Benefits of Spirulina and Why Quality Differs Widely

Spirulina is a blue-green algae that naturally occurs in tropical and subtropical areas in fresh water lakes with a high pH.[1]  Let’s take a look at why so many people like to consume spirulina and why all spirulina products are not of equal quality.

In 1974, the World Health Organization described spirulina as “an interesting food for multiple reasons, rich in iron and protein, and … able to be administered to children without any risk.” They called it “a very suitable food.”[2]

Back in the late 1980s and early 90s, both NASA and the European Space Agency stated that spirulina should be one of the primary foods to be cultivated during long-term space missions.[3][4]

In 2003 the United Nations established the Intergovernmental Institution for the use of Micro-algae Spirulina against Malnutrition.[5]  

Spirulina was a food source for the Aztecs in Mexico from the 14th to 16th century. They harvested spirulina from Lake Texacoco as noted by one of Cortes’ soldiers.[6][7]

There are different varieties of spirulina available, spirulina platensis and spirulina maxima are the most common. Platensis occurs in Africa, Asia and South America, maxima is found in Central America and spirulina pacifica is endemic to the Hawaiian Islands.[8]

Dried spirulina is extremely protein rich and contains approximately 60% protein.[9][10] It has an easily digestible complete protein containing all essential amino acids. The protein in spirulina is superior to most plant proteins such as that from legumes.[9][11][12]

Spirulina is an excellent source of beta-carotene; perhaps ten times more concentrated than that of carrots. It is also an excellent source of many B-vitamins including thiamin, riboflavin, and niacin.

Spirulina contains ample amounts of many essential minerals such as iron, potassium, manganese and magnesium.

Spirulina’s lipid profile is also impressive. It contains about 8% lipids by weight and its awesome array is made up of GLA (gamma-linolenic acid), ALA (alpha-linolenic acid), LA (linoleic acid), SDA (stearidonic acid) EPA (eicosapentaenoic acid), DHA, (docosahexaenoic acid) and AA (arachidonic acid).[13][14][15][16]

The largest commercial producers of spirulina are located in the USA, Thailand, India, Taiwan, China, Pakistan, Burma, Greece, and Chile.[8] But it is also being grown on a smaller scale in many places around the globe.

There is a huge difference in quality between the different growers and harvesters. For example, spirulina is being grown in India and China where there are few regulations on pesticides and the use of irradiation. Heavy metal pollution is also of concern in many countries.

Spirulina grown in and around cities may be contaminated with pollution common to cities. For example, Bangkok Thailand is a polluted city, yet someone decided that a good place to grow spirulina is on a rooftop inside the city.

Some spirulina is being harvested out of polluted lakes. In many developing countries natural water sources are also used to bathe and may contain sewage.

Numerous studies have been conducted on spirulina. A study published in April 2016 concluded, “Spirulina platensis is a good source of antioxidant peptides”. [17]

A ground-breaking study also published in April 2016 concluded that spirulina extract inhibited viral replication and reduced virus induced mortality in a broad range of influenza viruses. [18]

And another study published in May 2016 found that spirulina platensis has anti-inflammatory properties.[19]

I choose to take only the highest quality spirulina grown at almost 9000 feet above sea level high in the Andes Mountains. At that pristine elevation far from polluted cities Andes spirulina is fed minerals from pure glacial water.

Being grown at such a high elevation the algae receives more photon energy from the sun resulting in a vibrant product. Andes spirulina is dried at low temperature to preserve nutrients.

References

[1] Habib, M. Ahsan B.; Parvin, Mashuda; Huntington, Tim C.; Hasan, Mohammad R. (2008). “A Review on Culture, Production and Use of Spirulina as Food for Humans and Feeds for Domestic Animals and Fish” (PDF). Food and Agriculture Organization of The United Nations.

[2] “What the United Nations says about Spirulina” (PDF).Spirulina and the Millennium Development Goals. Intergovernmental Institution for the use of Micro-algae Spirulina Against Malnutrition. December 2010..

[3] Characterization of Spirulina biomass for CELSS diet potential. Normal, Al.: Alabama A&M University, 1988.

[4] Cornet J.F., Dubertret G. “The cyanobacterium Spirulina in the photosynthetic compartment of the MELISSA artificial ecosystem.” Workshop on artificial ecological systems, DARA-CNES, Marseille, France, October 24–26, 1990

[5] “Charter” (PDF). Intergovernmental Institution for the use of Micro-algae Spirulina Against Malnutrition. 5 March 2003. Retrieved 2 July 2014.

