Studies point to a simple reason, the prices, not to the amount of care. And lowering prices would upset a lot of people in the health industry.
The United States spends almost twice as much on health care, as a percentage of its economy, as other advanced industrialized countries — totaling $3.3 trillion, or 17.9 percent of gross domestic product in 2016.
But a few decades ago American health care spending was much closer to that of peer nations.
What happened?
A large part of the answer can be found in the title of a 2003 paper in Health Affairs by the Princeton University health economist Uwe Reinhardt: “It’s the prices, stupid.”
The study, also written by Gerard Anderson, Peter Hussey and Varduhi Petrosyan, found that people in the United States typically use about the same amount of health care as people in other wealthy countries do, but pay a lot more for it.
Ashish Jha, a physician with the Harvard T.H. Chan School of Public Health and the director of the Harvard Global Health Institute, studies how health systems from various countries compare in terms of prices and health care use. “What was true in 2003 remains so today,” he said. “The U.S. just isn’t that different from other developed countries in how much health care we use. It is very different in how much we pay for it.”
Assessing the systems in eight countries can inform the debate in the U.S. over universal coverage.
A recent study in JAMA by scholars from the Institute for Health Metrics and Evaluation in Seattle and the U.C.L.A. David Geffen School of Medicine also points to prices as a likely culprit. Their study spanned 1996 to 2013 and analyzed U.S. personal health spending by the size of the population; its age; and the amount of disease present in it.
They also examined how much health care we use in terms of such things as doctor visits, days in the hospital and prescriptions. They looked at what happens during those visits and hospital stays (called care intensity), combined with the price of that care.
The researchers looked at the breakdown for 155 different health conditions separately. Since their data included only personal health care spending, it did not account for spending in the health sector not directly attributed to care of patients, like hospital construction and administrative costs connected to running Medicaid and Medicare.
Over all, the researchers found that American personal health spending grew by about $930 billion between 1996 and 2013, from $1.2 trillion to $2.1 trillion (amounts adjusted for inflation). This was a huge increase, far outpacing overall economic growth. The health sector grew at a 4 percent annual rate, while the overall economy grew at a 2.4 percent rate.
You’d expect some growth in health care spending over this span from the increase in population size and the aging of the population. But that explains less than half of the spending growth. After accounting for those kinds of demographic factors, which we can do very little about, health spending still grew by about $574 billion from 1996 to 2013.
Did the increasing sickness in the American population explain much of the rest of the growth in spending? Nope. Measured by how much we spend, we’ve actually gotten a bit healthier. Change in health status was associated with a decrease in health spending — 2.4 percent — not an increase. A great deal of this decrease can be attributed to factors related to cardiovascular diseases, which were associated with about a 20 percent reduction in spending.
This could be a result of greater use of statins for cholesterol or reduced smoking rates, though the study didn’t point to specific causes. On the other hand, increases in diabetes and low back and neck pain were associated with spending growth, but not enough to offset the decrease from cardiovascular and other diseases.
Did we spend more time in the hospital? No, though we did have more doctor visits and used more prescription drugs. These tend to be less costly than hospital stays, so, on balance, changes in health care use were associated with a minor reduction (2.5 percent) in health care spending.
That leaves what happens during health care visits and hospital stays (care intensity) and the price of those services and procedures.
Did we do more for patients in each health visit or inpatient stay? Did we charge more? The JAMA study found that, together, these accounted for 63 percent of the increase in spending from 1996 to 2013. In other words, most of the explanation for American health spending growth — and why it has pulled away from health spending in other countries — is that more is done for patients during hospital stays and doctor visits, they’re charged more per service, or both.
Though the JAMA study could not separate care intensity and price, other research blames prices more. For example, one study found that the spending growth for treating patients between 2003 and 2007 is almost entirely because of a growth in prices, with little contribution from growth in the quantity of treatment services provided. Another study found that U.S. hospital prices are 60 percent higher than those in Europe. Other studies also point to prices as a major factor in American health care spending growth.
There are ways to combat high health care prices. One is an all-payer system, like that seen in Maryland. This regulates prices so that all insurers and public programs pay the same amount. A single-payer system could also regulate prices. If attempted nationally, or even in a state, either of these would be met with resistance from all those who directly benefit from high prices, including physicians, hospitals, pharmaceutical companies — and pretty much every other provider of health care in the United States.
Higher prices aren’t all bad for consumers. They probably lead to some increased innovation, which confers benefits to patients globally. Though it’s reasonable to push back on high health care prices, there may be a limit to how far we should.
