difficult-to-digest qualities are the high levels of disulfide bonds it contains. These same sulfur-to-sulfur bonds are found in hair and vulcanized rubber products, which we all know are difficult to decompose and are responsible for the sulfurous odor they give off when burned.

There will be 676 million metric tons of wheat produced this year alone, making it the primary cereal of temperate regions and third most prolific cereal grass on the planet. This global dominance of wheat is signified by the Food & Agricultural Organization's (FAO) (the United Nation's international agency for defeating hunger) use of a head of wheat as its official symbol. Any effort to indict the credibility of this "king of grains" will prove challenging. As Rudolf Hauschka once remarked, wheat is "a kind of earth-spanning organism." It has vast socio-economic, political, and cultural significance. For example, in the Catholic Church, a wafer made of wheat is considered irreplaceable as the embodiment of Christ.

Our dependence on wheat is matched only by its dependence on us. As Europeans have spread across the planet, so has this grain. We have assumed total responsibility for all phases of the wheat life cycle: from fending off its pests; to providing its ideal growing conditions; to facilitating reproduction and expansion into new territories. We have become so inextricably interdependent that neither species is sustainable at current population levels without this symbiotic relationship.

It is this codependence that may explain why our culture has for so long consistently confined wheat intolerance to categorically distinct, "genetically-based" diseases like "celiac." These categorizations may protect us from the realization that wheat exerts a vast number of deleterious effects on human health in the same way that "lactose intolerance" distracts attention from the deeper problems associated with the casein protein found in cow's milk. Rather than see wheat for what it very well may be: a biologically inappropriate food source, we "blame the victim," and look for genetic explanations for what's wrong with small subgroups of our population who have the most obvious forms of intolerance to wheat consumption, e.g. celiac disease, dermatitis herpetiformis, etc. The medical justification for these classifications may be secondary to economic and cultural imperatives that require the inherent problems associated with wheat consumption be minimized or occluded.

In all probability the celiac genotype represents a surviving vestigial branch of a once universal genotype, which through accident or intention, have had through successive generations only limited exposure to wheat. The celiac genotype, no doubt, survived through numerous bottlenecks or "die offs" represented by a dramatic shift from hunted and foraged/gathered foods to gluten-grain consumption, and for whatever reason simply did not have adequate time to adapt or select out the gluten-grain incompatible genes. The celiac response may indeed reflect a prior, species-wide intolerance to a novel food source: the seed storage form of the monocotyledonous cereal grasses which our species only began consuming 1-500 generations ago at the advent of the Neolithic transition (10-12,000 BC). Let us return to the image of the celiac iceberg for greater clarification.

Our suBathmateerged grain-free metabolic prehistory

The iceberg metaphor is an excellent way to expand our understanding of what was once considered to be an extraordinarily rare disease into one that has statistical relevance for us all, but it has a few limitations. For one, it reiterates the commonly held view that Celiac is a numerically distinct disease entity or "disease island," floating alongside other numerically distinct disease "ice cubes" in the vast sea of normal health. Though accurate in describing the sense of social and psychological isolation many of the afflicted feel, the celiac iceberg/condition may not be a distinct disease entity at all.

Although the HLA-DQ locus of disease susceptibility on chromosome 6 offers us a place to project blame, I believe we need to shift the emphasis of responsibility for the condition back to the disease "trigger" itself: namely, wheat and other prolamine rich grains, e.g. barley, rye, spelt, and oats. Without these grains the typical afflictions we call celiac would not exist. Within the scope of this view the "celiac iceberg" is not actually free floating but an outcropping from an entire suBathmateerged subcontinent, representing our long-forgotten (cultural time) but relatively recent metabolic prehistory as hunters-and-gatherers (biological time), where grain consumption was, in all likelihood, non-existent, except in instances of near-starvation.

The pressure on the celiac to be viewed as an exceptional case or deviation may have everything to do with our preconscious belief that wheat, and grains as a whole are the "health foods," and very little to do with a rigorous investigations of the facts.