[6] Diaz Del Castillo, B. The Discovery and Conquest of Mexico, 1517–1521. London: Routledge, 1928, p. 300.

[7] Osborne, Ken; Kahn, Charles N. (2005). World History: Societies of the Past. Winnipeg: Portage & Main Press.ISBN 1-55379-045-6.

[8] Vonshak, A. (ed.). Spirulina platensis (Arthrospira): Physiology, Cell-biology and Biotechnology. London: Taylor & Francis, 1997.

[9] Khan, Z; Bhadouria, P; Bisen, PS (October 2005). “Nutritional and therapeutic potential of Spirulina.”. Current pharmaceutical biotechnology 6 (5): 373–9.doi:10.2174/138920105774370607. PMID 16248810.

[10] Campanella, L; Russo, MV; Avino, P (April 2002). “Free and total amino acid composition in blue-green algae.”.Annali di Chimica 92 (4): 343–52. PMID 12073880.

[11] b c Ciferri, O (December 1983). “Spirulina, the edible microorganism”. Microbiol. Rev. 47 (4): 551–78.PMC 283708. PMID 6420655.

[12] b Babadzhanov, A. S.; Abdusamatova, N.; Yusupova, F. M.; et al. (2004). “Chemical Composition of Spirulina Platensis Cultivated in Uzbekistan”. Chemistry of Natural Compounds 40 (3): 276–279.doi:10.1023/b:conc.0000039141.98247.e8.

[13] Colla, LM; Bertolin, TE; Costa, JA (2003). “Fatty acids profile of Spirulina platensis grown under different temperatures and nitrogen concentrations.”. Zeitschrift für Naturforschung C 59 (1-2): 55–9. doi:10.1515/znc-2004-1-212. PMID 15018053.

[14] Golmakani, Mohammad-Taghi; Rezaei, Karamatollah; Mazidi, Sara; Razavi, Seyyed Hadi (March 2012). “γ-Linolenic acid production by Arthrospira platensis using different carbon sources”. European Journal of Lipid Science and Technology 114 (3): 306–314.doi:10.1002/ejlt.201100264.

[15] Jubie, S; Ramesh, PN; Dhanabal, P; Kalirajan, R; Muruganantham, N; Antony, AS (August 2012). “Synthesis, antidepressant and antimicrobial activities of some novel stearic acid analogues.”. European journal of medicinal chemistry 54: 931–5. doi:10.1016/j.ejmech.2012.06.025.PMID 22770606.

[16] Tokusoglu, O.; Unal, M.K. “Biomass Nutrient Profiles of Three Microalgae: Spirulina platensis, Chlorella vulgaris, and Isochrisis galbana”. Journal of Food Science 68 (4): 2003.doi:10.1111/j.1365-2621.2003.tb09615.x.

[17] http://www.ncbi.nlm.nih.gov/pubmed/27090190

[18] http://www.ncbi.nlm.nih.gov/pubmed/27067133

[19] http://www.ncbi.nlm.nih.gov/pubmed/27206252

 

 

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How to Use Ozone at Home for Healthy Teeth and Gums

Many years ago I had a dentist use a microscope to show me what types of bacteria I had living under my gum line. That same dentist suggested that I use a water flosser once per day to flush out the bacteria and spirochetes. After using the water flosser for one year I was retested and found that there were no more visible spirochetes and the amount of bacteria under my gum line was greatly reduced.

A few years later my dental hygienist told me that I had a few small spots where there were pockets beneath my gum line that were not 100% healthy. She suggested a deep cleaning. After understanding that a deep cleaning was a painful, time consuming and expensive process, I decided to do some research for alternatives. I learned about using ozone in a water flosser to kill the bacteria under the gum line that are difficult to access.