SOURCE: NY TIMES
LEUSDEN, Netherlands — The shouts of schoolchildren playing outside echoed through the gymnasium where an obstacle course was being set up.
There was the “Belgian sidewalk,” a wooden contraption designed to simulate loose tiles; a “sloping slope,” ramps angled at an ankle-unfriendly 45 degrees; and others like “the slalom” and “the pirouette.”
They were not for the children, though, but for a class where the students ranged in age from 65 to 94. The obstacle course was clinically devised to teach them how to navigate treacherous ground without having to worry about falling, and how to fall if they did.
“It’s not a bad thing to be afraid of falling, but it puts you at higher risk of falling,” said Diedeke van Wijk, a physiotherapist who runs WIJKfysio and teaches the course three times a year in Leusden, a bedroom community just outside Amersfoort, in the center of the country.
The Dutch, like many elsewhere, are living longer than in previous generations, often alone. As they do, courses that teach them not only how to avoid falling, but how to fall correctly, are gaining popularity.
This one, called Vallen Verleden Tijd course, roughly translates as “Falling is in the past.” Hundreds of similar courses are taught by registered by physio- and occupational therapists across the Netherlands.
Yet falling courses — especially clinically tested ones — are a fairly recent phenomenon, according to Richard de Ruiter, of the Sint Maartenskliniek in Nijmegen, the foundation hospital that developed this particular course.
Virtually unheard-of just a decade ago, the courses are now common enough that the government rates them. Certain forms of Dutch health insurance even cover part of the costs.
While the students are older, not all of them seemed particularly frail. Herman van Lovink, 88, arrived on his bike. So did Annie Houtveen, 75. But some arrived with walkers and canes, and others were carefully guided by relatives.
Falling can be a serious thing for older adults. Aging causes the bones to become brittle, and broken ones do not heal as readily.
Today, 18.5 percent of the Dutch population — roughly 3.2 million people — is 65 or older, according to official statistics. In 1950, about the time some of the younger course participants were born, people 65 or older made up just 7.7 percent of the population.
Across the Netherlands, 3,884 people 65 or older died as result of a fall in 2016, a 38 percent increase from two years earlier.
Experts say the rise in fatalities reflects the overall aging of the population, and also factors such as the growing use of certain medications or general inactivity.
“It’s same as with young children: More and more old people have an inactive lifestyle,” said Saskia Kloet, a program manager at VeiligheidNL, an institution that offers similar courses.
Even inactivity in one’s 30s or 40s could lead to problems later in life, she noted.
Like many people her age, Hans Kuhn, 85, worried that her daily routine — and the ability to live alone — would end if she ever lost her balance and fell.
She has lived in her house for decades, and alone since her partner died years ago. Its steeply winding staircase is equipped with a motorized chair on a rail to help reach upper floors. “I only use it when I have to bring lots of heavy things upstairs,” said Ms. Kuhn, herself a retired physiotherapist.
Ms. Kuhn’s entire house is a study in efficiency and simple modifications that can make all the difference for an older person. Hand grips are installed in just the right places, as well as ramps to accommodate her two walkers.
There is a stationary exercise bike to keep her moving, and a weight machine made from a big can of beans and string to maintain her upper body strength.
Even as she feels herself grow frailer and less flexible, she knows how to stay fit. “My main problem is I’m very afraid of falling,” she said.
So she joined the course, which meets twice a week. On Tuesdays, the students build confidence by walking and re-walking the obstacle course. Thursdays are reserved for the actual falls.
In order to learn, the students start by approaching the mats slowly, lowering themselves down at first. Over the weeks, they learn to fall.
“Naturally, they are not interested in courses on falling at first, but once they see that they can do it, then it’s fun,” Ms. Kloet said. “But there is also a very important social aspect.”
Indeed, seeing one another helplessly sprawled across the gym mats gave way to giggling and plenty of dry comments, knowing jokes, general ribbing and hilarity.
“Stop your chattering,” Ms. van Wijk warned a group of well-dressed women who were supposed to be concentrating on the correct way to let themselves fall onto the foot-thick blue mat.
“I would,” said Loes Bloemdal, 80, laughing. “But I have no one to talk with all day.”
In preparing their bodies for a possibly apocalyptic event, the students appeared to forget about their age.
Mr. van Lovink, the cyclist, asked if they would learn standing on one leg. “Why would you want to do that?” replied Ms. van Wijk.
