Alternate Nostril Breathing

Today, I have a great yogic technique that I want to share with you. It’s breath work that yogis use to control their moods and energies.

When we are distressed, we take quick, shallow breaths.

When we are relaxed, we take deep, full breaths.

When we practice regulating our breathing patterns, we improve our mental and physical state.

This technique is called Alternate Nostril Breathing.

The nerves going out from the two brain hemispheres cross at the level of the eyebrows. The left hemisphere connects to the right side of the body and right nostril, and the right hemisphere to the left side of the body and left nostril.

Right nostril breathing (Coffee Replacer).
It activates qualities of left brain: the Sun energy—warming, projective, concentrative, alert, and action oriented.screen-shot-2016-09-09-at-9-08-51-pm

  1. Have the left hand in Gyan mudra (touch thumb with index finger) relax on lap
  2. Raise your right hand, use the index finger  to close your left nostril
  3. Slowly inhale through the right nostril
  4. Eyes can be closed or 1/10 open looking at tip of nose
  5. Long deep breaths for 3 minutes
  6. To end you take a deep breath in with both nostrils, hold the breath, for a count of 10, then release.

Left nostril breathing (Calm Inducer). 
It activates right brain qualities: the Moon energy, calmness, receptive, cooling. Best to use before bed or anxiety.screen-shot-2016-09-09-at-9-08-56-pm

  1. Use the thumb on your right hand to cover your right nostril
  2. Breathe slowly through your left nostril
  3. Eyes can be closed or 1/10 open looking at tip of nose
  4. Long deep breathing for 3 minutes

Try RIGHT in the morning, and LEFT one before bed, and enjoy the powerful effects of this breath.

Happy Breathing!!

12 things that you can do immediately to improve your body’s circadian clock

Alignment is the key to health.  One aspect of many people’s lives that is out of alignment is their sleep and wake patterns.  One of the greatest detriments to a person’s health is a poor rest and recovery routine.  This short video will go over some the of the things that you can do to optimize your natural clock.  By doing so, you will have deeper sleep, wake up more refreshed, have better mid-day energy, better mental clarity, and natural weight loss.

Here are 12 things that you can do immediately to improve your body’s circadian clock.

  1. Wake up and go to sleep at the same time every day.  Ideally, asleep by 10 pm and up around 6 am.
  2. Use a salt lamp in your bedroom as a way to reset your circadian clock.  Turn it on in the morning and after the sun sets at night, candles are also an option.  Avoid full spectrum light after sunset.
  3. Be sure to get mid-day sunlight, this will help increase serotonin (happy) and melatonin (sleep).
  4.  Eliminate exposure to phones, tablets, computers, and television 2 hours before designated bedtime
  5. Sleep in completely dark room, you should not be able to see your hand in front of your face
  6. Avoid excessive fluid intake after 8 pm
  7. Avoid opening the mail or watching the news in the evening
  8. Avoid checking and responding to email in the evening
  9. Settle any conflicts before going to bed
  10. Use lavender essential oils to help promote calm
  11. Practice deep breathing exercises before bed to help you relax, click here for more info
  12. If you use a computer, download f.lux at as a digital filter for your screen

Electromagnetic Fields and Radiation: A hidden source of stress on the body

Some of the most overlooked stressors are electromagnetic fields (EMF) radiation and radio frequency radiation. On a daily basis, we are bombarded with radio frequencies and EMFs from televisions, computers, Wi-Fi signals, cellular phones and other electronic devices that we carry around like an extra limb. Even when we are travelling, we are exposed through cars, buses, and airplanes. The frightening aspect of EMF and radio frequency radiation is the fact that it simply has not existed long enough to allow us to know what the long term consequences really are. While the research in this area is still young, EMF radiation has been indicated as possible contributor to multiple types of cancer, Alzheimer’s disease, Parkinson’s disease, headaches, low sperm count, impaired immune function, mood disorders, and sleep disorders to name a few. One thing we do know conclusively is if there is EMF near us, our body is completely exposed. At this point in time, the National Institute of Environmental Health Sciences has identified EMF as a possible carcinogen. More information on EMF can be found at World Health Organization EMF Project ( 

This image below is a great illustration of the power and frequency of different electromagneticspectrums that we all exposed to (Photo courtesy of:

Hans Selye, considered the father of the concept of stress found that our response to stress typically goes one of two ways. The first step is the alarm stage where we perceive the stressor and our sympathetic nervous system (called the “fight or flight” system) gets activated. This phase can be defined by physiologic processes such as an increase in heart rate, inhibition of digestive function, constriction of blood vessels, dilation of the pupils, and dilation of the blood vessels for muscles. The second step is the resistance phase. This phase is characterized by the body adapting to the stressor and using resources such as the body’s natural coping mechanisms to defend off the stressor and move into the recovery phase. However, prolonged exposure to the stressor can deplete our resources and literally exhaust our body to move it into the second pathway: exhaustion. Selye indicated that this stage alone can be a trigger for a myriad of health conditions such as ulcers, gastrointestinal bleeding, and cardiovascular manifestations. If the stressor persists for long enough, it can ultimately lead to death. Since EMFs are all around us, these are stressors that are always there without our awareness and can be a hidden contributor to several pathologic processes.

One key point to remember is that not all stress is bad stress (“distress”). There is also good stress (“eustress”) which we need to move forward in our life and grow physically, mentally, emotionally and spiritually. Examples of eustress include physical exercise (including sports), getting married, watching a horror movie, going shopping, travelling, and getting a promotion at work. However, for individuals with compromised adrenal function (for more on adrenal fatigue visit our more detailed article), even a positive stressor such as physical exercise may be enough to cause distress. This further highlights the importance of minimizing EMF exposure and actively working to avoid this hidden factor can be vital in achieving optimal long-term health. Below I share 10 not-so-common tips to protect you from EMF that are highly effective and easy to implement:

  1. Turn off your Wi-Fi before you go to sleep. We are exposed to Wi-Fi signals on a daily basis, from coffee shops to malls to our own homes. If it is not a life or death situation, your Wi-Fi should be turned off before bed.
  2. Turn off your cell phone or at least put it into airplane mode. This terminates all signals coming and going from your cell phone and allows you to be protected while you sleep. This action step is extremely important as the vast majority of cell phone owners keep their phone near their bed in case of an emergency call or to use the alarm clock feature.
  3. Ditch the alarm clock, especially if it has a bright backlight so you can see the time all through the night. Not only will it interfere with your sleep by constantly reminding you what time it is, the light itself from the alarm clock will inhibit your ability to get deep and efficient sleep. Sleeping in a pitch-black environment is essential to waking up rested.
  4. Switch out your cordless phones for its predecessor. While this may not be the most convenient step, sticking to a landline phone will help limit your EMF exposure.
  5. Use a wired headset for any cell phone conversations. While you can’t always prepare to have a headset plugged in and ready to go, if you know you have a call to make, use a headset. This is an extremely cheap fix with a huge return on your investment.
  6. Buy EMF filters for all your outlets. These can be found online and are relatively cheap way to prevent your outlets from creating EMF.
  7. Unplug all electronics near your bed such as lamps before going to sleep. If you require a bedside light source, I recommend a Himalayan salt lamp which is a far more natural light to get you ready for bed.
  8. Invest in EMF protective clothing, especially if you are pregnant. You can find everything from hats to underwear and maternity clothing that actually blocks EMF.
  9. Move your furniture away from the wall. Even the wiring in your wall emits EMF and this can be dissipated by simply moving your furniture 3-6 inches from the wall. If you are building a new wall (new project or renovation), putting all your wires in piping can permanently block EMF from being created.
  10. The final step is simply to practice awareness. Be aware of how much you are using your cell phone, how close you’re sitting to the router and how much time you spend surrounded by EMF.

Given the fact that we live in a time where electronics have become a requirement for basic day to day requirements such as lighting and heating our homes, complete avoidance is not the goal and that could create another stressor in itself. By practicing awareness, you are protecting yourself from the unnecessary EMF that is completely avoidable.

Phases of Digestion

Phases of Digestion

Your digestive system will process 170,000 pounds of food over the course of your life.  Your digestive system has more nerve endings than your brain.  These facts are amazing and helps us to realize how critical the digestive system is to human health.  One of the most important functions of your digestive system is to physically and chemically break down food to allow for absorption further down the digestive tract.  What is the point of eating all this healthy food if your body cannot break it down properly to get the nutrients that it needs to benefit you?  We feel the digestive system is one of the most important yet overlooked systems in your body.

A simple way to think about digestion is to equate it to a car wash.  Each phase in the car wash is critical and dependent on the previous phase being completed.  These steps must occur in the right order.  You would never dry the car before it’s been soaped.  So let’s break the digestive process down so that you have a better understanding of how this amazing sequence of events takes place and turns your food into nutrition to fuel your body.
Digestive Health

Phase 1 – Food for Thought

Digestion starts in the brain.  The smell and anticipation of food triggers the brain and digestive system to start releasing enzymes and gastric juices to prepare for the incoming meal.  It is important that you are in a calm and stress-free environment when you eat.  This will keep your body in the “rest and digest” mode.

Phase 2 – Chew Your Food: your stomach does not have teeth!