I discovered that anyone can purchase an ozone machine made to send ozone gas into a water tank or sauna and as long as you have an air pump to push the ozonated air into the water, it can be used to infuse ozone into a water flosser. Then simply follow the instructions for using a water flosser and send the ozonated water into the gum line.  I made a video on how to do that and you can see it at this link: https://www.youtube.com/watch?v=3F0RBEnGEOw&feature=em-uploademail

Important suggestions for ozone use in a water flosser:

  • Don’t let the sweet taste of ozonated water fool you. High concentrations of ozone can be a potent respiratory hazard and can also damage mucus membranes. I don’t suggest infusing your water flosser for more than 10 seconds with ozone gas.
  • Don’t use this type of ozone generator in a bathroom after a shower where the air is steamy. There are two reasons for this. 1- The moisture in the air will cause the ozone generator to create nitric acid which is corrosive to human skin and turns our skin yellow. 2- The moisture in the air will shorten the life of the corona discharge unit. Only use the machine in a dry room.
  • Don’t turn the pressure on the water flosser up too high. You want to gently clean the gum line, not power wash it. I use my Hydro Floss at 50% power. One Hundred percent power might damage your gums.
  • Check with your dentist. Unless your dentist suggests it, don’t do this every day. I do this two or three times a week at most.
  • Do not swallow the ozonated water. It should be spit it out.

The following bullet points are copied from the National Institutes of Health: 

Advantages

  • Disinfectant.
  • Anti-inflammatory.
  • Activation of intracellular metabolism of oral mucosa and dental wounds.
  • Improvement of regional circulation.
  • Stimulation of regenerative processes.
  • Hemostasis in capillary bleedings.
  • Painless procedures.

Disadvantages

  • Ozone toxicity if the level increases at 0.0007% per application.
  • Instability.
  • Not readily available.

Indications

  • Chronic or recurrent infections in the oral cavity.
  • Prophylaxis and prevention of dental caries.
  • Remineralization of pit and fissure caries, root and smooth surface caries.
  • Bleaching of discolored root canal treated teeth.
  • Sterilization of cavities, root canals, periodontal pockets, herpetic lesions.
  • Desensitization of extremely sensitive tooth necks.
  • Pre-washing of surgical sites.
  • Plaque control.
  • Contamination control.

Source: National Institutes of Health (NIH)

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3722714/

Link to multipurpose ozone machine below

http://www.rawfoodsbible.com/index.php?page=misc/ozone

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Marvellous Medicinal Mulberries

There has been a lot of talk about the health benefits of mulberries. Let’s take a look at some published studies and see what good science there is to back up these claims.

In traditional Chinese medicine, mulberries have long been known to be an anti-aging agent. In published studies the conclusion was that mulberries exhibit a memory enhancing effect.(1)(2)

Published studies have concluded that mulberry fruit possesses strong antioxidant activity and also contains high amounts of resveratrol.(3)(4)

In a study published in November 2013, mulberry fruit suppressed the development of intestinal inflammation and the formation of tumors in both petri dishes and in living beings.(5)

Studies have shown that mulberry extract can be helpful to diabetics. The majority of the research on mulberries used to help diabetics has focused on the leaves and less on the fruit.(6)(7)

However, a study published in April 2015 concluded that a substance in mulberry fruit may be a potential phytotherapeutic agent for the prevention of diabetes.(8)(9)  .

Mulberries have been effectively used in Chinese medicine for the prevention of coronary heart disease. Studies now back up this claim finding that the anthocyanin components in mulberries have a preventative effect on the formation of atherosclerosis.(9)

Mulberries are generally found in two shades of color, red and white. Red mulberries turn purple to almost black when ripe and white mulberries turn beige when dried. Both of them are delicious, nutritious and provide beneficial medicinal properties.

When I can’t pick them myself fresh off the tree I purchase only the best organic mulberries from Divine Organics.

By Craig B Sommers ND, CN

 

References

(1) http://www.ncbi.nlm.nih.gov/pubmed/23182412

(2) http://www.ncbi.nlm.nih.gov/pubmed/22952555

(3) http://www.ncbi.nlm.nih.gov/pubmed/27076749

(4) http://www.ncbi.nlm.nih.gov/pubmed/25593373

(5) http://www.ncbi.nlm.nih.gov/pubmed/26615818

(6) http://www.ncbi.nlm.nih.gov/pubmed/26467565

(7) http://www.ncbi.nlm.nih.gov/pubmed/26972284

(8) http://www.ncbi.nlm.nih.gov/pubmed/25501967

(9) http://www.ncbi.nlm.nih.gov/pubmed/25435295

(10) http://www.ncbi.nlm.nih.gov/pubmed/19241587

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Boost Your Brain Power with Bacopa

When it comes to herbs that improve human brain function, Bacopa monnieri shines brightly with numerous studies showing its efficacy. It also has a long history of use on the continent of India where they call it Brahmi. Current research suggests that the herb works because it increases certain brain chemicals that are involved in learning, thinking and memory.

