array of bowel-destroying effects – there is an arsenal.
Non-Wheat Grains: You Might As Well Eat Jelly Beans
There is no question that, in this barrel of rotten apples, wheat is the rottenest. But you still may not want to make cider with those other apples.
What I call ‘non-wheat grains’, such as oats, barley, rye, millet, teff, sorghum, corn and rice, are nonetheless seeds of grasses with potential for curious effects in nonruminant creatures not adapted to their consumption. I would classify non-wheat grains as less bad than the worst – modern wheat – but less bad is not necessarily good. (That extraordinarily simple insight – that less bad is not necessarily good – is one that will serve you well over and over as you learn to question conventional nutritional advice. You will realize that much of what we have been told by the dietary community, the food industry and even government agencies violates this basic principle of logic again and again.) Less bad can mean that a variety of undesirable health effects can still occur with that seed’s consumption – those effects will just not be as bad as those provoked by modern wheat.
So what’s the problem with the seeds of non-wheat grasses? While none achieve the nastiness of the seeds of modern wheat, they each have their own unique issues. For starters, they’re all high in carbohydrates. Typically, 60 to 85 per cent of the calories from the seeds of grasses are in the form of carbohydrates. This makes sense, since the carbohydrate stored in the seed was meant to provide nutrition to the sprouting plant as it germinates. But the carbohydrate in seeds, called amylopectin A, is rapidly digested by humans and raises blood sugar, gram for gram, higher than table sugar does.
For instance, a 125 g (4½ oz) serving of cooked organic, stoneground oatmeal has nearly 50 grams of net carbohydrates (total carbohydrates minus fibre, which we subtract because it has no glycaemic potential), or the equivalent of slightly more than 11 teaspoons of sugar, representing 61 per cent of the calories in oatmeal. This gives it a glycaemic index (GI, an index of blood sugar-raising potential) of 55, which is enough to send blood sugar through the roof and provoke all the phenomena of glycation, i.e., glucose modification of proteins that essentially acts as biological debris in various organs. This irreversible process leads to conditions such as cataracts, hypertension, the destruction of joint cartilage that results in arthritis, kidney disease, heart disease and dementia. (Note that a glycaemic index of 55 falls into what dietitians call the ‘low’ glycaemic index range, despite the potential to generate high blood sugars. We discuss this common fallacy in Chapter 5.) All non-wheat grasses, without exception, raise blood sugar and provoke glycation to similar degrees.
Human manipulation makes it worse. If corn is not consumed as intact kernels but instead is pulverized into fine cornflour, the surface area for digestion increases exponentially and accounts for the highest blood sugars possible from any food. This is why the glycaemic index of cornflour is 90 to 100, compared with 60 for corn on the cob and 59 to 65 for sucrose or table sugar.
For years, we’ve been told that ‘complex’ carbohydrates are better for us than ‘simple’ sugars because the lengthy carbohydrate molecules of amylopectin A and amylose in grains don’t raise blood sugar as high as sugars with one or two sugar molecules, such as glucose (one sugar) or sucrose (two sugars: glucose and fructose), do. But this is simply wrong, and this silly distinction is therefore being abandoned: the GI of complex carbohydrates is the same as or higher than that of simple sugars. The GI of whole wheat bread: 72; the GI of millet as a hot cereal: 67. Neither are any better than the GI of sucrose: 59 to 65. (Similar relationships hold for the glycaemic load, a value that factors in typical portion size.) The World Health Organization (WHO) and the Food and Agriculture Organization of the United Nations have both advised dropping the complex versus simple distinction, and rightly so, as grains, from a blood sugar viewpoint, are the same as or worse than sugar.
And the problems with non-wheat grains don’t end with blood sugar issues.
Lectins: Good Enough for the KGB
The lectin proteins of grains are, by design, toxins. Lectins discourage creatures, such as moulds, fungi and insects, from eating the seeds of a plant by sickening or killing them. After all, the seed is the means by which plants continue their species. When we consume plants, we consume defensive lectins. Lectin proteins’ effects on humans vary widely, from harmless to fatal. Most plant lectins are benign, such as those in spinach and white mushrooms, which cause no adverse effects when consumed as a spinach salad. The lectin of castor beans is an entirely different story; its lectin, ricin, is highly toxic and is fatal even in small quantities. Ricin has been used by terrorists around the world. Gyorgy Markov, Bulgarian dissident and critic of the Soviet government, was murdered by KGB agents in 1978 when he was poked with the tip of an umbrella laced with ricin.
The lectin of the seed of wheat is wheat germ agglutinin (WGA). It is neither as benign as the lectin of spinach nor as toxic as the lectin of ricin; it is somewhere in between. WGA wreaks ill effects on everyone, regardless of whether you have coeliac disease, gluten sensitivity or no digestive issues at all. The lectins of rye, barley and rice are structurally identical to WGA and share all of its properties and are also called ‘WGA’. (The only substantial difference is that rye, barley and rice express a single form of lectin, while genetically more complex wheat expresses up to three different forms.) Interestingly, 21 per cent of the amino acid structure of WGA lectins overlaps with ricin, including the active site responsible for shutting down protein synthesis, the site that accounts for ricin’s exceptional toxicity.1
Lectin proteins have the specific ability to recognize glycoproteins (proteins with a sugar side chain). This makes plant lectins effective in recognizing common glycoproteins on, say, the surface of a fungal cell. But that same process can occur in humans. When a minute quantity, such as 1 milligram, of WGA is purified and intestinal tissue is exposed to it, intestinal glycoproteins are bound and severe damage that resembles the effects of coeliac disease results.2 We also know that WGA compounds the destructive intestinal effects of coeliac disease started by gliadin and other grain prolamin proteins.3 If you have inflammatory bowel disease, ulcerative colitis, or Crohn’s disease, grain lectins intensify the inflammation, making cramps, diarrhoea, bleeding and poor nutrient absorption worse.
WGA is oddly indestructible. It is unaffected by cooking, boiling, baking or frying. WGA is also untouched by stomach acid. Though the acid produced in the human stomach is powerfully corrosive (dip your finger in a glass full of stomach acid and you won’t have a finger for very long), WGA is impervious to it, entering the stomach and passing through the entire gastrointestinal tract unscathed, undigested and free to do what it likes to any glycoproteins exposed along the way.
While most WGA remains confined to the intestine, doing its damage along the 30-foot length of this organ, we know that a small quantity gets into your bloodstream. (We know this because people commonly develop antibodies to this protein.) Once WGA enters the bloodstream, odd things happen: red blood cells clump (or ‘agglutinate’, the basis for WGA’s name), which can, under certain circumstances (obesity, smoking, sedentary living, dehydration, etc.), increase the tendency of blood to clot – the process that leads to heart attack and stroke. WGA is often called a mitogen because it activates cell division, or mitosis (a concept familiar to anyone who studies cancer, a disease characterized by unrestrained mitosis). WGA has indeed been demonstrated to cause mitosis in lymphocytes (immune system cells) and cells lining the intestine.4 We know that such phenomena underlie cancer, such as the intestinal lymphoma that afflicts people with coeliac disease.5 WGA also mimics the effects of insulin on fat cells. When WGA encounters a fat cell, it acts just as if it were insulin, inhibiting activation of fat release and blocking weight loss while making the body more reliant on sugar sources for energy.6 WGA also blocks the hormone leptin, which is meant to shut off appetite when the physical need to eat has been satisfied. In the presence of WGA, appetite