Mom was right, chewing your food is good for you, but she may not have told you why.  Chewing your food is one of the most critical steps to digestion.  The physical crushing of food in your mouth breaks increases the surface  area of your food and unlocks the nutrients in the food for further digestion in the stomach. bigstock-Assorted-metal-gears-on-white-17158397Chewing your food also stimulates stomach secretions and mixes your saliva with your food to start the breakdown of carbohydrates. This critical step is not reproduced anywhere else and therefore is critical to the process.  If you food is not properly chewed it will disrupt the entire process that follows, there is nothing that can replicate this step for you.

Phase 3 – Stomach

When food enters the stomach, your stomach starts to secrete hydrochloric acid and digestive enzymes that work mainly on breaking down protein.  The hydrochloric acid also sterilizes your food stomach to prevent bugs that may be in your food from entering your bloodstream.

A common reason for heartburn is a lack of stomach acid secretion or dilution of enzymes.  This results from not chewing your food, or drinking lots of water with your food.  Food remains partially digested and starts to rot. This rotten food becomes acidic (lactic acid), which is acidic enough to burn your esophagus, but not acidic enough to digest your food properly. For this reason, in our office, we often prescribe digestive enzymes that actually acidify the stomach contents.

Phase 4 – Pancreas

The next step once the food has been sterilized and acidified is to further break down that food via the release of pancreatic enzymes.  The pancreatic enzymes also alter the pH of the food to make it more alkaline in preparation for entry into the jejunum.


Phase 5 – Gallbladder Secretion

The final major step in digestion takes place once bile is released to emulsify fats.  These fats are chemically broken down by bile so that they can be absorbed.  The gallbladder does not make bile, it stores it.  Bile is made from cholesterol and toxins that are neutralized by the liver.  Bile not only digests fats but it further sterilizes the bowel and promotes regularity.

The physical and chemical breakdown of food is critical to proper digestion and absorption. The problem with undigested food is that it is these food particles can leak into the bloodstream. Then the immune system will recognize that food particle as an invader. This is where lots of food sensitivities come from. This immune response can also increase inflammation and raise blood sugars, causing a system-wide reaction.

Woman choosing between healthy food and caloric food

What can you do to help with proper digestion?

  • Choose the right foods
  • Chew your food thoroughly
  • Don’t drink more than 8 oz. of fluid with meals
  • Eat in a relaxing environment
  • Eat fresh fiber first
  • Eliminate food allergens (get tested)
  • Identify and eliminate any microbes or parasites
  • Get a comprehensive stool test to identify digestive system health

At the Onna Lo MD Clinic we help you get to the underlying cause of your digestive issues, instead of just treating the symptoms.  We help you find out WHY you don’t feel well and what you can do about it.

A Functional Medicine Approach to Adrenal Fatigue

Adrenal fatigue is the common name for a set of symptoms that result from the adrenal glands being worked to exhaustion. For the majority of cases, adrenal fatigue is secondary to some other underlying health issue such as chronic, hidden inflammation.  Stress can come in a variety of forms, but your body’s response is the same.  It can take years for your adrenal glands to fail to meet the demands of your daily life, ultimately resulting in adrenal fatigue.

If you’re suspecting that you have adrenal fatigue.  Ask yourself if you suffer from these adrenal fatigue symptoms;

  • get tired for no reason
  • have trouble getting up in the morning
  • need caffeine or energy drinks to keep goingAdrenal Fatigue
  • crave either salty or sweet snacks
  • either have trouble falling asleep or staying asleep
  • chronic allergies
  • never get sick
  • get sick often
  • poor memory
  • poor concentration
  • depression
  • menstrual cycle irregularities
  • chronic pain
  • slow healing from injuries
  • bruise easily
  • inability to handle stress

If you answered yes to any of these questions then consider adrenal fatigue.

The Anatomy of Adrenal Fatigue

The adrenals are two small glands, each about the size of an almond, that are located above the kidneys. The adrenals have one of the highest rates of blood flow per gram of tissue, and the highest content of vitamin C per gram of any tissue in the body. Each adrenal gland is composed of two separate functional entities. The outer zone, or cortex, accounts for 80% to 90% of the gland and secretes adrenal steroids (cortisol, DHEA-S, aldosterone and small amounts of sex hormones). The inner zone, or medulla, comprises 10% to 20% of the gland and secretes the catecholamines (adrenaline and nor-adrenaline). Cortisol, DHEA, and adrenaline are the three main adrenal stress hormones. These hormones help you to buffer stress and adapt to everyday life demands. We’d love to talk to you about natural adrenal supplements.

Under stress, healthy adrenals increase their output of cortisol and DHEA to enable you to preserve health. They also secrete adrenaline, giving you a boost of energy when needed (ie mother lifting car off of a baby). If this becomes chronic, the adrenals can no longer keep up with the demand, and DHEA levels begin to fall, signifying adrenal fatigue.  In addition, the over-secretion of adrenaline can cause you to feel anxious and nervous.  Complaints of insomnia, fatigue, depression, irritability, and digestive difficulties are also common.  As adrenaline surges during stress, digestive enzymes are simultaneously lowered, and blood sugar levels rise.  As this becomes a more chronic occurrence, the results of high cortisol and adrenaline levels from prolonged stress wreak havoc on the body. Essentially under stress all systems that are required for rest, repair, and digestion shut down.

“Adrenal fatigue is the end-stage of a poorly adapted stress response that can take years to break down.”

Below are areas of the body that are negatively impacted by adrenal exhaustion and the chronic stress response that causes it.

Energy Production

Abnormal adrenal function can alter the ability of cells to produce energy for the activities of daily life. People who have a hard time rising in the morning, or who suffer from low energy throughout the day, often have abnormal adrenal rhythms, adrenal fatigue, and poor blood sugar regulation. The maintenance of a stable blood sugar level depends on food choice, lifestyle, adrenal function, and insulin activity.

Muscle and Joint Function

Abnormal adrenal rhythms are known to compromise tissue healing. Reduced tissue repair and increased tissue breakdown can lead to muscle and joint wasting with chronic pain.

Bone Health

The adrenal rhythm determines how well we build bone. If the night and morning cortisol levels are elevated, our bones do not rebuild well, and we are more prone to osteoporosis. Stress is the enemy of the bones. In postmenopausal women, the effect of stress worsens due to female hormone imbalances.

Immune Health

Various immune cells (white blood cells) cycle in and out of the spleen and bone marrow. The immune system trafficking follows the cortisol cycle. If the cycle is disrupted, especially at night, then the immune system is adversely affected. Short- and long-term stress is known to suppress the immune response in the lungs, throat, urinary tract and intestines. With reduction in the surface antibody (called secretory IgA), the resistance to infection is reduced and allergic reactions increase.

Sleep QualityAdrenal fatigue

In sleep-deprived individuals, the mean cortisol levels are elevated, and the quiescent period is shorter. Evening cortisol level is increased in patients with insomnia, affecting the first part of the nocturnal sleep period, increasing risk for depression. Chronic lack of REM sleep can reduce a person’s mental vitality, vigor and induce depression.


Couples with high level of stress markers are less likely to succeed in conceiving. Stress alters the brain signals that trigger the ovaries to release eggs each month, so women under non-stop stress ovulate fewer eggs than less stressed women. Stress can also affect testosterone level and sperm production in men. Helping couples to de-stress while trying to conceive can impact their success rate.

Skin Regeneration

Human skin regenerates mostly at night. With higher night cortisol values, less skin regeneration takes place. Thus normal cortisol rhythm is essential for optimal skin health.

Thyroid Function

The level of cortisol at the cellular level controls thyroid hormone production. Often, hypothyroid symptoms such as fatigue and low body temperature are due to a stress or adrenal fatigue.  Chronic stress will convert thyroid hormone to it’s inactive form (reverse T3) and shuts down the production of TSH.

Gluten Sensitivity and Stress Response

Approximately 12-18% of the U.S. population suffers from a genetic intolerance to grains, such as wheat, rye or barley contained in cereals, breads and pasta. A high incidence occurs in people with Celtic, Nordic, non-Caucasian and Mediterranean ethnicity. The gut becomes inflamed within 30 minutes after consuming grains, and this can lead to an adrenal stress response, increased cortisol and reduced DHEA.

Diabetes - BrainMemory

Sustained stress adversely affects brain function and memory processing. Too much cortisol interferes with the functioning chemicals the brain uses for its cellular intercommunication as well as decrease the function of the hippocampus, which is the part of your brain that forms memories. Chronic long term stress, with increased cortisol level at night, makes it perplexing to think, organize, and store new memories or retrieve long-term ones.

Chronic Fatigue Syndrome (CFS)

A common adrenal fatigue issue in CFS is impaired corticotrophin release.  As a result, low cortisol and eventual adrenal atrophy may be observed.  Simultaneous use of several therapies can help improve the debilitating effects of CFS.

Glycemic Dysregulation

Chronic low blood sugars can impair normal adrenal function by repetitive over-stimulation of cortisol production. Recurring exposure to high cortisol will impair insulin activity, and invariably lead to insulin resistance and beta-cell exhaustion (diabetes).

Allergies/Autoimmune Disorders

More than fifty years ago, Dr. W. Jefferies (author of Safe Uses of Cortisol) discovered that patients with environmentally triggered allergies and autoimmune diseases dramatically benefited when given cortisol for other purposes. More recently, German researchers reported that disruption of the adrenal axis and cytokine relationships lead to predisposition and aggravation of autoimmune diseases.