Bacopa monnieri is native to the wetlands of Africa, Asia, Australia, Europe, southern India and North & South America. There are other varieties of bacopa besides the monnieri variety, but this article will only cover Bacopa monnieri and refer to it simply as bacopa.

A meta-analysis of nine randomized controlled trials on the cognitive effects of bacopa extract found that 437 people showed improved cognition. The study concluded that bacopa has the potential to improve cognition, particularly speed of attention.[1]

In 2002, a randomized double-blind placebo-controlled study was published showing the efficacy of bacopa. There were seventy-six adults between the ages of 40 and 65. The result showed that taking bacopa had a significant positive effect on the retention of new information.[2]

Another randomized double-blind placebo-controlled study published in 2012 concluded that bacopa can improve attention, cognitive processing and working memory in senior citizens.[3]

Promising research suggests that bacopa can be of help to those people with age related memory impairment including those with conditions such as dementia and Alzheimer’s disease.[4][5]

In Ayurvedic medicine, bacopa has also been used to treat epilepsy, stress, allergies, irritable bowel syndrome and more.[6] Looking through the medical literature one can find studies done on both humans and animals where bacopa has been used to treat a variety of conditions. These include: anxiety and depression, bronchitis and asthma, gastrointestinal disorders, hypothyroidism, Parkinson’s disease, schizophrenia, attention deficit disorder in children and more. [7][8][9] The research is ongoing.

Therapeutic doses of bacopa have not been associated with any dangerous side effects. However, it is not advised to take larger doses than recommended. The usual dose is 300mg of extract per day for a period of 12 weeks. It is known that Bacopa has been used safely in India by for at least the last several hundred years and perhaps even thousands of years.

Craig B Sommers ND, CN

[1] http://www.ncbi.nlm.nih.gov/pubmed/24252493

[2] http://www.ncbi.nlm.nih.gov/pubmed/12093601

[3] http://www.ncbi.nlm.nih.gov/pubmed/23320031

[4] http://www.ncbi.nlm.nih.gov/pubmed/20703343

[5] http://www.ncbi.nlm.nih.gov/pubmed/22700087

[6] http://www.ncbi.nlm.nih.gov/pubmed/24029249  

[7] http://www.ncbi.nlm.nih.gov/pubmed/24682000

[8] http://www.ncbi.nlm.nih.gov/pubmed/21925152  

[9] http://www.ncbi.nlm.nih.gov/pubmed/23326095
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Branched-Chain Amino Acids- Not Just For Building Muscle

Amino acids are the building blocks of protein. The words “branched chain” simply refers to their chemical structure. They are amino acids that have one carbon atom bound to more than two other carbon atoms.

A study was published in the journal Cell Metabolism which concluded that branched chain’ amino acids (BCAAs) may increase life span by inducing mitochondrial biogenesis, which is the spontaneous generation of new mitochondria.[1] Mitochondria are known for supplying cellular energy. The study also concluded that BCAAs upregulate (make more of) the expression of a pro-longevity gene.[2,3,4]

The BCAAs are leucine, isoleucine and valine. These are essential amino acids. Each of these three benefit many biological processes in our body. But they are best known for their ability to build our muscle mass.[5]

Isoleucine is needed for the formation of hemoglobin and to regulate blood sugar and energy levels. It plays an important role in muscle strength and endurance and is a source of energy for muscle tissues. Isoleucine also promotes muscle recovery after an intense workout.[6]

Leucine facilitates healing by modulating the release of natural pain-reducers called enkephalins. Leucine is a precursor of cholesterol and also increases the synthesis of muscle tissue.[7]

Valine is essential in muscle growth and development, muscle metabolism, and the maintenance of nitrogen balance in the body. It can be used as an energy source in place of glucose. Valine has also been used as a treatment for brain damage caused by alcohol.[8]

The BCAAs are formed during photosynthesis when sunlight shines on a green plant. Since BCAAs originate from plants, and eating low on the food chain is the least polluted source of nutrition, I look towards plants to get mine. Beans and peas are a good source for all of the BCAAs. And if you’re interested in protein powder, pea protein powder happens to be high in BCAAs. My favorite source of the BCAAs is Warrior Blend, from SUNWARRIOR.

Craig B Sommers ND, CN

1 D’Antona G, Ragni M, Cardile A, et al. Branched chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice. Cell Metab. 2010 Oct 6;12(4):362-72.