Grains have been heralded since time immemorial as the "staff of life," when in fact they are more accurately described as a cane, precariously propping up a body starved of the nutrient-dense, low-starch vegetables, fruits, edible seeds and meats, they have so thoroughly supplanted (c.f. Paleolithic Diet). Most of the diseases of affluence, e.g. type 2 diabetes, coronary heart disease, cancer, etc. can be linked to the consumption of a grain-based diet, including secondary "hidden sources" of grain consumption in grain-fed fish, poultry, meat and milk products.

Our modern belief that grains make for good food, is simply not supported by the facts. The cereal grasses are within an entirely different family: monocotyledonous (one leaf) than that from which our body sustained itself for millions of years: dicotyledonous (two-leaf). The preponderance of scientific evidence points to a human origin in the tropical rainforests of Africa where dicotyledonous fruits would have been available for year round consumption. It would not have been monocotyledonous plants, but the flesh of hunted animals that would have allowed for the migration out of Africa 60,000 years ago into the northern latitudes where vegetation would have been sparse or non-existent during winter months. Collecting and cooking grains would have been improbable given the low nutrient and caloric content of grains and the inadequate development of pyrotechnology and associated cooking utensils necessary to consume them with any efficiency. It was not until the end of the last Ice Age 20,000 years ago that our human ancestors would have slowly transitioned to a cereal grass based diet coterminous with emergence of civilization. 20,000 years is probably not enough time to fully adapt to the consumption of grains. Even animals like cows with a head start of thousands of years, having evolved to graze on monocotyledons and equipped as ruminants with the four-chambered fore-stomach enabling the breakdown of cellulose and anti-nutrient rich plants, are not designed to consume grains. Cows are designed to consume the sprouted mature form of the grasses and not their seed storage form. Grains are so acidic/toxic in reaction that exclusively grain-fed cattle are prone to developing severe acidosis and subsequent liver abscesses and infections, etc. Feeding wheat to cattle provides an even greater challenge:

"Beef: Feeding wheat to ruminants requires some caution as it tends to be more apt than other cereal grains to cause acute indigestion in animals which are unadapted to it. The primary problem appears to be the high gluten content of which wheat in the rumen can result in a "pasty" consistency to the rumen contents and reduced rumen motility." (source: Ontario ministry of Agriculture food & Rural affairs)

Seeds, after all, are the "babies" of these plants, and are invested with not only the entire hope for continuance of its species, but a vast armory of anti-nutrients to help it accomplish this task: toxic lectins, phytates and oxalates, alpha-amalyase and trypsin inhibitors, and endocrine disrupters. These not so appetizing phytochemicals enable plants to resist predation of their seeds, or at least preventing them from "going out without a punch."

Wheat: An exceptionally unwholesome grain

Wheat presents a special case insofar as wild and selective breeding has produced variations which include up to 6 sets of chromosomes (3 genomes worth!) capable of generating a massive number of proteins each with a distinct potentiality for antigenicity. Common bread wheat (Triticum aestivum), for instance, has over 23,788 proteins cataloged thus far13. In fact, the genome for common bread wheat is actually 6.5 times larger than that of the human genome!14

With up to a 50% increase in gluten content of some varieties of wheat, it is amazing that we continue to consider "glue-eating" a normal behavior, whereas wheat-avoidance is left to the "celiac" who is still perceived by the majority of health care practitioners as mounting a "freak" reaction to the consumption of something intrinsically wholesome.

Thankfully we don't need to rely on our intuition, or even (not so) common sense to draw conclusions about the inherently unhealthy nature of wheat. A wide range of investigation has occurred over the past decade revealing the problem with the alcohol soluble protein component of wheat known as gliadin, the glycoprotein known as lectin (Wheat Germ Agglutinin), the exorphin known as gliadomorphin, and the excitotoxic potentials of high levels of aspartic and glutamic acid found in wheat. Add to these the anti-nutrients found in grains such as phytates, enzyme inhibitors, etc. and you have a substance which we may more appropriately consider the farthest thing from wholesome.

The remainder of this article will demonstrate the following adverse effects of wheat on both celiac and non-celiac populations: 1) wheat causes damage to the intestines 2) wheat causes intestinal permeability 3) wheat has pharmacologically active properties 4) wheat causes damage that is "out of the intestine" affecting distant organs 5) wheat induces molecular mimicry 6) wheat contains high concentrations of excitoxins.