Several recent publications report a hyperactive HPA axis in depressed patients. Elevated midnight salivary cortisol is now considered one of the best tests in diagnosing endogenous depression. Other anomalies in cortisol rhythm usually accompany the midnight elevation. On the other hand, cortisol elevations and rhythm disruptions throughout the day are typical of attention deficit disorders (ADD).


Our Clinic’s Approach to Adrenal Fatigue

As you can see, a chronic stress response that eventually develops into adrenal fatigue has a negative impact on virtually every aspect of health. Stress is reaching an epidemic proportion due to our fast-paced lifestyle and is at the heart of virtually all chronic disease.  As mentioned earlier, adrenal fatigue is secondary to a chronic stress stimulus. These stressors can be in the form of:

  • Dysbiosis (bacterial imbalance in the gut)
  • Food Sensitivities
  • Chemical Sensitivities
  • Chronic Pain
  • Blood Sugar issues such as reactive hypoglycemia and diabetes
  • Environmental factors such as quality of air, food, and water, as well as toxin exposure
  • Fast-paced lifestyle
  • Poor relationships

As Functional Medicine Providers, it is our job to dig through the dirt to find the underlying cause of your stress response gone awry.  Not only do we tell you WHY you don’t feel well, but teach you what YOU can do about it.  Let us help you develop a strategy to conquer adrenal fatigue and restore your vitality and quality of life.

Let us help navigate you towards better health!

Gluten Sensitivity

It is almost impossible to discuss health and nutrition these days without discussing the topic of gluten with our patients. Are food companies merely taking advantage of vulnerable consumers looking for the latest fad or is there merit to “going gluten-free”? With all the questions that we get surrounding gluten, we at the Living Proof Institute think that it is necessary to set the record straight. By now, many of you have certainly heard of celebrities following a gluten free diet, or have heard of someone’s health turning around as a result of gluten elimination. This report will give you a deeper understanding of what gluten is, where it is found, and the implications to your health.

The Gluten Free Industry

In the last few years, sales of gluten-free food has grown 27% and is estimated at being a $4.2 billion market in 2012. To say this is an exploding market is an understatement. Many foods have always been gluten free, but are now being labelled as such. Gluten free foods include nuts, seeds, dairy, meats, eggs, vegetables, fruits and several grains. To be considered Gluten-free typically means that a food must be processed in a separate plant that is certified Gluten-free. Technically, gluten-free means that a food has less than 30 parts per million (ppm) of gluten. Those with Celiac disease and severe reactivities to gluten can react at 3 ppm. Often the certification process is what accounts for the increased cost of gluten free foods. Also keep in mind that wheat is heavily subsidized unlike other gluten-free grains such as amaranth.

As consumer demand grows there will be more and more gluten-free products coming to the market. Our position on these foods is to consume them in extreme moderation. Replacing one grain with another will still have a negative impact on blood sugar, insulin and weight. Gluten free items should be used as a last solution, not a staple in your diet. You can find hundreds of recipes that are all gluten free at

What is Gluten?

Gluten is a protein molecule found in wheat, barley, rye, spelt, kamut, and 98% of oats (due to cross-contamination). Gluten literally means “glue”. Gluten is what gives bread its elasticity and texture. Modern wheat has been cultivated to contain higher amounts of gluten. This is great for manufacturers, at the price of your health. Until recently, there was no genetically modified (GM) wheat on the market. GM wheat was modified to “turn off” the gene that is responsible for the immune system response in a person with Celiac’s Disease. The problem with this is that that particular gene is also responsible for expressing other genetic traits. So the effects on a genetic level are unknown. Some animals that have consumed GM wheat have been reported to develop liver failure.

Hidden Sources of Gluten

Some hidden or unknown sources of gluten are soy sauce, food starches, food emulsifiers, food stabilizers, artificial food coloring, malt extract, beer, some red wines, seasonings and sauces. When in doubt, call the manufacturer or look for the gluten free label. Products that are manufactured in a plant that processes gluten may also be contaminated due to shared equipment.

Gluten Sensitivity and Chronic Illness

It is estimated that there are at at least 18 million Americans that have a gluten sensitivity. We feel that number is grossly underestimated, but it is difficult to estimate the breadth of the problem since many people are misdiagnosed and never receive the right treatment.

Celiac’s disease gets the lions share of attention when talking about gluten, we will discuss the many spin-off conditions that arise from gluten exposure later. To date, research indicates that over 200 diseases are associated with gluten sensitivity. These can range from seizures to skin conditions. The list would surprise you.

What is Gluten Sensitivity?

Gluten sensitivity can often be challenging for an untrained practitioner to identify. A sensitivity can cause subtle to severe symptoms depending on the patient. Another unfortunate fact regarding sensitivities is that they often occur outside of the digestive system, such as, joints, skin and nervous system. These reactions may also be delayed (30 minutes – 4 days), making it challenging for one to recognize gluten as the offending agent.

Once ingested the gluten molecule is particularly difficult for your body to digest. This undigested gluten can wreak havoc on the immune system all the way from the mouth to the anus. When ingested, anti-bodies to gluten are produced and gluten is “tagged” by the immune system as a foreign invader. This type of subtle and delayed reaction is known as an IGG response, much different than a IGE response often associated with foods like peanuts.

My Parents ate wheat and They seemed Fine

We have been eating wheat for generations, but not the commercial wheat that is grown today. By modifying wheat to contain more gluten than it originally did, the agriculture business has vastly increased our exposure. Also, the wheat a person eats today goes through a process called de-amidation, which your immune system happens to not like and it causes more of an immune reaction. The Standard American Diet (SAD) has very little nutritional value and our society is much more stressful, which contributes to the breakdown of our immune tolerance for substances like gluten. Lastly, without proper nutrition, our bodies have a tendency to make less of the enzymes required to digest and break down gluten particles. Chronic exposure combined with a compromised nutritional status and immune health seem the be the perfect storm for chronic illness related to gluten.

My doctor told me I Do Not Have Celiac Disease

As mentioned earlier, when a person hears the word gluten it is synonymous with Celiac’s Disease. However, the research clearly states that gluten sensitivity being regarded principally as a disease of the small bowel is a historical misconception. The research also demonstrates that for every gluten sensitive patient with symptoms of an enteropathy (Classic Celiac Disease), there are 8 people with no GI symptoms!

Thinking beyond the Gut

Other organs and areas that have been demonstrated to be involved in gluten sensitivity are the joints (Rheumatoid Arthritis and Ankylosing Spondylitis), the heart, thyroid, bone, and most notably the brain, cerebellum, and neuronal synapsins (think Multiple Sclerosis and Cerebellar Ataxia). There is a connection with gluten sensitivity and type 1 diabetes, osteoporosis, Addison’s disease, and ADHD. Gluten sensitivity has also been demonstrated to play a critical role in infertility and stillbirths. Lastly, people with a gluten sensitivity are 10 times more likely to develop an autoimmune disease. As you can see, the notion that gluten only affects the small bowel is archaic to say the least, it is time for a radical paradigm shift.

Gluten Sensitivity and Autism

80% of children diagnosed with autism not only produce antibodies to gluten, they also produce antibodies to their brain. This is a mind blowing number of children that are being mismanaged, misdiagnosed, and mistreated. How can a solution so simple, so effective and so cheap be ignored? At The Living Proof Institute going gluten free is our first line of therapy for our autistic patients.

Why has my doctor Never Mentioned Gluten Sensitivity? What shall I do?

The answer is easy, most clinicians are not trained to look at a gluten sensitivity when areas other than the GI tract are affected. Also, when most clinicians run an antibody test they are only looking for the alpha-gliadin marker. The problem with that is that only around 50% of celiac patients have antibodies to the alpha-gliadin portion of wheat, the other half are sensitive to a different portion.

What type of testing is best for Gluten Sensitivity?

The blood test that we recommend looks at 12 different peptides of gluten. Luckily, there is testing out there that is not only more accurate than the traditional blood test, but also easier to administer because it is done through saliva. This can be an excellent screen for people suspecting gluten sensitivity.

Despite advanced testing, it should be noted that the gold standard for any type of allergy or sensitivity is complete elimination for up to 6 months.

When going Gluten-free goes wrong

In rare instances patients may report that their symptoms worsen when going on a gluten free diet. There are three possible explanation for this. Firstly, gluten binds to opioid receptors in the brain and literally acts like a drug. Similar to coming off of any addictive substance there will be a withdrawal period. This may last a few days.

Secondly, around 36% of people that go gluten free are still getting accidental exposure. This exposure may be from cross contamination, poor technique at restaurants, lack of due diligence and the occasional ingestion such as at birthdays and celebrations.

Lastly, when people go gluten-free, they usually start ingesting other grains in place of gluten. In some cases, this may initiate an immune response very similar to eating gluten. This is a notion called cross-reactivity. Cross-reactivity is the ability of an antibody to bind with similar-looking parts on different proteins called epitopes. This phenomenon is also known as molecular mimicry. Up to 82% of gluten sensitive patients have antibodies to other foods including rice, milk, beef, sheep, and eggs. Other studies have identified cross-reactivity with chocolate, sesame, hemp, rye, kamut, buckwheat, sorghum, millet, spelt, amaranth, quinoa, yeast, tapioca, oats, coffee, corn, and potatoes. As you can see, a lot of the foods that people use to replace gluten in their diet are on this list. Luckily, there is a test that we recommend that looks at these cross-reactivities as well as other common food sensitivities in those that are unresponsive to gluten elimination.