2 Chowanadisai W, Bauerly KA, Tchaparian E, Wong A, Cortopassi GA, Rucker RB. Pyrroloquinoline quinone stimulates mitochondrial biogenesis through cAMP response element-binding protein

phosphorylation and increased PGC-1alpha expression. J Biol Chem. 2010 Jan 1;285(1):142-52.

3 Kelly G. A review of the sirtuin system, its clinical implications, and the potential role of dietary activators like resveratrol: part 1. Altern Med Rev. 2010 Sep;15(3):245-63.

4 Kelly GS. A review of the sirtuin system, its clinical implications, and the potential role of dietary activators like resveratrol: part 2. Altern Med Rev. 2010 Dec;15(4):313-28. 


5 Karlsson, H. K. R. (2004). "Branched-chain amino acids increase p70S6k phosphorylation in human skeletal muscle after resistance exercise". AJP: Endocrinology and Metabolism287: E1–7. doi:10.1152/ajpendo.00430.2003. PMID 14998784.

6,7,8 http://en.wikibooks.org/wiki/Structural_Biochemistry/Proteins/Amino_Acids#Amino_Acid_Subdivisions
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C-Reactive Protein, a Known Risk Factor

C-reactive protein, abbreviated CRP, is produced in the liver and released into the bloodstream when there is inflammation in the body.[1] It can be measured in the blood, and is a known risk factor for many common diseases. Unfortunately, the blood test does not pinpoint where the inflammation is coming from or what is causing it.

Research shows that people with high CRP concentrations are more likely to develop heart attacks, strokes and severe peripheral vascular disease.[2]   Research also shows that people with elevated levels of CRP are at an increased risk of diabetes.[3][4]

An elevated level of CRP can be observed in people with inflammatory bowel diseases such as ulcerative colitis and Crohn’s disease.[5]

The normal concentration of CRP in a healthy person’s blood serum is usually lower than 10 mg/L. This number increases slightly with aging. Levels of 10–40 mg/L are found in women during late pregnancy and in people with mild inflammation and viral infections. Active inflammation and bacterial infection bring the level up from 40–200 mg/L. Severe bacterial infections and burns may bring the level to greater than 200 mg/L.[6]

Fortunately for us, it is possible to lower CRP. There are both, natural methods and pharmaceutical drugs that will the job. However, I suggest the natural approach because anti-inflammatory drugs are known to have many unhealthy side effects. The natural approach usually yields positive effects such as increased vitality.

Diet plays a major role in the elevation of CRP. A study was done on over 700 nurses. They split the group into four segments. Those in the group with the highest trans-fat consumption had blood levels of CRP that were 73% higher than those in the group with the lowest trans-fat consumption.[7]  Saturated fats have also been shown to raise CRP.

Hidden food allergies are a common cause of elevated levels of CRP.  Foods to avoid include refined glutinous flour products, refined sugars and processed food.

Bacterial infections, viral infections, obesity, stress, cigarette smoking, lack of exercise, toxins such as heavy metals, pesticides [8] and mold spores have also been associated with elevated levels of CRP.

There are healthy nutritional supplements that have been shown to lower CRP. Omega 3 fats are highly anti-inflammatory. The cleanest source of omega 3 is DHA from algae oil.

You can also add turmeric to your diet. In Italy, there was a three-month trial with 50 people. A team of researchers were investigating the effect of treating people who had arthritis with an oral turmeric extract called curcumin.  After 90 days, blood tests showed a 16-fold decline in C-reactive protein levels.[9]

To sum it up, I suggest the consumption of a plant based diet composed primarily of unprocessed whole food, avoiding the unhealthy fats and the common allergenic foods, gentle but regular exercise and the practice of stress reduction techniques.

Regardless of how you feel, studies show that it is important for everyone to be sure that their CRP level is not elevated. Many researchers now believe that knowing your CRP level is more important than knowing your cholesterol level.

[1] Pepys MB, Hirschfield GM (June 2003). "C-reactive protein: a critical update". J. Clin. Invest. 111 (12): 1805–12. doi:10.1172/JCI18921.PMC 161431. PMID 12813013.

[2]- Clearfield MB (September 2005). "C-reactive protein: a new risk assessment tool for cardiovascular disease". The Journal of the American Osteopathic Association 105 (9): 409–16. PMID 16239491.

[3] Pradhan AD, Manson JE, Rifai N, Buring JE, Ridker PM (July 2001). "C-reactive protein, interleukin 6, and risk of developing type 2 diabetes mellitus".JAMA 286 (3): 327–34. doi:10.1001/jama.286.3.327. PMID 11466099.