“To be able to put on my pants,” Mr. van Lovink said seriously, but to the amusement of his classmates.
Ms. van Wijk advised them all to always sit when putting on their pants.
“That’s the power of physiotherapy with geriatrics,” she said. “You practice the things you know you can do, and not the things you can’t.”
Happiness has little to do with it. Research suggests meaning in your life is important for well-being.
My favorite medical diagnosis is “failure to thrive.”
Not because patients are failing to thrive — that part makes me sad. But because of the diagnosis’s bold proposition: Humans, in their natural state, are meant to thrive.
My patient, however, was not in his natural state. Cancer had claimed nearly every organ in his body. He’d lost a quarter of his body mass. I worried his ribs would crack under the weight of my stethoscope.
“You know,” he told me the evening I admitted him. “A few years ago, I wouldn’t have cared if I made it. ‘Take me God,’ I would’ve said. ‘What good am I doing here anyway?’ But now you have to save me. Sadie needs me.”
He’d struggled with depression most of his life, he said. Strangely enough, it seemed to him, he was most at peace while caring for his mother when she had Parkinson’s, but she died years ago. Since then, he had felt aimless, without a sense of purpose, until Sadie wandered into his life.
Sadie was his cat.
Only about a quarter of Americans strongly endorse having a clear sense of purpose and of what makes their lives meaningful, while nearly 40 percent either feel neutral or say they don’t. This is both a social and a public health problem: Research increasingly suggests that purpose is important for a meaningful life — but also for a healthy life.
Purpose and meaning are connected to what researchers call eudaimonic well-being. This is distinct from, and sometimes inversely related to, happiness (hedonic well-being). One constitutes a deeper, more durable state, while the other is superficial and transient.
Being a pediatric oncologist, for example, is not a “happy” job, but it may be a very rewarding one. Raising a family can be profoundly meaningful, but parents are often less happy while interacting with their children than exercising or watching television.
Having purpose is linked to a number of positive health outcomes, including better sleep, fewer strokes and heart attacks, and a lower risk of dementia, disability and premature death. Those with a strong sense of purpose are more likely to embrace preventive health services, like mammograms, colonoscopies and flu shots.
And people with high scores on measures of eudaimonic well-being have low levels of pro-inflammatory gene expression; those with high scores on hedonic pleasure have just the opposite.
Doing good, it seems, is better than feeling good.
One study analyzed how having purpose influences one’s risk of dementia. Researchers assessed baseline levels of purpose for 951 individuals without dementia, then followed them for seven years, controlling for things like depression, neuroticism, socioeconomic status and chronic disease. Those who had expressed a greater sense of purpose were 2.4 times less likely to develop Alzheimer’s, and were far less likely to develop even minor cognitive problems.
Another study followed more than 6,000 individuals over 14 years and found that those with greater purpose were 15 percent less likely to die than those who were aimless, and that having purpose was protective across the life span — for people in their 20s as well as those in their 70s.
Having purpose is not a fixed trait, but rather a modifiable state: Purpose can be honed through strategies that help us engage in meaningful activities and behaviors. This has implications at both the dinner table and the hospital bed.
A recent randomized control trial compared the effect of “meaning-centered” versus “support-focused” group therapy for patients with metastatic cancer. Patients in the support groups met weekly and discussed things like “the need for support,” “coping with medical tests” and “communicating with providers.”
Patients in the meaning-centered groups focused instead on spiritual and existential questions. They explored topics like “meaning before and after cancer,” “what made us who we are today,” and “things we have done and want to do in the future.” Meaning-centered patients experienced fewer physical symptoms, had a higher quality of life, felt less hopeless — and were more likely to want to keep living.
Other research suggests that school programs that allow students to discuss positive emotions and meaningful experiences may enhance psychological well-being, and protect against future behavioral challenges. But this isn’t how we usually operate. We instead assume that anxiety and depression are problems to be treated — not that emotional resilience and human flourishing are states to be celebrated.
What’s powerful about these conversations is not just that they can help cancer patients through treatment or help teenagers build resiliency — they can also help the rest of us. We should all consider asking ourselves and our loved ones these questions more often.
During my most trying months of medical school, I met every Sunday evening with three friends. Phones off, lights dim, wine glasses full. We shared the most challenging and most rewarding moments of our weeks. These conversations helped each of us glean — or perhaps create — meaning in challenging, sometimes traumatic, experiences: the death of a child we’d cared for; abusive language from a superior; the guilt of committing a medical error.