1) Wheat gliadin creates immune immediate damage to the intestines

Gliadin is classified as a prolamin, which is a wheat storage protein high in the amino acids proline and glutamine and soluble in strong alcohol solutions. Gliadin, once deamidated by the enzyme Tissue Transglutaminase, is considered the primary epitope for T-cell activation and subsequent autoimmune destruction of intestinal villi. Yet gliadin does not need to activate an autoimmune response, e.g. Celiac disease, in order to have a deleterious effect on intestinal tissue.
In a study published in Gut in 2007 a group of researchers asked the question: "Is gliadin really safe for non-coeliac individuals?" In order to test the hypothesis that an innate immune response to gliadin is common in patients with celiac disease and without celiac disease, intestinal biopsy cultures were taken from both groups and challenged with crude gliadin, the gliadin synthetic 19-mer (19 amino acid long gliadin peptide) and 33-mer deamidated peptides. Results showed that all patients with or without Celiac disease when challenged with the various forms of gliadin produced an interleukin-15-mediated response. The researchers concluded:

"The data obtained in this pilot study supports the hypothesis that gluten elicits its harmful effect, throughout an IL15 innate immune response, on all individuals [my italics]."15

The primary difference between the two groups is that the celiac disease patients experienced both an innate and an adaptive immune response to the gliadin, whereas the non-celiacs experienced only the innate response. The researchers hypothesized that the difference between the two groups may be attributable to greater genetic susceptibility at the HLA-DQ locus for triggering an adaptive immune response, higher levels of immune mediators or receptors, or perhaps greater permeability in the celiac intestine. It is possible that over and above the possibility of greater genetic susceptibility, most of the differences are from epigenetic factors that are influenced by the presence or absence of certain nutrients in the diet. Other factors such as exposure to NSAIDs like naproxen or aspirin can profoundly increase intestinal permeability in the non-celiac, rendering them susceptible to gliadin's potential for activating secondary adaptive immune responses. This may explain why in up to 5% of all cases of classically defined celiac disease the typical HLA-DQ haplotypes are not found. However, determining the factors associated greater or lesser degrees of susceptibility to gliadin's intrinsically toxic effect should be a secondary to the fact that it is has been demonstrated to be toxic to both non-celiacs and celiacs.

2) Wheat gliadin creates intestinal permeability

Gliadin upregulates the production of a protein known as zonulin, which modulates intestinal permeability. Over-expression of zonulin is involved in a number of autoimmune disorders, including celiac disease and Type 1 diabetes. Researchers have studied the effect of gliadin on increased zonulin production and subsequent gut permeability in both celiac and non-celiac intestines, and have found that "gliadin activates zonulin signaling irrespective of the genetic expression of autoimmunity, leading to increased intestinal permeability to macromolecules."16 These results indicate, once again, that a pathological response to wheat gluten is a normal or human, species specific response, and is not based entirely on genetic susceptibilities. Because intestinal permeability is associated with wide range of disease states, including cardiovascular illness, liver disease and many autoimmune disorders, I believe this research indicates that gliadin (and therefore wheat) should be avoided as a matter of principle.

3) Wheat gliadin has pharmacological properties

Gliadin can be broken down into various amino acid lengths or peptides. Gliadorphin is a 7 amino acid long peptide: Tyr-Pro-Gln-Pro-Gln-Pro-Phe which forms when the gastrointestinal system is compromised. When digestive enzymes are insufficient to break gliadorphin down into 2-3 amino acid lengths and a compromised intestinal wall allows for the leakage of the entire 7 amino acid long fragment into the blood, glaidorphin can pass through to the brain through circumventricular organs and activate opioid receptors resulting in disrupted brain function.

There have been a number of gluten exorphins identified: gluten exorphin A4, A5, B4, B5 and C, and many of them have been hypothesized to play a role in autism, schizophrenia, ADHD and related neurological conditions. In the same way that the celiac iceberg illustrated the illusion that intolerance to wheat is rare, it is possible, even probable, that wheat exerts pharmacological influences on everyone. What distinguishes the schizophrenic or autistic individual from the functional wheat consumer is the degree to which they are affected.