[4] Dehghan A, Kardys I, de Maat MP, Uitterlinden AG, Sijbrands EJ, Bootsma AH, Stijnen T, Hofman A, Schram MT, Witteman JC (March 2007). "Genetic variation, C-reactive protein levels, and incidence of diabetes". Diabetes 56(3): 872–8. doi:10.2337/db06-0922. PMID 17327459.

 [5]-Liu S, Ren J, Xia Q, Wu X, Han G, Ren H, Yan D, Wang G, Gu G, Li J (May 2013). "Preliminary Case-control Study to Evaluate Diagnostic Values of C-Reactive Protein and Erythrocyte Sedimentation Rate in Differentiating Active Crohn's Disease From Intestinal Lymphoma, Intestinal Tuberculosis and Behcet's Syndrome". Am. J. Med. Sci. 346 (6): 467–72.doi:10.1097/MAJ.0b013e3182959a18.PMID 23689052

[6] Clyne B, Olshaker JS (1999). "The C-reactive protein". J Emerg Med 17 (6): 1019–25. doi:10.1016/S0736-4679(99)00135-3. PMID 10595891.

[7]  Lopez-Garcia E, Schulze MB, Meigs JB, Manson JE, Rifai N, Stampfer MJ, Willett WC, Hu FB (March 2005). "Consumption of trans fatty acids is related to plasma biomarkers of inflammation and endothelial dysfunction". J. Nutr.135 (3): 562–6. PMID 15735094.

[8] http://www.ncbi.nlm.nih.gov/pubmed/22509446

[9] http://www.ncbi.nlm.nih.gov/pubmed/20657536

 

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Acid Reflux, Treat the Cause, Not the Symptoms

Stomach acid is essential for good digestion and absorption of nutrients from your diet. Suppressing stomach acid only treats the symptoms, it does not treat the cause of the disease. In fact, it can actually make things worse. Taking acid blocking drugs long enough will cause numerous nutrient deficiencies, including vitamin, mineral, and especially vitamin B12 and amino acid deficiencies.

Studies have shown that people who take acid blocking drugs long term, may end up with a variety of illnesses including osteoporosis, hip fracture, IBS, fatigue, nerve damage and eventually dementia. Long term use can also lead to an overgrowth of clostridia in the small intestine that can be life threatening.

Stomach acid, also called hydrochloric acid (HCL) is needed for both, separating vitamin B12 from food to make it absorbable and also for breaking down protein rich food so that the amino acids can be absorbed. Not enough amino acids can lead to depression, insomnia, brain fog, anxiety, trouble building and maintaining muscles and more. Amino acids are precursors for essential neurotransmitters which are needed for proper brain function.

Stomach acid is essential for killing bacteria and other pathogenic organisms that might be ingested while eating or drinking. If the stomach acid is too low, these pathogens can colonize in your intestines and cause many health problems.

When pathogenic organisms take up residence in your digestive tract, they can create gas and bloating while feeding on the food you have eaten. The pressure from the gas and bloating can push up through the stomach and then through the upper stomach valve (esophageal sphincter) causing acid reflux.

A urine test or breath test for small bowel bacterial overgrowth can diagnose the presence of certain strains of bacteria.

Hiatal hernia can also cause acid reflux. This can be diagnosed with an x-ray. Extra fat around the midline can also contribute. Stress is another contributing factor.

Food allergies to gluten and dairy products may also contribute to acid reflux. I suggest completely eliminating these two foods for a month or so and see if it makes a difference. Other food allergies may also be a factor.

Nutritional deficiencies can also lead to acid reflux. If you are on a low sodium diet you might become deficient in the minerals sodium and chloride. Zinc, magnesium, vitamin C and B vitamins are also needed to have a properly functioning stomach.

Helicobacter pylori, is another common cause of acid reflux. However, unless you go to a holistic or functional medicine doctor, you most likely will not get tested for it unless you have an ulcer. H-pylori can be diagnosed with a simple stool test.

Numerous holistic and functional medicine doctors have been testing their clients who have acid reflux and finding that most of them have low stomach acid levels. Not high levels!

The following is an example of how low stomach acid can lead to acid reflux.