Our Approach to Gluten Sensitivity

In the face of so much research and empirical data it is difficult to ignore the elephant in the room. Going gluten free can be an extremely easy dietary change with the right guidance and by taking small efforts to read food labels more closely. When in doubt stick to a whole food diet that excludes processed and packaged foods. Refer to our recipe website for food options if you have a gluten sensitivity.

By listening to your unique story, we help you uncover why you don’t fell well and what you can do about it. Call us today to schedule a personal health consultation.


  1. Vojdani A, O’Bryan T, Green J, McCandless J, Woeller K, Vojdani E, Nourian E, Cooper E, Immune Response to Dietary Proteins, Gliadin and Cerebellar Peptides in Children with Autism, Nutritional Neuroscience, Volume 7 Number 3 (June 2004), pp. 151–161.
  2. Marks J, Shuster S, Watson AJ. Small bowel changes in dermatitis herpetiformis. Lancet 1966; 2:1280- 1282.
  3. Cooke WT, Thomas-Smith W. Neurological disorders associated with adult celiac disease. Brain 1966; 89:683-722.
  4. Hvatut M, Kanerud L, Hällgren R, Brandtzaeg P. The gut-joint axis: cross-reactive food antibodies in rheumatoid arthritis. Gut 2006; 55:1240-1247.
  5. Kjeldsen-Kragh J, Hvatum M, Haugen M, Forre O, Scott H. Antibodies against dietary antigens in rheumatoid arthritis patients treated with fasting and a one-year vegetarian diet. Clin Exp Rheumatol 1995; 13:167-172.
  6. Koot VC, Van Straaten M, Hekkens WT, Collee G, Dijkmans BA. Elevated level of IgA gliadin antibodies in patients with rheumatoid arthritis. Clin Exp Rheumatol 1989; 7:623-626.
  7. O’Farelly C, Marten D, Melcher D, McDougall B, Price R, Goldstein AJ, Sherwood R, Fernandes L.A. VOJDANI ET AL.Association between villous atrophy in rheumatoid arthritis and a rheumatoid factor and gliadin-specific IgG. Lancet 1988; 2:819-822.
  8. Quan CP, Berneman A, Pires R, Avrameas S, Bouvet JP. Natural polyreactive secretory immunoglobulin A autoantibodies as a possible barrier to infection in humans. Infect Immun 1997; 65:3997-4004.
  9. Frustaci A, Cuoco L, Chimenti C, Pieroni M, Fioravanti G, Gentiloni N, Maseri A, Gasbarrini G. Celiac disease associated with autoimmune myocarditis. Circulation 2002; 105:2611-1618.
  10. Chimenti C, Pieroni M, Frustac IA. Celiac disease in idiopathic dilated cardiomyopathy. Ital Heart J 2001; 2:658-659.
  11. Counsell CE, Taha A, Ruddell WS. Coeliac disease and autoimmune thyroid disease. Gut 1994; 35:844- 846.
  12. Natter S, Granditsch G, Reichel GL, Baghestanian M, Valent P, Elfman L, Gronlund H, Kraft D, Valenta R. IgA cross-reactivity between a nuclear autoantigen and wheat proteins suggests molecular mimicry as a possible pathomechanism in celiac disease. Eur J Immunol 2001; 31:918-928.
  13. Pedeira S, Vazquez H, Sugai E, Niveloni S, Smecuol E, Mazure R, Flores D, Maurino E, Bai JC. Clinical significance of anti-smooth muscle antibody (SMA) fluorescence in patients with celiac disease. Gastroenterol 2000; 118:A363.
  14. Sugai E, Cherñavsky A, Pedreira S, Smecuol E, Vazquez H, Niveloni S, Mazure R, Mauriño E, Rabinovich GA, Bai JC. Bone-specific antibodies in sera from patients with celiac disease: characterization and implications in osteoporosis. J Clin Immunol 2002; 22:353-362.
  15. Vazquez H, Mazure R, Gonzalez D, Flores D, Pedreira S, Niveloni S, Smecuol E, Mauriño E, Bai JC. Risk of fractures in celiac disease patients: A cross-sectional, case-control study. Am J Gastroentero1 2000; 95:183-189.
  16. Pratesi R, Gandolfi L, Friedman H, Farage L, De Castro CAM, Catassi C. Serum IgA antibodies from patients with coeliac disease react strongly with human brain blood-vessel structures. Scand J Gastroenterol 1998; 33:817- 821.
  17. Volta U, De Giorgio R, Petrolini N, Stangbellini V, Barbara G, Granito A, De Ponti F, Corinaldesi R, Bianchi FB. Clinical findings and anti-neuronal antibodies in celiac disease with neurological disorders. Scand J Gastroenterol 2002; 137: 1276- 1281.
  18. Hadjivassiliou M, Grünewald R, Sharrack B, Sanders D, Lobo A, Williamson C, Woodroofe N, Wood N, Davies-Jones A. Gluten ataxia in perspective: epidemiology, genetic susceptibility and clinical characteristics. Brain 2003; 126:685-691.
  19. Abele M, Schöls L, Schwartz S, Klockgether T. Prevalence of antigliadin antibodies in ataxia patients. Neurology 2003; 60:1674-1675.
  20. Hadjivassiliou M, Boscolo S, Davies-Jones GA, Grünewald RA, Not T, Sanders DS, Simpson JE, Tongiorgi E, Williamson CA, Woodroofe NM. The humoral response in the pathogenesis of gluten ataxia. Neurology 2002; 58:1221-1226.
  21. Hadjivassiliou M, Davies-Jones GAB, Sanders DS, Grünewald RA. Dietary treatment of gluten ataxia. J Neurol Neurosurg Psychiatry 2003; 74:1221-1224.
  22. Vojdani A, O’Bryan T, Green JA, McCandless J, Woeller KN, Vojdani E, Nourian AA, Cooper EL. Immune response to dietary proteins, gliadin and cerebellar peptides in children with autism. Nutritional Neurosciences 2004; 7(3):151-161.
  23. Alaedini A, Okamoto H, Briani C, Wollenberg K, Shill HA, Bushara KO, Sander HW, Green PH, Hallett M, Latov N. Immune cross-reactivity in celiac disease: anti-gliadin antibodies bind to neuronal synapsin I. J Immunol 2007; 178:6590- 6595.
  24. Green PH, Alaedini A, Sander HW, Brannagan TH III, Latov N, Chin RL. Mechanisms underlying celiac disease and its neurologic manifestations. Cell Mol Life Sci 2005; 62:191-199.
  25. Hilfiker S, Benfenati F, Doussau F, Nairn AC, Czernik AJ, Augustine GJ, Greengard P. Structural domains involved in the regulation of transmitter release by synapsins. J Neurosci 2005; 25:2658- 2669.
  26. Sommer C, Weishaupt A, Brinkhoff J, Biko L, Wessig C, Gold R, Toyka KV. Paraneoplastic stiff- person syndrome: passive transfer to rats by means of IgG antibodies to amphiphysin. Lancet 2005; 365: 1406-1411.
  27. Takenoshita HM, Shizuka-Ikeda M, Mitoma H, SongS-Y, Harigaya Y, Igeta Y, Yaguchi M, Ishida K, Shoji M, Tanaka M, Mizusawa H, Okamoto K. Presynaptic inhibition of cerebellar GABAergic transmission by glutamate decarboxylase autoantibodies in progressive cerebellar ataxia. J Neural Neurosurg Psychiatry 2001; 70:386-389.
  28. Zelnick N, Pacht A, Obeid R, Lerner A. Range of neurologic disorders in patients with celiac disease. Pediatr 2004; 113:1672-1676.
  29. Hadjivassiliou M, Williamson CA, Woodroofe N. The immunology of gluten sensitivity beyond the gut. Trends Immunol 2004; 25:578-582.
  30. Kumar V, Rajadhyaksha M, Wortsman J. Celiac disease associated autoimmune endocrinopathies. Clin Diag Lab Immunol 2001; 8:678-685.
  31. Funda DP, Kaas A, Bock T, Tlaskalová-Hogenová H, Buschard K. Gluten-free diet prevents diabetes in NOD mice. Diabetes Metab Res Rev 1999; 15:323-327.
  32. Westman E, Ambler GR, Royle M, Peat J, Chan A. Children with coeliac disease and insulin-dependent diabetes mellitus-growth, diabetes control dietary intake. J Pediatr Endocrinol Metab 1999; 12:433-37.
  33. Cronin CC, Shanahan F. Insulin-dependent diabetes
mellitus and coeliac disease. Lancet 1997; 349:1096- 442.
  34. Lorini R, Scotta MS, Cortona L, Avanzini MA, Vitali 
L, De Giacomo C, Scaramuzza A, Severi F. Celiac disease and type I (insulin-dependent) diabetes mellitus in childhood: follow-up study. J Diabetes Complications 1996; 10:154-159.
  35. Velluzzi F, Caradonna A, Boy MF, Mossa P, Corda G, Pinna MA, Cabula R, Lai MA, Piras E, Atzeni F, Loviselli A, Usai P, Mariotti S. Thyroid and celiac disease: clinical, serologic and echographic study. Am J Gastroenterol 1998; 93:976-979.