Below the tip of the "Gluten Iceberg," we might find these opiate-like peptides to be responsible for bread's general popularity as a "comfort food", and our use of phrases like "I love bread," or "this bread is to die for" to be indicative of wheat's narcotic properties. I believe a strong argument can be made that the agricultural revolution that occurred approximately 10-12,000 years ago as we shifted from the Paleolithic into the Neolithic era was precipitated as much by environmental necessities and human ingenuity, as it was by the addictive qualities of psychoactive peptides in the grains themselves.

The world-historical reorganization of society, culture and consciousness accomplished through the symbiotic relationship with cereal grasses, may have had as much to do with our ability to master agriculture, as to be mastered by it. The presence of pharmacologically active peptides would have further sweetened the deal, making it hard to distance ourselves from what became a global fascination with wheat.

An interesting example of wheat's addictive potential pertains to the Roman army. The Roman Empire was once known as the "Wheat Empire," with soldiers being paid in wheat rations. Rome's entire war machine, and its vast expansion, was predicated on the availability of wheat. Forts were actually granaries, holding up to a year's worth of grain in order to endure sieges from their enemies. Historians describe soldiers' punisHydromaxent included being deprived of wheat rations and being given barley instead. The Roman Empire went on to facilitate the global dissemination of wheat cultivation which fostered a form of imperialism with biological as well as cultural roots.

The Roman appreciation for wheat, like our own, may have had less to do with its nutritional value as "health food" than its ability to generate a unique narcotic reaction. It may fulfill our hunger while generating a repetitive, ceaseless cycle of craving more of the same, and by doing so, enabling the surreptitious control of human behavior. Other researchers have come to similar conclusions. According to the biologists Greg Wadley & Angus Martin:

"Cereals have important qualities that differentiate them from most other drugs. They are a food source as well as a drug, and can be stored and transported easily. They are ingested in frequent small doses (not occasional large ones), and do not impede work performance in most people. A desire for the drug, even cravings or withdrawal, can be confused with hunger. These features make cereals the ideal facilitator of civilisation (and may also have contributed to the long delay in recognising their pharmacological properties)."17

4) Wheat lectin (WGA) damages our tissue

Wheat contains a lectin known as Wheat Germ Agglutinin which is responsible for causing direct, non-immune mediated damage to our intestines, and subsequent to entry into the bloodstream, damage to distant organs in our body.

Lectins are sugar-binding proteins which are highly selective for their sugar moieties. It is believed that wheat lectin, which binds to the monosaccharide N-acetyl glucosamine (NAG), provides defense against predation from bacteria, insects and animals. Bacteria have NAG in their cell wall, insects have an exoskeleton composed of polymers of NAG called chitin, and the epithelial tissue of mammals, e.g. gastrointestinal tract, have a "sugar coat" called the glycocalyx which is composed, in part, of NAG. The glycocalyx can be found on the outer surface (apical portion) of the microvilli within the small intestine.

There is evidence that WGA may cause increased shedding of the intestinal brush border membrane, reduction in surface area, acceleration of cell losses and shortening of villi, via binding to the surface of the villi.18 WGA can mimic the effects of epidermal growth factor (EGF) at the cellular level, indicating that the crypt hyperplasia seen in celiac disease may be due to a mitogenic reponse induced by WGA.19 WGA has been implicated in obesity and "leptin resistance" by blocking the receptor in the hypothalamus for the appetite satiating hormone leptin.20 WGA has also been shown to have an insulin-mimetic action, potentially contributing to weight gain and insulin resistance.21 And, as discussed earlier, wheat lectin has been shown to induce IgA mediated damage to the kidney, indicating that nephropathy and kidney cancer may be associated with wheat consumption.