When the acid level in the stomach is too low, the upper stomach valve might not stay closed and the acid from the stomach can leak up into the throat. Our body needs to sense enough HCL in the stomach in order for the upper valve to stay closed properly. Note that in this case, acid reflux is caused by low stomach acid and not by high stomach acid. It is very often the case that people identify acid reflux as having too much stomach acid while most of the time it is caused by not enough stomach acid.

 

Traditional medical doctors are trained to prescribe acid blocking drugs to treat the symptoms and seem to overlook the dangers of using these drugs. Instead they should be testing the person’s stomach acid level, testing for microbial overgrowth or looking for other causes.

The gastric analysis by radio telemetry test is the most accurate way to measure stomach acid. One just needs to swallow a small capsule with a radio transmitter that measures the pH of the stomach. The result of this test provides you with a graph showing your pH levels at regular intervals over time. If the test shows the HCL level to be low, a betaine HCL supplement can be taken with meals to raise the acid which may keep the upper valve closed when food is present.

There are also two other tests. These can be done at home but are not very accurate. The baking soda test is performed by drinking ¼ teaspoon of baking soda mixed into 5 ounces of water first thing in the morning after waking up. Because the baking soda is very alkaline and your stomach should be very acidic, it will produce carbon dioxide gas that causes burping. You need to measure the exact amount of time that passes from the time you drink the solution until the time that the burping starts. The result gives you an idea of the amount of HCL in the stomach. If it takes more than five minutes to start burping, in may mean that you have low stomach acid. Please note that this test is not always accurate because there are many variables that can give false results.

The betaine HCL test for low stomach acid is the most reliable at home test you can perform. The test is done by taking a betaine HCL pill in the middle of a protein rich meal. If there is no burning sensation after the meal, then do the same thing at your next protein rich meal. If you do this several times and there is no burning sensation, most likely you have low stomach acid.

You may then take 2 pills in the middle of your next protein rich meal and wait to see if there is a burning sensation. Again, if there is no sensation, do the same thing at your next protein rich meal. You can raise the amount of pills by one after every few protein rich meals and see how many pills it takes to feel the burning sensation. When you finally get to the point that you feel the burning, you should then take one less pill during the next meal.

Now that you have determined how many pills your body needs, continue to supplement the HCL with protein rich meals. Over time, your body should need less and less of the HCL supplements as your stomach acid levels normalize. Eventually, you should be able to go off the supplement and not have reflux if the reflux was caused by low stomach acid.

If you have acid reflux, no matter what the cause, it is important to avoid overeating. You will also need to avoid acidic food items such as tomato sauce, fried food, soda, coffee, alcoholic beverages, spicy food and citrus. It is also very important to not eat for a few hours before lying down.

I suggest working with a qualified practitioner who can help you find the cause of the reflux and then slowly wean you off acid blocking drugs. Quitting acid blocking drugs can be dangerous if not supervised by an experienced doctor.

And last thing I would like to share is that there are nutritional supplements that can help. Probiotics are essential to colonize the intestines with good bacteria. DGL (deglycerized licorice) can help with the symptoms. Magnesium is an important nutrient for the proper function of the valves at the top and bottom of the stomach. These valves are actually muscles and muscles need magnesium. And a high quality multivitamin and protein supplement will help replenish nutritional deficiencies that were caused by the acid blocking drugs.

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How to Grow Strong Healthy Nails

Our nails can reflect our general state of health. No one wants to have weak brittle nails. Yet having brittle nails, also known as onychorrhexis, is a very common condition affecting approximately 20 percent of the population and is more common in women.[1]

Human fingernails and toenails are primarily composed of a protein called keratin and also contain an array of minerals. Keratin is an extremely strong protein.

Like other proteins, keratin is composed of amino acids. Keratin has large amounts of the sulfur-containing amino acid cysteine. Cysteine is required for giving nails their strength and rigidity.[2]

The mineral composition of a human nail includes: calcium, copper, iron, magnesium, sodium, sulphur and zinc. A deficiency in any one of these minerals can affect the health and growth of our nails.[3]

Aside from having a deficiency in the building blocks of nails, brittle nails can be caused by a variety of different things some of which include: chronic dehydration, a deficiency in omega-3 fatty acids and a biotin deficiency. [4]

Several chronic health conditions can also cause brittle nails, including: anorexia, bulimia, iron deficiency anemia, and underactive thyroid.[5] Furthermore, psoriasis has been linked to brittle nails. Brittle nails can even be a side effect of certain pharmaceutical medications.

And let’s not overlook the fact that nails which are excessively exposed to water, soap or solvents can also become brittle.

