In our pursuit of health (the state of being free from illness or injury) we discovered the magic of meditation, the wonderful benefits of prayer, and the infusion of mind, body, and spirit through the consumption of tea. In this pursuit, we have come across various writings, videos, and artistic presentations which can further these efforts. To be of additional service to you, we have compiled an assortment of these works which you may find helpful. Please enjoy as we have.
Life Extension Benefits of Methionine Restriction
by Ben Best
- METHIONINE BASICS
- METHIONINE RESTRICTION EFFECTS
- METHIONINE RESTRICTION FOOD DATA
- METHIONINE RESTRICTION DIET
Methionine is the only essential amino acid containing sulfur. Methionine is the precursor of the other sulfur-containing amino acids: cysteine, taurine, homocysteine, and cystathione. Methionine is essential for the synthesis of proteins and many other biomoleules required for survival. Rats fed a diet without methionine develop fatty liver disease which can be corrected by methionine supplements [DIGESTIVE DISEASES AND SCIENCES; Oz,HS; 53(3):767-776 (2008)]. Dietary methionine is essential for DNA methylation. Reduced DNA methylation results in genetic instability, aberrant gene expression, and increased cancer.
The above paragraph is the first paragraph from the section on methionine in my article dealing with the Methionine Cycle. Material in that article is useful background for the information below. Note that there is an inverse correlation between lifespan and the methionine content of protein in the heart muscle of eight mammalian species [MECHANISMS OF AGEING AND DEVELOPMENT; Ruiz,MC; 126(10):1106-1114 (2005)]. The methionine content of the milk of cows is higher than that of primates, and the methionine content of the milk of humans and great apes is lower than that of other primates [JOURNAL OF NUTRITION; Davis,TA; 124:1126 (1994)]. Methionine restriction has been shown to increase the replicative lifespan (reduce the replicative senescence) of human fibroblasts [AGING CELL; Koziel,R; 13(6):1038-1048 (2014)].
The sulfur-containing amino acids methionine and cysteine are the most readily oxidized of any of the amino acids — both as free amino acids or in proteins. Methionine is oxidized to methionine sulfoxide, but methionine sulfoxide reductases enzymatically regenerate methionine [BIOPHYSICA ET BIOCHEMICA ACTA; Lee,BC; 1790 (11): 1471-1477 (2009)].
Substantial evidence indicates that as much as half of the life-extension benefits of CRAN (Calorie Restriction with Adequate Nutrition) are due to restriction of the single amino acid methionine. In a study of rats given 20% the dietary methionine of control rats, mean lifespan increased 42% and maximum lifespan increased 44% [THE FASEB JOURNAL;Richie,JP; 8(15):1302-1307 (1994)]. Blood glutathione levels were 81% higher in the methionine-restricted rats at maturity, and 164% higher in old age. Long-lived Ames dwarf mice have an enhanced methionine metabolism that increases tissue glutathione (GSH) [MECHANISMS OF AGING AND DISEASE; Uthus,EO; 127(5):444-450 (2006)]. Neither the long-lived growth hormone receptor knock-out mouse nor the Ames dwarf mouse show additonal lifespan extension with methionine restriction, suggesting that stimulation of protein synthesis by either methionine or growth hormone shortens lifespan [AGING CELL; Brown-Borg,HM; 13(6):1019-1027 (2014)].
In other studies, methionine-restricted rats showed greater insulin sensitivity and reduced fat deposition [AMERICAN JOURNAL OF PHYSIOLOGY; Hasek,BE; 299:R728-R739 (2010), EXPERIMENTAL GERONTOLOGY; Sanchez-Roman,I; 48(10):1030-1042 (2013), and AGING CELL; Malloy,VL; 5(4):305-314 (2006)]. Methionine-restricted rats lost weight, despite greater food consumption, because of heat loss associated with metabolically inefficient conversion of glucose to fat [Hasek, Ibid.]
An experiment on mice given 35% the methionine of controls showed only a 7% increase in median life span [JOURNALS OF GERONTOLOGY; Sun,L; 64(7):711-722 (2009)]. Another mouse study showed lowered serum insulin, IGF−1, glucose, and thyroid hormone for methionine at one-third the normal intake. There was significant mouse mortality for methionine less than one-third normal intake, but with one-third intake of methionine maximum lifespan was significantly increased [AGING CELL; Miller,RA; 4(3):119-125 (2005)].