  36. Sategna-Guidetti C, Bruno M, Mazza E, Carlino A, Predebon S, Tagliabue M, Brossa C. Autoimmune thyroid disease and coeliac disease. Eur J Gastroenterol Hepatol 1998; 10:927-931.
  37. Venture A, Neri E, Ughi C, Leopaldi A, Citta A, Not T. Gluten-dependent diabetes-related and thyroid- related antibodies in patients with celiac disease. J Pediatr 2000; 137:263-265.
  38. Valentino R, Savastano S, Tommaselli AP, Dorato M, Scarpitta MT, Gigante M, Lombardi G, Troncone R. Unusual association of thyroiditis, Addison’s disease, ovarian failure and celiac disease in a young woman. J Endocrinol Investig 1999; 22:390-394.
  39. Selby P. Bone loss in celiac disease is related to secondary hyperparathyroidism. J Bone Mineral Res 1999; 14:652-657.
  40. Iafusco D, Rea F, Chiarelli F, Mohn A, Prisco F. Effect of gluten-free diet on the metabolic control of type I diabetes in patients with diabetes and celiac disease. Diabetes Care 2000; 23:712-713.
  41. Hadjavassilios, M., Gluten Sensitivity as a Neurological illness, J Neurol Neurosurg Psychiatry 2002;72:560–563.
  42. van Heel D., West J, Recent Advances in Coeliac Disease, Gut 2006;55:1037–1046.
  43. Fasano A, Catassi C., Current Approaches to Diagnosis and Treatment of Celiac Disease: An Evolving Spectrum Gastroenterology 2001;120:636-651.
  44. Goddard CJ., Gillett H R., Complications of coeliac disease: are all patients at risk? Postgrad. Med. J. 2006;82;705-712.
  45. Green PHR, Stavropoulos SN, Panagi SG, et al. Characteristics of adult celiac disease in the USA: results of a national survey. Am J Gasroenterol 2001;96:126–31.
  46. Olesen M, Eriksson S, Bohr J, Jarnerot G, Tysk C. Microscopic colitis: a common diarrhoeal disease. An epidemiological study in Orebro, Sweden, 1993-1998. Gut, 2004; 53:346-350.
  47. Gillet HR, Freeman HJ. Prevalence of celiac disease in collagenous and lymphocytic colitis. Can J Gastroenterol, 2000; 14: 919-921.
  48. Koskela RM, Niemelä SE, Karttunen TJ, Lehtola JK. Clinical characteristics of collagenous and lymphocytic colitis. Scand J Gastroenterol, 2004;39: 837-845.
  49. Corrao G, Corrazza GR, Bagnardi V, et al. Mortality in patients with coeliac disease and their relatives: a cohort study. Lancet 2001;358:356–61.
  50. Hill I Salem W, Dirks M, Liptak G, Colletti R , Fasano A, Guandalini S, Hoffenberg E, Horvath K, Murray J, Pivor M, Salem W, Seidman E, Guideline for the Diagnosis and Treatment of Celiac Disease in Children: Recommendations of the North American Society for Pediatric Gastroenterology, Hepatology and Nutrition, J Pediatr Gastroenterol Nutr, Vol. 40, No. 1, January 2005.
  51. Hadjavassilios, M, Gluten Sensitivity: from Gut to Brain. Lancet Neurol 2010; 9: 318–30.
  52. Fasano, A, Celiac Disease-How to handle a Clinical Chameleon, NEJM 348;25 June 19,2003.
  53. Arnson Y, Amital H, and Shoenfeld Y, Vitamin D and autoimmunity: new aetiological and therapeutic considerations, J of Immunology, 2005, 175: 4119–4126.
  54. Alaedini A, Okamoto H, Briani, C, Wollenberg K, Shill H, Bushara K, Sander H, Green P, Hallett M, Latov N, Immune Cross-Reactivity in Celiac Disease: Anti-Gliadin Antibodies Bind to Neuronal Synapsin I, The Journal of Immunology, 2007, 178: 6590– 6595.
  55. Bland J., Understanding the Origins and Applying Advanced Nutritional Strategies for Autoimmune Disease, Metagenics Seminar Series, 2006.
  56. Green P, Alaedini A, Sander HW, Brannagan III TH, Latov N, Chin R, Mechanisms underlying celiac disease and its Neurologic Manifestations Cell. Mol. Life Sci. 62 (2005) 791–799.
  57. Marietta E, Black K, Camilleri M, Krause P, Rogers RS 3rd, David C, Pittelkow MR, Murray JA., A new model for dermatitis herpetiformis that uses HLA-DQ8 transgenic NOD mice, J Clin Invest. 2004 Oct;114(8):1090-7.
  58. Lindqvist U, Rudsander A, Boström A, Nilsson B, Michaëlsson G., IgA antibodies to gliadin and coeliac disease in psoriatic arthritis, Rheumatology (Oxford). 2002 Jan;41(1):31-7.
  59. Humbert P, Pelletier F, Dreno B, Puzenat E, Aubin F, Gluten intolerance and skin diseases, Eur J Dermatol 2006; 16 (1): 4-11.
  60. Selva-O’Callaghan A, Casellas F, de Torres I, Palou E, Grau-Junyent JM, Vilardell- Tarrés M., CELIAC DISEASE AND ANTIBODIES ASSOCIATED WITH CELIAC DISEASE IN PATIENTS WITH INFLAMMATORY MYOPATHY, Muscle Nerve. 2007 Jan;35(1):49-54.
  61. Hadjivassiliou M, Grünewald R, Sharrack B, Sanders D, Lobo A, Williamson C, Woodroofe N, Wood N, Davies-Jones A., Gluten ataxia in perspective: epidemiology, genetic susceptibility and clinical characteristics, Brain. 2003 Mar;126(Pt 3):685-91.
  62. Hadjivassiliou M, Aeschlimann D, Grünewald RA, Sanders DS, Sharrack B, Woodroofe N, GAD antibody-associated neurological illness and its relationship to gluten sensitivity, Acta Neurol Scand. 2010 Apr 15.
  63. Eaton W, Mortensen PB, Agerbo E, Byrne M, Mors O, Ewald H., Coeliac disease and schizophrenia: population based case control study with linkage of Danish national registers, BMJ. 2004 Feb 21;328(7437):438-9.
  64. Hadjivassiliou M, Grünewald RA, Chattopadhyay AK, Davies-Jones GAB, Gibson A, Jarratt JA, et al. Clinical, radiological, neurophysiological and neuropathological characteristics of gluten ataxia. Lancet 1998;352:1582-5.
  65. J Neurol Neurosurg Psychiatry. 2006 Nov;77(11):1262-6., Hadjivassiliou M, Grünewald RA, Kandler RH, Chattopadhyay AK, Jarratt JA, Sanders DS, Sharrack B, Wharton SB, Davies-Jones GA, Neuropathy associated with gluten sensitivity.
  66. Gluten sensitivity: from gut to brain., Hadjivassiliou M, Sanders DS, Grünewald RA, Woodroofe N, Boscolo S, Aeschlimann D, Lancet Neurol. 2010 Mar;9(3):318-30.
  67. Hopper A.,, Pre-endoscopy serological testing for coeliac disease:evaluation of a clinical decision tool, BMJ. 2007 Apr 7;334(7596):729.
  68. Hill ID., What are the sensitivity and specificity of serologic tests for celiac disease? Do sensitivity and specificity vary in different populations? Gastroenterology. 2005 Apr;128(4 Suppl 1):S25-32.
  69. Memeo L, Jhang J, Hibshoosh H, Green PH, Rotterdam H, Bhagat G., Duodenal intraepithelial lymphocytosis with normal villous architecture: common occurrence in H. pylori gastritis, Mod Pathol. 2005 Aug;18(8):1134-44.
  70. Abrams JA, Diamond B, Rotterdam H, Green PH. Seronegative celiac disease: increased prevalence with lesser degrees of villous atrophy, Dig Dis Sci. 2004 Apr;49(4):546-50.
  71. Tursi A., Seronegative Coeliac Disease: a Clinical Challenge. BMJ 26 April, 2005.
  72. Rostami, K., Unforgiving Master of Non-Specificity and Disguise, BMJ 27, April 2005.
  73. Lebwold, Green P., Screening for Celiac Disease. N Engl J Med Oct.23 2003,1673-4.
  74. Freeman HJ., Pearls and pitfalls in the diagnosis of adult celiac disease. Can J Gastroenterol 2008;22(3):273-280.
  75. Bonamico M., Serologic and Genetic Markers of Celiac Disease: A Sequential Study in the Screening of First Degree Relatives, Journal of Pediatric Gastroenterology and Nutrition 42:150–154.
  76. Fasano A., Catassi C., Current Approaches to Diagnosis and Treatment of Celiac Disease: An Evolving Spectrum, GASTROENTEROLOGY 2001;120:636–651.
  77. Hadjavassiliou M., Grunewald R., The Neurology of Gluten Sensitivity:Science vs. Conviction Practical Neurology, 2004, 4, 124–126.
  78. Camarca, A.,, Intestinal T Cell Responses to Gluten Peptides Are Largely Heterogeneous: Implications for a Peptide-Based Therapy in Celiac Disease, J. Immunol. 2009;182;4158-4166.
  79. Meresse B., , Ripoche J., Heyman M., Cerf-Bensussan N., Celiac disease: from oral tolerance to intestinal inflammation, autoimmunity and lymphomagenesis, Nature Vol 2 No 1, JANUARY 2009.
  80. Bethune M.,Parallels Between Pathogens and Gluten Peptides in Celiac Sprue, Plos Pathogens Feb 2008 Vol 4: 2;e34.