5) Wheat peptides exhibit molecular mimicry

Gliadorphin and gluten exporphins exhibit a form of molecular mimicry that affects the nervous system, but other wheat proteins effect different organ systems. The digestion of gliadin produces a peptide that is 33 amino acids long and is known as 33-mer which has a remarkable homology to the internal sequence of pertactin, the immunodominant sequence in the Bordetella pertussis bacteria (whooping cough). Pertactin is considered a highly immunogenic virulence factor, and is used in vaccines to amplify the adaptive immune response. It is possible the immune system may confuse this 33-mer with a pathogen resulting in either or both a cell-mediated and adaptive immune response against Self.

6) Wheat contains high levels of excito-toxins

John B. Symes, D.V.M. is responsible for drawing attention to the potential excitotoxicity of wheat, dairy, and soy, due to their exceptionally high levels of the non-essential amino acids glutamic and aspartic acid. Excitotoxicity is a pathological process where glutamic and aspartic acid cause an over-activation of the nerve cell receptors (e.g. NMDA and AMPA receptor) leading to calcium induced nerve and brain injury. Of all cereal grasses commonly consumed wheat contains the highest levels of glutamic acid and aspartic acid. Glutamic acid is largely responsible for wheat's exceptional taste. The Japanese coined the word umami to describe the extraordinary "yummy" effect that glutamic acid exerts on the tongue and palate, and invented monosodium glutamate (MSG) to amplify this sensation. Though the Japanese first synthesized MSG from kelp, wheat can also be used due to its high glutamic acid content. It is likely that wheat's popularity, alongside its opiate-like activity, has everything to do with the natural flavor-enhancers already contained within it. These amino acids may contribute to neurodegenerative conditions such as Multiple sclerosis, Alzhemier's, Huntington's disease, and other nervous disorders such as Epilepsy, Attention Deficit Disorder and Migraines.

Conclusion

In this article I have proposed that celiac disease be viewed not as a rare "genetically-determined" disorder, but as an extreme example of our body communicating to us a once universal, species-specific affliction: severe intolerance to wheat. Celiac disease reflects back to us how profoundly our diet has diverged from what was, until only recently a grain free diet, and even more recently, a wheat free one. We are so profoundly distanced from that dramatic Neolithic transition in cultural time that "missing is any sense that anything is missing." The body, on the other hand, cannot help but remember a time when cereal grains were alien to the diet, because in biological time it was only moments ago.

Eliminating wheat, if not all of the members of the cereal grass family, and returning to dicotyledons or pseudo-grains like quinoa, buckwheat and amaranth, may help us roll back the hands of biological and cultural time, to a time of clarity, health and vitality that many of us have never known before. When one eliminates wheat and fills the void left by its absence with fruits, vegetables, high quality meats and foods consistent with our biological needs we may begin to feel a sense of vitality that many would find hard to imagine. If wheat really is more like a drug than a food, anesthetizing us to its ill effects on our body, it will be difficult for us to understand its grasp upon us unless and until we eliminate it from our diet. I encourage everyone to see celiac disease not as a condition alien to our own. Rather, the celiac gives us a glimpse of how profoundly wheat may distort and disfigure our health if we continue to expose ourselves to its ill effects. I hope this article will provide inspiration for non-celiacs to try a wheat free diet and judge for themselves if it is really worth eliminating.