Rats generally show greater longevity benefits from CRAN than mice. Piglets showed comparable benefits to rats in a two-week study, including decreased reactive oxygen species in mitochondrial complex I and reduced apoptosis-inducing factor [EXPERIMENTAL GERONTOLOGY; Ying,Y; 65:35-41 (2015)]. Methionine-restricted rats had increased FGF21, showing many of the same benefits as FGF21-treated rats, including improved insulin sensitivity, reduced adiposity, more mitochondria, and AMPK activation [JOURNAL OF NUTRIGENETICS AND NUTRIGENOMICS; Perrone,CE; 5:132-157 (2012)].
Mitochondrial free radical generation is believed by many biogerontologists to be a significant contributor to aging damage. Rats given 20% the dietary methionine of control rats show significantly decreased free radical generation from complex I and complex III of liver mitochondria as well as from complex I of heart mitochondria — associated with reduced oxidative damage to mitochondrial DNA and protein [THE FASEB JOURNAL;Sanz,A; 20(8):1064-1073 (2006)]. These results are comparable to the reduced mitochondrial free radical generation seen in CRAN rats [ENDOCRINOLOGY; Gredilla,R; 146(9):3713-3717 (2005)]. Rats given 60% rather than 20% of the methionine of control rats showed nearly the same amount of reduced mitochondrial free radical generation and damage [BIOCHEMICA ET BIOPHYSICA ACTA; Lopez-Torres,M; 1780(11):1337-1347 (2008)]. Body weight was not reduced with 60% dietary methionine, leading to the conclusion that such reduction would not result in reduced growth in children [REJUVENATION RESEARCH; Caro,P; 12(6):421-434 (2009)]. It was concluded that methionine restriction is the sole reason for reduced mitochondrial free radical generation and damage associated with CRAN [Ibid.] and protein restriction [BIOGERONTOLOGY; Caro,P; 9(3):183-196 (2008)]. Rats methionine-restricted by 40% rather than by 80% showed similar benefits, but without the negative impact on growth, puberty, or body size seen with 80% methionine restriction [JOURNAL OF BIOENERGETICS AND BIOMEMBRANES; Sanchez-Roman,I; 63(6):699-708 (2011)].
A human clinical trial on cancer patients given the methionine-reduced supplement powder Hominex-2 showed a 75% decrease in plasma methionine [NUTRITION AND CANCER; Epner,DE; 42(2):158-166 (2002)], whereas a clinical trial using Hominex-2 on metabolic syndrome patients resulted on only a 14% decrease [JOURNAL OF CLINICAL ENDOCRINOLOGY AND METABOLISM; Plaisance,EP; 96(5):E836=E840 (2011)], probably due to poor palatability and low compliance. Nonetheless, the metabolic syndrome patients showed an average 27% increase in plasma adiponectin. Cancer cells are more sensitive to methionine restriction than are normal cells [NUTRITION AND CANCER; Epner,DE; 42(2):158-166 (2002)]. Hominex-2 contains corn syrup solids as the primary ingredient. Cysteine content in Hominex-2 may reverse the effects of methionine restriction [JOURNAL OF NUTRIGENETICS AND NUTRIGENOMICS; Perrone,CE; 5:132-157 (2012)].
Further evidence for the suggestion that methionine oxidation plays a significant role in lifespan can be found in the considerable lifespan extension benefits seen in transgenic fruit flies that overexpress a gene for repairing oxidized methionine in protein [PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES (USA); Ruan,H; 99(5):2748 (2002)]. The sulfur-containing amino acids methionine and cyteine are more easily oxidized in proteins than other amino acids [JOURNAL OF PHYSIOLOGY; Hoshi,T; 531:1 (2001)], which is apparently related to the reduced free radical generation in mitochondria seen in methionine restriction. Both the fruit fly experiment and the methionine restriction experiments indicate a significant impact on lifespan from methionine oxidation.