It was in these sessions that I chose my specialty, decided to apply to policy school, and vowed to reconnect with a lost friend.
Meaning grows not just from conversation, of course, but also from action. One recent study randomly assigned 10th graders to volunteer weekly with elementary students — to help with homework, cooking, sports, or arts and crafts — or put them on a wait list.
Teenagers who volunteered had lower levels of inflammation, better cholesterol profiles and lower body mass index. Those who had the biggest jumps in empathy and altruism scores had the largest reductions in cardiovascular risk.
Engaging in these kinds of activities may be most important for individuals whose identity is in flux, like parents with children leaving for college or workers preparing for retirement. A program run by Experience Corps, an organization that trains older adults to tutor children in urban public schools, has shown marked improvements in mental and physical health among tutors. The improvements included higher self-esteem, more social connectedness, and better mobility and stamina. (The children do better, too.)
This work hints at an underlying truth: Finding purpose is rarely an epiphany, nor is it something you pick up at the mall or download from the app store. It can be a long, arduous process that requires introspection and conversation, then a commitment to act.
The key to a deeper, healthier life, it seems, isn’t knowing the meaning of life — it’s building meaning into your life. Even if meaning is a four-legged friend named Sadie.
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Research indicates that the consumption of wheat contributes to the growth of pathogenic bacteria in our gut, adding to growing concern that wheat (which is often contaminated with Roundup herbicide) is one of the worst foods to consume for gut health.
A concerning study published in FEMS Microbiology Ecology titled, “Diversity of the cultivable human gut microbiome involved in gluten metabolism: isolation of microorganisms with potential interest for coeliac disease,” reveals something remarkable about the capabilities (and liabilities) of human gut bacteria (microbiome) when exposed to foods such as wheat.
Some of the extremely hard to digest proteins in wheat colloquially known as “gluten” (there are actually over 23,000 identified in the wheat proteome and not just one problematic protein as widely believed) were found metabolizable through a 94 strains of bacterial species isolated from the human gut (via fecal sampling).
This discovery is all the more interesting when you consider that, according to Alessio Fasano, the Medical Director for The University of Maryland’s Center for Celiac Research, the human genome does not possess the ability to produce enzymes capable of sufficiently breaking down gluten.
As reported on TenderFoodie in interview:
“We do not have the enzymes to break it [gluten] down. It all depends upon how well our intestinal walls close after we ingest it and how our immune system reacts to it.”
The new study helps to fill the knowledge gap as to how humans are capable of dealing with wheat consumption at all, considering it did not play a role in the diets of non-Western peoples until very recently (perhaps only a few generations), and even in those who have consumed it for hundreds of generations, it is still on a biological scale of time a relatively new food in the human diet which was grain free for 99.999% of human evolution.
As we have analyzed in a previous essay, The Dark Side of Wheat, the consumption of wheat is a relatively recent dietary practice, stretching back only 10,000 years – a nanosecond in biological time. We simply have not had time to genetically adapt to its consumption (at least not without experiencing over 200 empirically confirmed adverse health effects!).
The new finding reported here shows that bacteria in our microbiome extend our ability to digest physiologically incompatible foods – or at least tolerate them to the degree that they don’t outright kill us. This may explain why there is such a wide variability in responses to gluten and why the health of our microbiome may play a — if not the — central role in determining our levels of susceptibility to its adverse effects.
Another provocative finding of the study is that some of the strains capable of breaking down the more immunotoxic peptides in wheat, including the 33 amino acid long peptide known as 33-mer, are highly pathogenic, such as Clostridium botulinum – the bacteria that is capable of producing botulism. As we discussed in a previous article on Monsanto’s Roundup herbicide (glyphosate) contributing to the overgrowth of this pathogenic strain of bacteria in animals exposed to GMO feed,
“[It]t only takes 75 billionths of a gram (75 ng) to kill a person weighing 75 kg (165 lbs). It has been estimated that only 1 kilogram (2.2 lbs) would be enough to kill the entire human population.”
There are several important implications to this finding. First, the consumption of wheat preferentially favors the growth of pathogenic bacteria in the gut. Second, given that much of the Western diet now contains Roundup herbicide contaminated food, including wheat – where Roundup is used as a pre-harvest dessicant, virtually guaranteeing it is contaminated with it despite being non-GMO – there is likely an amplifying effect of this pathogenic bacteria in those who consume both wheat and GMO food (i.e. synergistic toxicity). This may help to explain why the mass introduction of GMOs over the past decade has contributed to the explosion in diagnoses of gluten sensitivity.