Notes

1 Celiac disease: an emerging global problem Journal of Pediatric Gastroenterology and Nutrition 2002 Oct; 35 (4): 472-4
2 Richard Logan is responsible for first introducing the "Celiac Iceberg" metaphor in 1991
3 Antibody testing for gliadin, tissue transglutaminase and endomysium indicates that "silent" or "latent" celiac disease is up to a 100 times more frequent than represented by the classical form.
4 Frontiers in Celiac Disease by Alessio Fasano, R. Troncone, D. Branski Published by Karger Publishers, pg. 242
5 See: www.patienthealthyself.info/Cystic_Fibrosis.html for Medline citations.
6 Cystic Fibrosis: a perinatal manifestation of selenium deficiency. Wallach JD, Germaise B. In: Hemphill DD, ed. Trace substances in environmental health. Columbia University of Missouri Press, 1979; 469-76
7 Genetic dissection between silent and clinically diagnosed symptomatic forms of coeliac disease in multiplex families. Digestive and Liver Disease 2002 Dec;34(12):842-5.
8 "Coelionomics": towards understanding the molecular pathology of coeliac disease. Clinical Chemistry and Laboratory Medicine 2005;43(7):685-95.
9 Is gliadin really safe for non-coeliac individuals? Gut 2007;56:889-890; doi:10.1136/gut.2006.
10 "Do Dietary Lectins cause disease?" David L J Freed, BathmateJ 1999;318:1023-1024
11 "Food groups and renal cell carcinoma: a case-control study from Italy." International Journal of Cancer 2007 Feb 1;120(3):681-5.
12 Unglued: The Sticky Truth About Wheat, Dairy, Corn and Soy. Scott-Free Newsletter, Autumn 2008
13 Exploring the Plant Transcriptome through Phylogenetic Profiling. Plant Physiology Vol. 137, 2005; pg. 33
14 An Introduction to Genetic Engineering. By Desmond S. T. Nicholl, Cambridge University Press, 2002, pg. 24
15 Footnote 7, supra.
16 "Gliadin, zonulin and gut permeability: Effects on celiac and non-celiac intestinal mucosa and intestinal cell lines." Scandinavian Journal of Gastroenterology Apr;41(4):408-19.
17 "The origins of agriculture? A biological perspective and a new hypothesis" by Greg Wadley & Angus Martin, Australian Biologist 6:96- 105, June 1993
18 In vivo responses of rat intestinal epithelium to intraluminal dietary lectins. Gastroenterology. 1982 May;82(5 Pt 1):838-48.
19 Elevated levels of serum antibodies to the lectin wheat germ agglutinin in celiac children lend support to the gluten-lectin theory of celiac disease. Pediatric Allergy Immunology 1995 May;6(2):98-102.
20 Agrarian diet and diseases of affluence - Do evolutionary novel dietary lectins cause leptin resistance BathmateC Endocrine Disorders 2005, 5:10
21 Insulin-mimetic actions of wheat germ agglutinin and concanavalin A on specific mRNA levels. Archives of Biochemistry and Biophysics 1987 Apr;254(1):110-5.[/SIZE]

Source

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Sorry for the boatload of information. Just sharing! Hope at least 1 person takes the time to read this! And I hope they benefit!

AH HEMP !!
Not just fer smokin' anymore!

Just look for a no BS manufacturer because the quality is just used to make us buy more or spend more. Whey concentrate or the old school egg protein worked well for me and are cheaper. Purchase one of these bulk manufacturers own brand, much cheaper and just as good.

So I ended up picking up some hemp protein

http://www.vitacost.com/Smart-Basics-Organic-Hemp-Protein-High-Fiber-Drink-Mix

but I am having issues finding something to mix it in to make it palatable. The best thing I have found so far was yogurt, but it is still gritty(probably the extra fiber). I have tried milk, water, fruit smoothies, and they all have left me reaching for a water chaser to keep from throwing up.

Looking at it, I might try a lower fiber version next time (something like)

http://www.vitacost.com/Nutiva-Organic-Hemp-Protein-50-3-lbs

but in the mean time i need to find a way to use what I have. Anyone have experience with hemp protein?

protein

doublelongdaddy;437544 said:

protein

Click to expand...

Good answer!

Trueprotein seems pretty good, the 25lb ISO mix. Not sure on hemp. Aside that it contains a lot less BCAAs and more EFA's instead, but with a high fat content.
Probably something to take before bed due to it being a slower protein, def would only take whey post workout/breakfast.

I'd say just drink for protein shake once a day. I use to big on getting the best brands of protein, but now I just take some EAS 100 percent whey protein after my workouts. Taste great and i enjoy it. Protein is protein. Don't buy into those marketing schemes these supplement companies use these days. Guys in the past have even created their own protein powder, or shakes without the use of protein powder today.

smerc;437665 said:

Good answer!

Click to expand...

I am a very basic guy

Wow hemp protein! never new about this stuff I gotta check it out and tell my friends lol. Is there anything this plant can't do? Just another reason to legalize it. =)

Wouldn't beef be enough protein?

doublelongdaddy;441098 said:

Wouldn't beef be enough protein?