It has been suggested that glycine supplementation has the same effect as methionine restriction. An experiment with glycine supplementation in rats showed a 30% extension in maximum lifespan [FASEB JOURNAL; Brind,J; 25:528.2 (2011)]. Additionally, three grams of glycine daily has been shown to improve sleep quality in young (average age 31) female Japanese adults [SLEEP AND BIOLOGICAL RHYTHM; Inagawa,K; 4:75-77 (2006)]
The adjoining table (my Table 1) from [AMERICAN JOURNAL OF CLINICAL NUTRITION; Young,VR; 59(suppl):1203s-1212s (1994)] indicates the essential amino acids most likely to be limited in plant protein foods. Cereal protein contains comparable sulfur-containing amino acids (including methionine) per gram as animal foods, whereas fruit and legume protein contain about 65% as much methionine. Nuts and seeds are particularly high in methionine, on average 20% higher in methionine than animal protein, although the absolute amount of protein in animal foods tends to be higher, which makes total methionine intake generally higher in animal foods. Vegetables are not shown in Table 1, but as described in Table 4 in the AMERICAN JOURNAL OF CLINICAL NUTRITION paper from which Table 1 is taken, vegetables are on average in the 1-2% range for percent protein and fruits are in the 0.5-1% protein range — so neither fruits nor vegetables should be considered serious sources of protein (green peas are an exceptional vegetable with 5.4% protein, and avacado is an exceptional fruit with 2% protein). Cereals are typically 7-13% protein and legumes are typically 20-30% protein (soybeans are exceptionally high in protein even for legumes, being in the range of 35-45% protein).
The dry weight of beef, broccoli, peanuts, and peas is about one-third protein, whereas cereals and fruits are less than 10% dry weight protein. Unlike many other plant proteins, legumes are not particularly low in lysine, and they are close to animal protein in threonine content. Vegetarians attempting to achieve complete protein often combine cereals (which are relatively high in methionine for plant protein) with legumes (which are relatively high in lysine for plant protein).
Lentils and other beans contain high amounts of phytic acid (phosphate-rich inositol), which can chelate positively-charged multivalent mineral ions (especially iron, zinc, magnesium, and calcium), preventing absorption. Soaking lentils and beans in warm water overnight not only makes them easier to cook, it allows some of the phytates to be soaked-out (and thrown-away with the water). Acidic solution (such as vinegar) better removes the phytates. Cooking also helps destroy phytates.
Although it would be very difficult to determine a diet providing optimum methionine for maximum human lifespan — even on the basis of rat experiments — evidence is convincing that reducing dietary methionine can help extend lifespan. The Table 2, listing milligrams of methionine per 100 grams of food (rather than per gram of protein, as in Table 1), could be helpful. Table values are based on [FOOD VALUES OF PORTIONS COMMONLY USED by Jean Pennington (1989)].
The absolute methionine content of a food is better evaluated knowing what the water, fat, carbohydrate, fiber, and protein content of that food is. A higher protein content and a lower methionine content is better than having a low methionine content because the food is low in protein and high in water, fat, or carbohydrate. Lima beans and rice are relatively high in both carbohydrate and methionine. Onions and strawberries are low in methionine, but are high in water and low in protein.
The data for Table 3 is taken from [NUTRITIVE VALUE OF FOODS; USDA Bulletin 72 (1981)], but is adjusted to give percent protein by dry weight. Percent water in the food is not related to the other columns. Fiber content is not given, and I suspect that fiber is equated with carbohydrate. I may have made a few errors, and I suspect that the data contains a few errors (garbage-in, garbage-out). But for the most part I think the data is good, my transcription is accurate, and my calculations are correct.
Brown rice would be more nutritious than white rice, except that the fats in germ that is removed to make white rice can go rancid. Ingestion of Advanced Glycation End-Products (AGES) is detrimental to health.
Table 4gives the percent fat obtained for selected items in the above table, and breaks down the fat into percent saturated, monosaturated, and polyunsaturated fat. Numbers are rounded to the nearest whole number, which is why the total percentages don’t always add to 100. Monosaturated fats and polyunsaturated fats are preferred to unsaturated fats except where there is rancidity. Again, ingestion of Advanced Glycation End-Products (AGES) is detrimental to health. I had no data for non-fat cheese, the only kind of cheese that I eat.
Table 5 gives relative proportions of all of the essential amino acids (plus tyrosine) for some representative high-protein animal foods as well as for some low-methionine plant foods.