Additionally, a recent article by Dr. Kelly Brogan, MD, discussed how the hunter-gatherer microbiome is conspicuously low in the Clostridium bacteria family, based on research into the modern hunter-gatherer Hadza gastrointestinal flora. This study indicates that for much of our evolution – the vast majority of it – Clostridium was not present in significant quantities in our bodies, likely because their diet did not encourage it.
From the perspective of our ancestral microbiome, modern humankind has become almost a new species due to our reliance on novel new ‘foods’ like wheat and agrochemical contaminated GMOs that have contributed to the development of a relationship with strains of bacteria that were alien to us, for some populations, even 100 years ago. The microbiome’s genome is 99% larger than our genome – containing 2 million protein coding genes versus only 23,000 for the human body alone. The shift towards pathological strains may have to do both with a radical change in the human diet to a grain-based — and particularly wheat-based diet – and, again, the ever-expanding consumption of Roundup herbicide laden foods.
This study adds to a growing body of research showing that wheat is toxic to everyone, and not only to those with celiac disease. By forcing our body to become inhabitants of strains of bacteria that we have never before needed to occupy our bodies, and which are capable of doing great harm, it can lead to a wide range of health problems, such as infections and intestinal disases, that conventional medical thinking never connects to the diet. While some of the strains that degrade gluten are non-pathogenic (e.g. 39% were from the mostly beneficial Lactobacillus family), taken as a whole, the discovery that a variety of Clostridium strains (as well as related potentially pathogenic strains from genuses such as Klebsiella and Staphylococcus) thrive in a wheat-based diet, and adding in the fact that GMO foods further contribute to their overgrowth, it seems that the pathway towards optimal health requires the elimination of both.
Now that celiac disease has been allowed official entry into the annals 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, it also pulls the rug out from under one of the health food industry’s favorite poster children since high concentrations of WGA is found in “whole wheat,” including its supposedly superior sprouted form. Below the radar of conventional serological testing for antibodies against 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 connected with health or illness, even when their consumption may greatly reduce both the quality and length of our lives.
Although significant progress has been made in exposing the dark side of wheat [1] over the past decade, gluten receives a disproportionate share of the attention. Given that modern bread wheat (Triticum aestivum) is an allohexaploid species containing six 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. [2] What is unique about WGA 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 within 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. Therefore, 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, which function much like “invisible thorns.” Cooking, sprouting, fermentation and digestion are the traditional ways in which people, for instance, deal with the various anti-nutrients found within this family of plants, However, 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 (as used in bowling bowls) and human hair so strong, flexible and durable. Like synthetic pesticides, lectins are extremely small, resistant to decomposition by living systems, and tend to accumulate and incorporate 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, 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 sugar-binding proteins 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 from and attach to the surface of cells. In the case of WGA, the two glycoproteins it selects, 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 depends 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 at the top to the alimentary tube at the bottom, 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 perfectly designed WGA 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. In the short term, they may effectively anesthetize us 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. In a previous article on the topic, The Dark Side of Wheat: New Perspectives on Celiac Disease and Wheat Intolerance, we explored the role that these psychotropic qualities in grains played in ushering in civilization at the advent of the Neolithic transition, around 10,000 BC. No doubt the narcotic properties of wheat is the primary reason why suspicions about its toxicity have remained merely speculative 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 nourishment from the soil, its roots are challenged with fungi and bacteria that seek to invade the plant. In its quest for sunlight and other nourishment 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 retains 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 one 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 Centers for Disease Control and Prevention, 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 purest 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 that occuring 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 can 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 nonsteroidal 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’ worth of 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 both palliative supplements and medicines.
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 (nanomolar) concentrations, 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 species[5] 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 rats[7] and 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 the immunoglobulins 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 sheath[14] and is capable of inhibiting nerve growth factor [15] 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-mitogenic [17] activities. WGA may prevent DNA replication[18] 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 inhibit with digestion and 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 removes 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 cytoskeletal 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 neuraminidase enzyme for viruses and the sialic acid binding sites on the WGA lectin.Once the influenza virus and WGA lectin 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 replicate itself, with the result that our immune system must attack its own virally transformed cell, 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 nonetheless result in autoimmunity.
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 we separate from our infatuation with wheat, we will grow more sensitive to our bodies’ true needs and discover far more suitable forms of nourishment that nature has not impregnated with such high levels of addictive and potentially debilitating proteins.
ARYAN'S BLOG 