  81. Ehrhardt G., Discriminating gene expression profiles of memory B cell subpopulations JEM VOL. 205, August 4, 2008.
  82. Martucci S., Corazza G., Spreading and Focusing of Gluten Epitopes in Celiac Disease GASTROENTEROLOGY Vol. 122, No. 7, 2002.
  83. Pastore L.,, Orally Based Diagnosis of Celiac Disease: Current Perspectives, J Dent Res 87(12):1100-1107, 2008.
  84. Vader W.,, The Gluten Response in Children With Celiac Disease Is Directed Toward Multiple Gliadin and Glutenin Peptides, GASTROENTEROLOGY 2002;122 :1729–1737.
  85. Green P, Cellier C, Celiac Disease NEJM 357;17 Oct 25, 2007.
  86. Leffler DA, Dennis M, Hyett B, Kelly E, Schuppan D, Kelly CP., Etiologies and predictors of diagnosis in nonresponsive celiac disease, Clin Gastroenterol Hepatol. 2007 Apr;5(4):445-50.
  87. Sicherer SH., Clinical implications of cross-reactive food allergens, J Allergy Clin Immunol. 2001 Dec;108(6):881-90.
  88. Kristjánsson G, Venge P, Hällgren R., Mucosal reactivity to cow’s milk protein in coeliac disease, Clin Exp Immunol. 2007 Mar;147(3):449-55.
  89. Bürgin-Wolff A, Hernandez R, Just M, Signer E., Immunofluorescent antibodies against gliadin: a screening test for coeliac disease, Helv Paediatr Acta. 1976 Dec;31(4-5):375-80.
  90. Ferguson A, Carswell F, Precipitins to dietary proteins in serum and upper intestinal secretions of coeliac children, Br Med J. 1972 Jan 8;1(5792):75-7.
  91. Becker CG, Van Hamont N, Wagner M. Tobacco, cocoa, coffee, and ragweed: cross-reacting allergens that activate factor-XII-dependent pathways. Blood, 1981; 58(5):861-867.
  92. Gangur V, Kelly C, Navuluri L. Sesame allergy: a growing food allergy of global proportions? Ann Allergy Asthma Immunol, 2005; 95:4-11.
  93. Kagi Mk, Wuthrich B. Falafel burger anaphylaxis due to sesame seed allergy. Ann Allergy, 1993; 71(2):127-129.
  94. Keskinen H, Ostman P, Vaheria E, et al. A case of occupational asthma, rhinitis and urticaria due to sesame seed. Clin Exp Allergy, 1991; 21:623-624.
  95. Pecquet C, Leynadier F, SaÏag P. Immediate hypersensitivity to sesame in foods and cosmetics. Contact Dermatitis, 1998; 39:313.
  96. Perkins MS. Raising awareness of sesame allergy. Pharma J, 2001; 267:757-758.
  97. Popa V, Gavrilescu N, Preda N, et al. an investigation of allergy in byssinosis: sensitization to cotton, hemp, flax and jute antigens. Brit J Industr Med, 1969; 26:101-108.
  98. Ciclitiera PJ and Ellis HJ. Relation of antigenic structure of cereal proteins to their toxicity in coeliac patients. Brit J Nutr, 1985; 53:39-45.
  99. Kasarda DD. Grains in relation to celiac disease. Cereal Foods World, 2001; 46:209-210.
  100. Simonato B, Pasini G, Giannattasio M, Curioni A. Allergenic potential of Kamut® wheat. Allergy, 2002; 57:653-654.
  101. Göhte C-J, Wislander G, Ancker K, Forsbeck M. bucksheat allergy: health food, an inhalation health risk. Allergy, 2007; 38(3):155-159.
  102. Hekkens WT. The determination of prolamins in gluten-free food. Introductory remarks. Panminerva Med, 1991; 33(2):61-64.
  103. Kim J-L, Wieslander G, Norbäck D. Allergy/Intolerance to buckwheat and other food products among Swedish subjects with celiac disease. Proc. 9th Int’l Symp Buckwheat, Prague, 2004:705-709.
  104. Lee SY, Lee KS, Hong CH, Lee KY. Three cases of childhood nocturnal asthma due to buckwheat allergy. Allergy, 2001; 56:763-766.
  105. Pomeranz Y, Marshall HG, Robbins Gs, Gilbertson JT. Protein contect and amino acid composition of maturing buckwheat (Fagopyrum esculentim moench). Cereal Chem, 1975; 52:479-484.
  106. De Maat-Bleeker F, Stapel SO. Cross-reactivity between buckwheat and latex. Allergy, 1998; 53:538-539.
  107. Sdepanian VL, Scaletsky ICA, Fagundes-Neto U, de Morais MB. Assessment of gliadin in supposedly gluten-free foods prepared and purchased by celiac patients. J Ped Gastroenterol Nutr, 2001; 32:65-70.
  108. Skerritt JH, Devery JM, Hill AS. Chemistry, coeliac-toxicity and detection of gluten and related prolamins in foods. Panminerva Med, 1991; 33(2):65-74.
  109. Wieslander G, Norbäck D. Buckwheat allergy. Allergy, 2001; 56:703-704.
  110. Bietz JA. Cereal prolamin evolution and homology revealed by sequence analysis. Biochm Gentics, 1982; 20(11/12):1039-1053.
  111. Cicek M and Esen A. Stucture and expression of a dhurrinase (-glucosidase) from sorghum. Plant Physiol, 1998; 116:1469-1478.
  112. Mazhar H, Chandrashekar A, Shetty HS. Isolation and immunochemical characterization of the alcohol-extractabel proteins (kafirins) of Sorghum bicolor (L.) Moench. J Cereal Sci, 1993; 17(1):83-93.
  113. Gaitan E, Cooksey RC, Legan J, Lindsay RH. Antithyroid effects invivo and invitro of vitexin: a C-glucosylflavone in millet. J Clin Endocrinol Metab, 1995; 80(4):114-1147.
  114. Monteiro PV, Virupaksha TK, Rao DR. Proteins of Italian millet: amino acid composition, solubility fractionation and electrophoresis of protein fractions. J Sci Food Agric, 1982; 33(11):1072-1079.
  115. Monteiro PV, Sudharhsna L, Ramachandra G. Japanese barnyard millet (Echinochloa frumentacea): protein content, quality and SDS-PAGE of protein fractions. J Sci Food Agric, 1988; 43(1):17-25.
  116. Parameswaran KP and Thayumanavan B. Homologies between prolamins of different minor millets. Plant Foods Human Nutr, 1995; 48:119-126.
  117. Parameswaran KP and Thayumanavan B. Isolation and characterization of a 20 kD prolamin from kodo millet (Paspalum scrobiculatum) (L.): homology with other millets and cereals.. Plant Foods Human Nutr, 1997; 50:359-373.
  118. Grela ER. Nutrient composition and content of antinutritional factors in spelt (Triticum spelta L.) cultivars. J Sci Food Agric, 1996; 71(3):399-404.
  119. Jones SM, Megnolfi CG, Cooke SK, Sampson HA. Allergens, IgE, mediators, inflammatory mechanisms: immunologic cross-reactivity among cereal grains and grasses in children with food hypersensitivity. J Allergy Clin Immunol, 1995; 96:341-351.
  120. Pastorello EA, Farioli L, Robino A, et al. A lipid transfer protein involved in occupational sensitization to spelt. J Allergy Clin Immunol, 2001; 108(1):145-146.
  121. Skrabaqnja V, Kovac B, Golob T, et al. Effect of spelt wheat flour and kernel on bread composition and nutritional characteristics. J Agric Food Chem, 2001; 49:497-500.
  122. Aphalo P, Castellani OF, Martinez EN, Anón MC. Surface phyusicochemical properties of globulin-P amaranth protein. J Agric Food Chem, 2004; 52:616-622.
  123. Gorinstein S, Delgado-Licon E, Pawelzik E, et al. Characterization of soluble amaranth and soybean proteins based on fluorescence, hydrophobicity, electrophoresis, amino acid analysis, circular dichroism, and differential scanning calorimetry measurements. J Agric Food Chem, 2001; 49:5595-5601.
  124. Vasco-Méndez NL and Paredes-López O. antigenic homology between amaranth glutelins and other storage proteins. J Food Biochem, 1995; 18(4):227-238.
  125. Aluko RE and Monu E. Functional and bioactive properties of quinoa seed protein hydrolysates. J Food Sci, 2003; 68(4):1254-1258.
  126. Lee AR, Ng DL, Dave E, et al. The effect of substituting alternative grains in the diet on the nutritional profile of the gluten-free diet. J Hum Nutr Diet, 2009; 22:359-363.
  127. Wright KH, Huber KC, Fairbanks DJ, Huber CS. Isolation and characterization of Atriplex hortensis and sweet Chenopodium quinoa starches. Cereal Chem, 2002; 79(5):715-719.
  128. Heelan Bt, Allan S, Barnes RMR. Identification of a 200-kDa glycoprotein antigen of Saccharomyces cerevisiae. Immunol Lett, 1991; 28:181-186.