Lysine is given after methionine because lysine is most often the limiting amino acid (the essential amino acid found in the smallest quantity relative to requirement) in cereals, nuts, and seeds — but lysine in abundant in legumes, for which methionine is typically the limiting amino acid [AMERICAN JOURNAL OF CLINICAL NUTRITION; Young,VR; 59(suppl):1203s-1212s (1994)]. Lysine is therefore listed second in the table. Leucine is listed third because of its paradoxical ability to reduce fat in high doses [DIABETES; Zhang,Y; 56(6):1647-1654 (2007)] and low doses [DIABETES; Cheng,Y; 59(1):17-25 (2010)]. Leucine and threonine are the limiting amino acid in vegetables and fruits, although vegetables and fruits are too low in protein to be considered significant proteins sources. Trytophan restriction has been shown to have a modest (compared to methionine restriction) ability to extend lifespan in rats [ MECHANISMS OF AGEING AND DEVELOPMENT; Ooka,H; 43(1):79-98 (1988)], reputedly by opposing an age-related increase in brain serotonin.
Tyramine was evaluated because of claims that high dietary tyramine could have adverse reactions with monoamine oxidase inhibitors (I take deprenyl). But none of the foods listed have seriously high levels of tyramine, so tyramine is not really a concern.
Again, this data is taken from [FOOD VALUES OF PORTIONS COMMONLY USED by Jean Pennington (1989)]. I have adjusted the Pennington data to be standardized for 100 grams of food, rather than reproducing the variable quantities of food given, which makes comparison difficult. I may have made transcription errors, but probably not many (if any).
Confusion can be caused by the variable amounts of proteins in the foods. Some foods have high water content (such as onion), or high carbohydrate content (such as rice), or high fat content (such as nuts). To compare relative amounts of methionine in the proteins in the foods, I have created Table 6 in which I have adjusted the values to reflect milligrams of amino acid per gram of protein, rather than the per 100 grams of food used in the previous table. To do this, I first calculate dry weight [(100 − % water) / 100] and then divide by % protein. (Note that Persian/English walnuts contain 60% the protein of black walnuts, mostly because of higher fat content. This creates a misimpression that Persian/English walnuts are much lower in methionine than black walnuts.)
I make no guarantee that I have made no transcription errors in manually copying data from either table to my calculator.
I am searching for foods that are high in protein, but low in methionine, as a source of protein. Preferably the foods should be high in the essential amino acids (other than methionine), and low in fat (especially saturated fat) and low in carbohydrate. As sources of protein, the data in the Table 6 are important in proportion to the percent protein in the food, especially when the water content is low. As long as protein is adequate in the diet overall, other foods that are low in protein and high in water are not much of a concern from a methionine restriction point of view. Legumes offer the best tradeoff of low methionine, and high protein (high essential amino acids), particularly lentils and pinto beans. Adzuki beans would be a contender except that the high fiber content makes them hard to process. I prefer to get my fiber from other sources.
Table 7 was created by dividing methionine amount into the amounts of the other essential amino acids shown in Table 5. Thus, the numbers in the lysine column reflect how many times the lysine content of the food exceed the methionine content.
Pinto beans and lentils are the high-protein foods that show the best low-methionine, high-lysine profile, by a large margin. Lentils, however, are easier to soak before cooking to remove phytates, and produce a bit less odiferous flatulance than pinto beans. Both legumes, however, are high in phytic acid and raffinose oligosaccharides. Humans lack the enzyme to digest raffinose, which passes to the lower intestine where bacteria possessing the digestive enzyme create gases which can be quite odiferous.
Soaking pinto beans for 16 hours at room temperature only reduces raffinose oligosaccharides by 10%, and 90 minutes of cooling only cuts the raffinose oligosaccharide content in half [JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY; Song,D; 54(4):1296-1301 (2006)].
Just as the objective of calorie restriction is not to live without calories, methionine is an essential amino acid that can be reduced to 60% normal consumption to obtain most of the benefit [BIOGERONTOLOGY; Caro,P; 9(3):183-196 (2008)]. That dietary objective can be met without the need to consume legumes.
This is the 11th article in our Controversies series and the second devoted to the topic of proteins.
Today we are going to continue our examination of protein consumption and its impact on cancer and longevity.
To do that, we will discuss three relatively unknown subjects: the ‘engine of aging’ enzyme (TOR), an adrenal steroid hormone (DHEA), and an amino acid called methionine.
All may have serious repercussions on the length of our lives as well as our risk of cancer.
And each may be controlled by the consumption of the right type of protein.
Let me explain.
Let’s start with an explanation of TOR.
Nicknamed the ‘engine of aging’ enzyme, TOR functions as a master regulator of cellular growth and proliferation.