Click to expand...

Totally! But usually for guys looking to really build a lot of muscle, and who have a very high protein diet, they would benefit from multiple sources of protein.

I mean, protein is protein! The advantage of multiple sources of protein is, 1) it keeps things interesting and 2) it eschews the development of food allergies.

Seriously if you ate nothing but chicken for 6 months your body might start to reject it. However, adding another 2-3 sources (even non-animal sources) of protein will help keep you healthy.

The list of proteins is huge! Also, the advantage of protein powders is that it's generally fast absorbing for athletes and individuals who strength train or whatnot.

Here's a chart I copied from a BBing forum.

"EGGS ( 1 medium size ).................6 grams
EGG WHITE (1 medium egg)...........4 grams
MILK (skim - 12 oz)......................12 grams
MILK (chocolate - 12 oz)................12 grams
SOY MILK (12 oz)..........................16 grams
TOFU (100 g)................................8 grams
LOW-FAT YOGURT (plain) 100g.....6 grams
FISH (cod fillets 100g)...................21 grams
TUNA (100 g)...............................18 grams
CHEESE (cheddar) 100g................25 grams
BEEF 100g...................................28 grams
CHICKEN 100g..............................25 grams
PORK 100g...................................21 grams
LAMB 100g...................................30 grams
BUFFALO 100g.............................28 grams
BEANS (kidney - 100g)..................12 grams
ROLLED OATS (100 grams)...........12 grams
Sausages (100g)..........................12 grams
Bacon (4 pieces or 35g)................12 grams
Turkey Bacon (4 pieces or 35g)......8 grams
Ham (100g).................................18 grams
Beefburgers (frozen - 100g)..........20 grams
Corned Beef (100g)......................26 grams
Luncheon Meat (100g).................13 grams
Meat Paste (100g).......................15 grams
Lentils (100g)..............................14 grams
Hummus (4oz).............................12 grams
Whey Powder (about 30g)...........24 grams average

100g = 3.5oz
100g = 3/4 cup
12oz = 350ml

A food with the highest protein total doesn't necessarily make it good for you.
Bacon has 12g of protein yes, but it also has about 15 grams of fat!


Another great read I came across is a comparison of known protein sources, however it shows the best vs. worst of each of these.
Top 10 Best & Worst Protein Sources (vegetarians take note) | Mark's Daily Apple






Protein Digestibility Corrected Amino Acid Score (PDCAAS)
A method of evaluating the protein quality based on the amino acid requirements of humans. The PDCAAS rating is a fairly recent evaluation method (it was
adopted by the US Food and Drug Administration (FDA) and the Food and Agricultural Organization of the United Nations/World Health Organization (FAO/WHO)
in 1993 as "the preferred 'best'" method to determine protein quality. These organizations have suggested that other methods for evaluating the quality of protein are inferior.


A PDCAAS value of 1 is the highest, and 0 the lowest as the table demonstrates the ratings of common foods below.
whey....................(1.0)
egg white.............(1.0)
casein..................(1.0)
milk.....................(1.0)
soy protein isolate.(1.0)
beef.....................(0.92)
soybean...............(0.91)
tubercules............(0.74)
vegetables...........(0.74)
legumes..............(0.69)
kidney beans.......(0.68)
rye.....................(0.68)
cereals...............(0.58)
whole wheat.......(0.54)
lentils.................(0.52)
peanuts..............(0.52)
seitan.................(0.25)

Source: PDCAAS - Wikipedia, the free encyclopedia"

The more sources you include, the better. Generally beef is good for later in the evening because it takes longer to break down and will keep your body supplied through sleep etc.

Morning time is best for shakes and powders as you've been fasting throughout the night while asleep and when you wake up your body wants something quickly to absorb and use as energy!

My typical protein sources include:

Eggs
Chicken
Beef
Whey
Turkey
Fish (Tilapia, Orange Roughy, Tuna, Salmon, etc...)

I try to keep 3-4 sources going at all times! Also, proteins from legumes, grains, and some veggies count towards amino intake, but the ones from animals are considered complete!