  129. Oshitani N, Hato F, Kenishi S, et al. Cross-reactivity of yeast antigens in human colon and peripheral leukocytes. J Pathol, 2003; 199:361-367.
  130. Sendid B, Quinton JF, Charrier G, et al. Anti-Saccharomycies cerevisiae mannan antibodies in familial Crohn’s disease. Am J Gastroenterol, 2001; 93(8):1306-1310.
  131. Vojdani A, Rahimian P, Kalhor H, Mordechai E. Immunological cross reactivity between candida albicans and human tissue. J Clin Lab Immunol, 1996; 48:1-15.
  132. Young Ca, Sonnenberg A, Berns EA. Lymphocyte proliferation response to baker’s yeast in Crohn’s disease. Digestion; 1994:55(1):40-43.
  133. Beezhold DH, Sussman GL, Liss GM, Chang NS. Latex allergy can induce clinical reactions to specific foods. Clin Exp Allergy, 1996; 26(4):416-422.
  134. Brehler R, Theissen U, Hohr C, Luger T. “Latex-fruit syndrome”: frequency of cross-reacting IgE antibodies. Allergy, 1997; 52:404-410.
  135. Ibero M, Castillo MJ, Pineda F. Allergy to cassava: a new allergenic food with cross-reactivity to latex. J Investig Allergol Clin Immunol, 2007; 17(6):409-412.
  136. Mikkola JH, Alenius H, Kalkkinen N, et al. Hevein-like protein domains as a possible cause for allergen cross-reactivity between latex and banana. J Allergy Clin Immunol, 1998; 102:1005- 1012.
  137. Arentz-Hansen H, Fleckenstein B, Molberg Ø, et al. The molecular basis for oat intolerance in patients with celiac disease. PLoS Med, 2004 1(1):084-092.
  138. Janatuinen EK, Pekka HP, Kemppainen TA, et al. A comparison of diets with and without oats in adults with celiac disease. N Engl J Med, 1995; 333:1033-1037.
  139. Reunala T, Collin P, Holm K, et al. Tolerance to oats in dermatitis herpetiformis. Gut, 1998; 43:490-493.
  140. Silano M, Dessì M, De Vincenzi M, Cornell H. In Vitro tests indicate that certain varieties of oats may be harmful to patients with coeliac disease. J Gastroenterol Hematol, 2007; 22:528-531.
  141. Srinivasan U, Jones E, Carolan J, Feighery C. Immunohistochemical analysis of coeliac mucosa following ingestion of oats. Clin Exp Immunol, 2006; 144:197-203.
  142. Thompson T. Gluten contamination of commercial oat products in the United States. N Engl J Med. 2004; 351(19):2021-2022.
  143. Axelsson IG. Allergy to the coffee plant. Allergy, 1994; 49(10):885-887.
  144. Caballero Tm, Garcia-Ara C, Pascual C, et al. Urticaria induced by caffeine. J Investig Allergol Clin Immunol, 1993; 3(3):160-162.
  145. Moneret-Vautrin DA, Kanny G, Faller JP, et al. [Severe anaphylactic shock with heart arrest caused by coffee and gum Arabic, potentiated by beta-blocking eyedrops]. Rev Med Interne, 1993; 14(2):107-111.
  146. Osterman K, Johansson SG, Zetterström O. Diagnostic tests in allergy to green coffee. Allergy, 1995; 40(5):336-343.
  147. Treudler R, Tebbe B, Orfanos CE. Coexistence of type I and type IV sensitization in occupational coffee allergy. Contact Dermatitis, 1997; 36:109.
  148. Davidson IW, Lloyd RS, Whorwell PJ, Wright R. Antibodies to maize in patients with Crohn’s disease, ulcerative colitis and coelic disease. Clin Exp Immunol, 1979, 35:147-148 lxvi Lehrer SB, Reese G, Malo J-L, et al. Corn Allergens: IgE antibody reactivity and cross- reactivity with rice, soy, and peanut. Int Arch Allergy Immunol, 1999; 118:298-299.
  149. Paulis JW and Bietz JA. Separation of alcohol-soluble maize proteins by reversed-phase high performance liquid chromatography. J Cereal Sci, 4986; 4:205-216.
  150. Asero R, Amato S, Alfieri B, et al. Rice: another potential cause of food allergy in patients sensitized to lipid transfer protein. Int Arch Allergy Immunol, 2007; 143:69-74.
  151. Horikoshi M, Kobayashi H, Yamazoe Y, et al. Purification and complete amino acid sequence of a major prolamin of rice endosperm. J Cereal Sci, 1991; 14(1):1-14.
  152. Urisu A, Yamada K, Masuda S, et al. 16-kilodalton rice protein is one of the major allergens in rice grain extract and responsible for cross-allergenicity between cereal grains in the poaceae family. Int Arch Allergy Immunol, 1991; 96(3):244-252.
  153. Wen T-N and Luthe DS. Biochemical characterization of rice glutelin. Plant Physiol, 1985; 78:172-177.
  154. Yamada K, Urisu A, Komada H, et al. [Involvement of rice protein 16KD in cross- allergenicity between antigens in rice, wheat, corn, Japanese millet, Italian millet]. Arerugi, 1991; 40(12):1485-1495.
  155. Racusen D and Foote M. A major soluble glycoprotein of potato tubers. J Food Biochem, 1980; 4(1):43-52.
  156. Vos-Scheperkeuter GH, De Boer W, Visser RGF, et al. Identification of granule-bound starch synthase in potato tubers. Plant Physiol, 1986; 82:411-416.
  157. Vos-Scheperkeuter GH, de Wit JG, Ponstein AS, et al. Immunological comparison of the starch branching enzymes from potato tubers and maize kernels. Plant Physiol, 1989; 90:75-84.
  158. Hvatum M, Scott H, Brandtzaeg P., Serum IgG subclass antibodies to a variety of food antigens in patients with coeliac disease, Gut. 1992 May;33(5):632-8.
  159. Husby S, Foged N, Oxelius VA, Svehag SE,Serum IgG subclass antibodies to gliadin and other dietary antigens in children with coeliac disease,Clin Exp Immunol. 1986 Jun;64(3):526-35.
  160. Breiteneder H, Ebner C., Molecular and biochemical classification of plant-derived food allergens, J Allergy Clin Immunol. 2000 Jul;106(1 Pt 1):27-36. Review
  161. Scott H, Fausa O, Ek J, Brandtzaeg P., Immune response patterns in coeliac disease. Serum antibodies to dietary antigens measured by an enzyme linked immunosorbent assay (ELISA), Clin Exp Immunol. 1984 Jul;57(1):25-32.
  162. Farthing M, Rees L, Edwards C, Dawson A. Male gonadal func- tion in coeliac disease: 2. Sex hormones. Gut, 1983; 24, 127-135. 26. Betterle C, Zanchetta R. Update on autoimmune polyendocrine syndromes (APS). Acta Bio Medica, 2003; 74; 9-33.
  163. F, Facciuto E, Migliaccio S, Bardella MT, Dubini A, Borghi MO, Saraifoger S, Teti A, Bianchi ML. Imbalance of osteoclastogene- sis-regulating factors in patients with celiac disease. J Bone Miner Res, 2004; 19: 1112-1121.
  164. da Silva K, Kotze L, Nishihara R, daRosa U, Piovezan G, Kotze L. Thyroid disorders in Brazilian patients with celiac disease. J Clin Gastroenterol, 2006; 40(1):33-36.
  165. Stone S, Khamashta MA, Poston L. Placentation, antiphospholipid syndrome and pregnancy outcome. Lupus, 2001;10:67-74.
  166. Shamir R, Shoenfeld Y, Blank M, Eliakim R, Lahat N, Sobel E, Shinar E, Lerner A. The prevalence of coeliac disease antibodies in patients with the antiphospholipid syndrome. Lupus, 2003;12;394.
  167. La Villa G, Pantaleo P, Tarquini R, Cirami L, Perfetto F, Man- cuso F, Laffi G. Multiple immune disorders in unrecognized celiac disease: a case report. World J Gastroenterol, 2003;9(6): 1377-1380.
  168. Sategna-Guidetti C,V olta U, Ciacci C, Usai P , Carlino A, De Franceschi L, Camera A, Pelli A, Brossa C. Prevalence of Thy- roid Disorders in Untreated Adult Celiac Disease Patients and Effect of Gluten Withdrawal: An Italian Multicenter Study. AJG, 2001;Vol. 96, No. 3: 751-757.
  169. Levine JS, Branch DW, Rauch J. The antiphospholipid sindrome. NEJM, 2002; 346: 752-763.
  170. Djuric Z, Zivic S, Katic V. Coeliac disease with diffuse cutaneous Vitamin K deficiency bleeding. Adv Ther, 2007;24(6):1286- 1289.
  171. Rujner J. Age at menarche in girls with celiac disease. Ginekol Pol, 1999;70:359-362.
  172. Sher KS, Mayberry JF. Female fertility, obstetric and gynaeco- logical history in coeliac disease: a case control study. Acta Pae- diatr Suppl, 1996;412:76-77.
  173. Martinelli P, Troncone R, Paparo F, Torre P, Trapanese E, Fasano C, et al. Coeliac disease and unfavourable outcome of pregnancy. Gut, 2000;46(3):332-335.