TOR gets its name (Target of Rapamycin) because it can be inhibited (‘targeted’) by the drug rapamycin, an antifungal produced by a bacterium first isolated on Easter Island. In mammals, it is called mTOR (for mechanistic or mammalian TOR), and rapamycin has been used as an immunosuppressant in humans to prevent rejections of transplanted organs.
While we need it early on in life to grow, high levels of mTOR in adulthood seem to be linked to a significantly higher risk of cancer as well as premature death.
Perhaps the best way to describe mTOR is to employ the analogy of a speeding car. When you are young and growing, it is okay for the car (mTOR) to go ‘fast.’ You need cells to proliferate and grow in infancy and early life.
However, when you enter the low-speed zone of adulthood, cell growth needs to slow down. But if mTOR is continuously stimulated (by what we eat among other things), that will not happen.
mTOR is the engine of growth in childhood but the engine of aging in adulthood.
Studies show that in almost 100 percent of advanced human prostate cancers, mTOR is present in higher amounts. Similarly, higher levels of mTOR are found in breast cancer tissues and appear to be associated with advanced disease and worse overall survival rates.
Simply put, if you suppress mTOR, you may reduce your risk of cancer and increase your chances of living longer.
So what is the best way to do that?
One strategy to stem mTOR production (and in turn extend lifespan) seems to be the severe restriction of calorie consumption.
When food is abundant, mTOR soars, encouraging body cell division. However, when there is scant food, mTOR shifts into conservation mode and slows down cell division, kicking in a process called autophagy (literally translated as to ‘eat oneself’), which cleans and renews cells.
A better way to reduce mTOR production is to restrict animal protein intake.
One of the drivers of mTOR appears to be the amino acid leucine, which is found in higher amounts in animal foods (e.g. dairy, meat, chicken, fish, and eggs).
Therefore, to lower your leucine intake (and mTOR levels), you need to either restrict your consumption of animal proteins or, better yet, adopt a 100 percent plant-based diet. (While plant foods contain small amounts of leucine, it is nothing in comparison to animal proteins.)
Eating plants—and specifically cruciferous veggies—decreases mTOR activation and provides natural mTOR inhibition. Some of the best mTOR-inhibiting fruits and veggies include broccoli, green tea, soy, turmeric, grapes, onions, strawberries, blueberries, and mangoes.
You only have to look at the example of the older generation Okinawa Japanese for evidence that this approach seems to work. For centuries, the extremely long-lived Okinawans have traditionally consumed a largely plant-based diet; only a scant 1 percent of their diet was made up of fish, meat, eggs, and dairy.
Reducing our animal protein intake (versus restricting calories) is a much easier approach when it comes to decreasing mTOR levels—and also a more powerful one.
That is because lowering the consumption of animal protein will not only suppress mTOR production but also decrease IGF-1 levels as we discussed in our first protein article (while calorie restriction will lower mTOR but not IGF-1).
What About DHEA?
Let us now turn to the topic of DHEA.
As we age, the level of DHEA in our bodies drops significantly.
So while we want to decrease mTOR production, we would like to increase DHEA.
One way to raise DHEA is—once again—to restrict calorie consumption.
But probably the best path to naturally boosting your DHEA levels is through nutrition—specifically by eating a plant-based diet.
Research shows that the amount of DHEA in the blood increases as much as 20 percent after only five days of adhering to an egg-free vegetarian diet (compared to meat eaters consuming equivalent amounts of calories).
And even more interestingly, these levels rise not necessarily because the body is producing more DHEA but because a plant-based diet causes the body to lose less in the first place.
More About Methionine
Last but not least, let’s turn to the third subject in our protein triumvirate: methionine.
An important scientific article published 40 years ago indicated that many human cancer cells are ‘absolute methionine dependent.’ More specifically, the study showed that normal cells grown in vitro without methionine seemed to thrive while cancer cells died.
Two decades later, this methionine dependence was further reported in 5 types of fresh patient tumors (e.g. colon, breast, ovary, prostate, and melanoma) grown in vitro.
In other words, unlike ‘healthy’ tissues, some human tumors seemed to require the amino acid methionine to grow.
So, when you lower methionine, you may reduce your cancer risk.
Restricting high methionine animal foods and consuming a plant-based diet that is naturally low in it may do just that.
For Senior Citizens Only
One question I am frequently asked when discussing protein is this:
What is the optimal source and amount of protein for senior citizens?
Sedentary individuals over the age of 65 lose about 1 percent of their muscle mass every year while older adults on bed rest can lose muscle mass 6 times faster than a younger person.
Physical activity is one of the best approaches to halt muscle mass loss later in life.
Another way to protect aging muscles is to eat vegetables; you can cut your odds of losing muscle mass by 50 percent just by consuming the daily recommended servings of veggies.
Why does eating vegetables help?
A recent study showed that a plant-based diet was positively associated with muscle mass in women aged 18-79 years old. It appears that the alkalizing effect of veggies may neutralize the mild metabolic acidosis that occurs with age—the same extra acid that stimulates the breakdown of muscle.
A chronic low-grade acidosis with advancing age is associated with declining kidney performance. But it is also a result of a Western dietary pattern (or the ‘meat-sweet’ diet), which is high in acid-promoting animal and sugary foods while low in alkalinizing fruits and veggies.
So we have covered three protein-related topics today: mTOR (and leucine), methionine, and DHEA. All three play an important role in our aging process and risk of cancer. In the case of mTOR (leucine) and methionine, levels should go down or stay low, while we need to keep our DHEA levels high.
And this can be easily accomplished by consuming primarily or exclusively plant-based proteins found in fruits, vegetables, legumes, whole grains, and nuts.
We make a wide variety of hormones that circulate throughout our bodies to help with growth, mood, sexual function and metabolism. It’s a complicated web that can be easily thrown off kilter, leading to symptoms that can disrupt our fertility, weight, menstrual cycles and our ability to cope with stress. Food is an incredibly helpful tool when dealing with hormone imbalances and today, we’re going to share our best hormone balancing foods with you.
Note that we cannot cover all of the hormones in the body and their unique effects, but we’re covering some of the most common hormone imbalances our grads from the Culinary Nutrition Expert program see in their clients.
How Do I Know If My Hormones Aren’t Balanced?
Before you include hormone-balancing foods into your diet, you need to know which ones are too high or too low. We recommend working with a health practitioner, who can help you assess your symptoms and determine which hormones need some fine tuning.
BEST HORMONE BALANCING FOODS
What Are They: Our sex hormones manage our reproduction, the development of sex characteristics (eg breast and hips) and sexual motivation. Some of the main hormones are estrogen, progesterone and testosterone.
How Do They Get Out of Whack? Our sex hormone levels can change naturally during different stages of life (eg puberty or menopause), but they can also be thrown out of balance by diet, lifestyle and our exposure to toxins.
BEST SEX HORMONE BALANCING FOODS
Flax seeds are rich in anti-inflammatory omega-3 fats and contain phytoestrogens, which are plant-based compounds that mimic estrogen, bind to our estrogen receptors and help us excrete excess estrogen from the body. They can also help improve or prevent additional hormone-related issues including breast cancer, menopausal symptoms and osteoporosis.
Salmon is an excellent source of Vitamin D, a fat-soluble vitamin that helps us make our sex hormones. and boost testosterone levels. Vitamin D is important for bone health and immunity, too. Salmon is also high in omega-3 fatty acids, which have been shown to reduce our risk of breast cancer and prostate cancer.
Soy is a controversial topic for many reasons, including genetic modification and allergies, but when you choose good sources like organic miso and tempeh you can garner the positive benefits of soy’s isflavones, which have phytoestrogenic properties and can reduce the risk of breast cancer. The source of soy is definitely important – and a fermented choice like tempeh or miso will bring you the beneficial probiotics that improve digestion and mood. Balanced digestive flora also reduces the activity of an enzyme called beta-glucaronidase, which is linked to estrogen-related cancers.
Broccoli is a member of the cruciferous family of vegetables (which also includes cauliflower, kale, cabbage and Brussels sprouts). Crucifers are rich in glucosinolates, which are sulphur compounds that help to neutralize and eliminate carcinogens, as well as isothiocyanates and indole-3-carbinol (I3C) – important nutrients that prevents estrogen-related cancers. Broccoli is also high in fibre, which helps us eliminate excess estrogen through our bowel movements.
Love these tubers already? Now you have another reason – they are high in Vitamin B6, a vitamin that helps with liver detoxification. Other foods rich in Vitamin B 6 include spinach, turkey and chicken. Any food that aids with liver detox is going to also help rid us of any excess hormones. You can read up on more detoxifying foods here.