A fizzy gut healing surprise: Beet Kvass

Fermented food has been known to help rebuild our gut flora and support immune response along with digestion in our gut. This year, in supporting my own gut healing journey, I set the intention to learn the art of all things fermented. We had all these excess beets from our CSA veggie box, so we started making this simple refreshing, fermented drink. A nice alternative to kombucha.

Beet Kvass


  • 3 medium beets cut into small chunks
  • 2 – 3 slices of ginger
  • 4 tsp salt
  • Filtered water
  • 1 large glass jar


  1. Place beets in a bowl and sprinkle with salt. Combine the mixture and place into the glass container and fill with filtered water. Cover container.
  2. Keep at room temperature for 3 to 6 days until it starts tasting tart. I like mine tart, so I keep it for 5-6 days. Then transfer liquid into container to be refrigerated.
  3. You can keep some left over Kvass as inoculant for the next batch.
  4. Recommend 1/2 cup per day. I use the leftover beet chunks as pickles for a side dish or in salads. You can add them to soups, but heating will kill the beneficial bacteria.

***It is always important to keep the liquid covering the food that’s fermenting to prevent mold from growing.



Lower Cancer Risk When Getting enough Vitamin D

What is your blood Vit D level?

Does it matter?

A recent study looked at 2300 women over 55 years old and found that if their vitamin D serum level were greater than or equal to 40 ng/ml, then they had a 67% lower risk of cancer than those with serum levels <20 ng/ml (P-value = .02). Read paper.

The standard recommendation levels of vit D level is 40-60 ng/ml.

So, why should we test, rather than just take vitamin D supplements daily?

The same people who did this study also found that when measuring vitamin D blood serum levels, supplementation response varies greatly person-to-person.  For example, 2 people could both take 4,000 IU/day, they both measure their vitamin D levels and one could have the level 10 ng/ml, while another could be 120 ng/ml – a 10-fold variation in response to the same supplementation dose of 4,000 IU/day.

Reasons for such variability can be due to skin tone (those with darker skin tones need to spend more time in ultraviolet light to make vitamin D than those with lighter skin tones), gut absorption, and utilizations in the body.

So rather than just supplement your vitamin D,  check your serum level with your doctor.  It’s called Serum 25-Hydroxyvitamin D.  Read more about Vitamin D here.




4 Natural Immune Boosting Tips

Whether you are a parent with kids going back to school, or you work in a large office environment with lots of handshakes or door knobs to grab, September to November months are often when people begin the cycle of cough and colds, earaches, strep throats and sinus symptoms.  Some more prone to it than others.

Here are some simple tools to boost your immune system so you can avoid being out from work, or avoid frequent visits to the doctors.

1. Pay attention to Diet

Remove inflammatory foods can make a huge difference in boosting your immune system, and we now know that foods with high phytonutrients can fight disease too.

  • Remove most sugar, including artificial sugar, processed sugar, fruit juices and sodas.
  • Remove cow and goat dairy like cheese, yoghurt, milk.  It is known to cause more phlegm and mucus in our body.
  • Eat 8 servings (a small fist/serving) of fruits, especially berries and vegetables like dark leafy greens, cruciferous vegetables (broccoli, kale, cauliflower)
  • Use food as medicine and eat lots of onions, garlic and ginger to benefit from their anti-microbial, anti-inflammatory
  • Eat high quality protein (fish, lean meats) and fats (olive oil, coconut oil, avocado)

2. Get enough Sleep

It’s easy to extend the summer fun and push for late night social events or watch one too many TV series.  Instead, give yourself more time to sleep by going to bed early, and try to get at least 8 hours of sleep. 

Our body fights inflammation better with melatonin from our body during our sleep, and we make better at repairing our body with protein and cells when we have enough sleep.

3. Use a Nasal Saline Rinse daily

Using a nasal rinse using saline can help reduce respiratory infections significantly.  You can use a neti pot, my favorite is the Neil Med Sinus Rinse Bottle that you can get in major pharmacies.  And use the pre-packaged pH balanced saline packets so it’s soothing to the nasal cavities.

4. Take these 3 vitamins every day

  • Vitamin C –
    • Study shows cold symptoms decrease by 13% with taking 1 gram daily of Vitamin C for prevention.
    • Take 500mg buffered ascorbic acid twice a day, or 1000mg daily.
  • Vitamin D –
    • Vitamin D is essential fat soluble vitamin that acts like a hormone in our body, important for immune functioning, decreasing inflammation, control of cell growth.
    • Get 10 -15 minutes of mid-day sun exposure to your skin (Adjust base on your location and how close you are to the equator and also the time of year. )
    • Take 2000 IU (international units) per day
  • Zinc –
    • Zinc is an essential mineral for keeping a healthy immune system, building proteins, triggering enzymes and creating DNA.  If you take it daily for up to 5 months, zinc reduces chances of you getting a viral infection such as colds.
    • Food sources of proteins includes oysters, crabs, nuts, spinach, seeds: sesame, pumpkin, sunflowers, chia and flaxseeds, dark chocolate, and mushrooms.
    • Take 25mg per day.


Brown R, Pang G, Husband AJ, King MG. Suppression of immunity to influenza virus infection in the respiratory tract following sleep disturbance. Reg Immunol. 1989;2:321–325

Pratter MR. Cough and the common cold: ACCP evidence-based clinical practice guidelines. Chest. 2006;129(1 suppl):72S-74S.

Singh M, Das RR. Zinc for the common cold. Cochrane Database Syst Rev. 2011;(2):CD001364

Slapak I, Skoupá J, Strnad P, Horník P. Efficacy of isotonic nasal wash (seawater) in the treatment and prevention of rhinitis in children. Arch Otolaryngol Head Neck Surg. 20 08 ;134 (1) : 67-74.




The Skinny on Vitamin D

What’s the deal on Vitamin D?   Should I check my levels?  Can I just get it from being in the sun daily?  How much is enough?  Where else can I get Vitamin D?

These are some common questions I get daily about vitamin D.  So here’s the skinny on Vitamin D.

What is Vitamin D? Why do we need it?

Vitamin D is a a potent neuroregulatory steroidal hormone that influences nearly 3,000 of your 25,000genes.1 It  turns on and off genes that can exacerbate — or prevent — many diseases.  Our body will not work correctly if we do no get enough.  We now know that mild deficiency can cause a range of chronic disease including osteoporosis, heart disease, blood pressure issues, impaired immune functions, autoimmune diseases like diabetes and multiple sclerosis, and even cancers like breast, colon, lung, lymphoma and prostate.

Where do I get Vitamin D?

The major source is your skin.  When the surface of our skin is exposed to UVB light, it converts a chemical compound to Vitamin D3, cholecalciferol.  If we are indoors all the time, or only outdoors in the morning or evening, we don’t produce enough Vitamin D.  You can also get vitamin D from food(limited), and supplements.

How much sun exposure is enough?

It’s different based on where you are in relationship to the equator, and how dark is your skin.  A light skinned person will full body exposure will make 15,000IU Vitamin D in 15-20 minutes in July at noon.  Darker skinned person can take twice as long to get same effect.

Should I worry about Skin Cancer?

Sun screen blocks UVB light and prevents Vit D being made.  However, it should be safe with 15 minutes of sun exposure before you apply sunblock.

Why is Vitamin D particularly important in pregnancy and newborn?

Having enough vitamin D during pregnancy reduces the risk of premature birth, low birth weight babies, Cesarean sections, and various others of the many complications of pregnancy. It also helps the unborn infant program its own body so as to reduce the risk of a host of disorders that may not appear until many years after birth. 4000 IU/day was demonstrated to be safe in a randomized trial to help pregnant women achieve a serum level of approximately 40 ng/mL. (Reference: Hollis, Wagner, Am J Obstet Gynecol. 2012 Nov 3) The American Academy of Pediatrics strongly recommends that all babies, whether breastfed or bottle fed, need supplemental vitamin D of 400 to 800 IU/d during the first year of life.

Which form of Vitamin D should I take?

Vitamin D3(cholecalciferol) is the form that our bodies make naturally on exposure to the sun. Vitamin D2(ergocalciferol) is synthesized from plant product precursors. Vitamin D3 is recommended because it’s more potent than vitamin D2.

How much Vitamin D do I need?

A person need 4000 IU/day from all sources to maintain a normal Vitamin D level in the blood.  If you are not exposed to sunlight regularly during the day, take 2000-4000IU daily.

According to the Institute of Medicine, there’s no observable adverse event at 10,000IU/day.

How much should I take?

Average requirement is about 35 IU/pound of body weight (75 IU/kg) per day, from all sources. So if you weigh 150lb, that’s 5000 IU daily Vitamin D3.  The best approach is still checking your vitamin D levels .

What level should my vitamin D be?

Aim for 40ng/ml or above of 25 OH-Vitamin D. Studies have shown that levels over 40 ng/ml 25 OH-Vitamin D are associated with lower risk of cancer such as Breast Cancer, decrease pregnancy comorbidities, type 2 diabetes.2

In summary, Vitamin D is a useful chemical our body needs, and it’s worth it to ask your doctor to check your levels in your next appointment, or supplement if you are not often exposed to regular midday sunlight.