What Are They: Thyroid hormones are responsible for energy and metabolism. They include T3, T4 and calcitonin. TSH, which is produced in the pituitary, helps to regulate the thyroid.
How Do They Get Out of Whack? Iodine deficiency, an inability to produce the proper amount of thyroid hormones, autoimmunity when the body attacks thyroid tissue, a growth in the thyroid.
BEST THYROID HORMONE BALANCING FOODS
Sea vegetables (nori, wakame, dulse, arame, kombu, hikiji, etc.) are amazing sources of iodine, an important mineral that helps us manufacture our thyroid hormones.
Brazil nuts are packed with selenium, an antioxidant that protects the thyroid gland and helps the body convert T4 into T3, the active form of the thyroid hormone. Having just a couple of Brazil nuts each day is enough to meet your selenium needs and they taste delicious, so this is very easy to do!
People with an underactive thyroid tend to have low levels of B12, and sardines are a great source of this important nutrient. Sardines also contain a good amount of selenium and a small quantity of iodine, so they are an overall thyroid-supportive food.
Iron-rich foods like spinach help to enhance thyroid function and aid the production of thyroid hormones. Its iron content, as well as the range of B vitamins, can also offer an energy boost to those who are feeling sluggish and tired.
Quinoa is definitely a superfood, with a broad spectrum of minerals, protein and fibre. A slow thyroid can also slow down digestion, leading to constipation. Quinoa’s high fibre content can get the bowels moving, and it’s a good source of zinc, another mineral that assists us with thyroid hormone production.
What Are They: The adrenal glands sit atop the kidneys. They are responsible for helping us manage stress, regulating our blood sugar and blood pressure, and help us produce sex hormones. Adrenal hormones include cortisol, adrenaline, DHEA, aldosterone and norephinephrine.
How Do They Get Out of Whack? Chronic physical and emotional stress, lack of sleep, poor diet (including excessive sugar, which sets off blood sugar imbalance)
BEST ADRENAL HORMONE BALANCING FOODS
These sweet peppers give us a boost of Vitamin C, an antioxidant vitamin that is essential to the function of the adrenal glands. We store a load of Vitamin C in our adrenals and when we are stressed, we use up a lot of it. Vitamin C-rich foods like bell peppers offer us replenishment, along with a spate of B vitamins that will offer us energy and help us reduce stress levels.
Dark leafy greens such as kale provide a wide spectrum of nutrients, in particular the antioxidant Vitamins K, A and C. Similar to bell peppers, kale’s Vitamin C will help shore up our adrenals and its B vitamins will nourish our nervous systems. These antioxidants also help to combat the damage caused by stress.
Blood sugar imbalances can disrupt our adrenal hormones. Sugary foods in particular will affect our blood sugar levels. Avocados are a rich source of healthy fats that will help keep our blood sugar levels even, and will support our nervous system function. They also contain Vitamin B5, otherwise known as pantothenic acid, a stress-fighting B vitamin that helps us handle stress.
Pumpkin seeds are a source of magnesium. When we are stressed, we can deplete our magnesium levels. Magnesium is our anti-stress mineral that works alongside Vitamin C and Vitamin B5 to support the adrenal glands and lower stress levels. In short, magnesium-rich foods like pumpkin seeds can help us relax!
Reach for eggs to grab a dose of choline, a vitamin that helps us produce the neurotransmitter acetylcholine, which is essential to the nervous system, brain health, memory and development. They also contain omega 3 fatty acids, the anti-inflammatory fats that support the brain. When our minds and nervous systems are healthy, we are better able to cope with stress. Aim to buy organic, pasture-raised eggs instead of conventional.
Millet is a gluten-free whole grain that contains a wide spectrum of B vitamins that will support our nerves and brains in times of stress. It also contains magnesium and fibre, which contributes to balanced blood sugar.
Aldosterone, one of our adrenal hormones, is responsible for fluid balance and blood pressure. If our adrenals aren’t functioning well and aldosterone levels fall, we can secrete more sodium, leading to salt cravings. A good dash of sea salt to your food or even a glass of water will help to replenish sodium levels and offer trace minerals. You can also try seaweeds or miso for their salt content.
Our hormones are a complicated business and it’s important to work with a qualified health practitioner to ensure you are able to properly correct any imbalances. Once you know which hormones are out of whack, you can use hormone-balancing foods to bring your health into harmony.