If you are wondering why some of your nails grow slower than the rest, there is no need to worry. In humans, the nail of the index finger may grow faster than that of the little finger and fingernails may grow up to four times faster than toenails.[6]

Provided you do not have a medical condition, keeping well-nourished with all the building blocks that nails need can result in strong healthy nails. A balanced diet composed primarily of a variety of unprocessed whole food is a great start.

To take your nails to the next level try supplementing your diet with a high quality protein powder, a good multi mineral complex, biotin and omega-3 fatty acids.

[1] Rapini, Ronald P.; Bolognia, Jean L.; Jorizzo, Joseph L. (2007). Dermatology: 2-Volume Set. St. Louis: Mosby. ISBN 1-4160-2999-0

[2] http://www.wisegeek.org/what-is-keratin.htm

[3] https://www.ncbi.nlm.nih.gov/pubmed/20620759  

[4] http://www.ncbi.nlm.nih.gov/pubmed/8477615

[5[ James, William; Berger, Timothy; Elston, Dirk (2005). Andrews' Diseases of the Skin: Clinical Dermatology. (10th ed.). Saunders. ISBN 0-7216-2921-0

[6]  Ravosa, Matthew J.; Dagosto, Marian (2007). Primate origins: adaptations and evolution. Springer. pp. 389–90. ISBN 0-387-30335-9
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Ten Reasons to Choose Plant Protein Over Whey Protein

  1. Whey protein linked to cancer promotion:

The hormone IGF-1 only occurs in animal protein, one of the best sources being protein from cow’s milk. IGF-1 has been shown to promote cancer cell growth in humans.[1]  Studies show that increased levels of IGF-1 lead to increased growth of existing cancer cells.[1] Dietary interventions and modifications such as vegan diets have been shown to down regulate (make less of) IGF-1 and have been associated with lower risk of cancer.[2]  It has been proven that people with exceptionally low levels of IGF-1 (Laron syndrome) are resistant to cancer.[3][4][5][6]   IGF-1 does not occur in plant protein and plant protein has not been shown to promote cancer growth.

  1. Whey protein linked to aggravation of acne:

According to studies, healthy male adults may develop acne after the consumption of whey protein. The studies indicate that dairy protein enhances IGF-1 and acne aggravation.[7][8] Plant protein has not been linked to acne.

  1. Whey protein linked to flatulence, bloating, cramps, diarrhea, nausea and rumbling stomach:

Seventy-five percent of all African American, Jewish, Mexican American, and Native American adults are lactose intolerant.[9] Both whey concentrate and whey isolate contain lactose.[10]  However, whey concentrates contain higher amounts of lactose.  Lactose intolerant people will suffer a variety of digestive issues which may include abdominal bloating, cramps, flatulence, diarrhea, nausea, vomiting and a rumbling stomach.[11]   Lactose only occurs in dairy protein and does not occur in plant protein.

  1. Whey protein may cause constipation:

Numerous studies concluded that constipation in children can have an allergic pathogenesis to whey and other dairy proteins.[12][13][14] Plant protein has not been linked to constipation.

  1. Whey protein can dangerously lower blood sugar:

Whey protein has been shown to lower blood sugar.[15] Caution is advised for people with diabetes or low blood sugar and in those taking drugs that affect blood sugar. According to Mayo Clinic, blood sugar levels may need to be monitored by a qualified healthcare professional and medication adjustments may be necessary for those consuming whey protein.[16] Plant protein has not been shown to have effects on blood sugar.

  1. Whey protein may cause abnormal heart rhythms:

According to Mayo Clinic, whey protein may cause abnormal heart rhythms.[16]  Plant protein has not been shown to effect heart rhythms.

  1. Whey protein may cause headaches:

According to Mayo Clinic, whey protein may cause headaches. [16] Plant protein has not been linked to headaches.

  1. Whey protein may increase the risk of diabetes:

According to Mayo Clinic, whey protein may increase the risk of diabetes. [16] Plant protein has not been linked to increased risk of diabetes.

  1. Whey protein may increase the risk of bleeding:

According to Mayo Clinic, whey protein may increase the risk of bleeding.[16] Caution is advised in people with bleeding disorders or in those taking drugs that may increase the risk of bleeding. Dosing adjustments may be necessary. Plant protein has not been shown to increase the risk of bleeding.

  1. Whey protein may cause drowsiness:

According to Mayo Clinic, drowsiness or sedation may occur when consuming whey protein. They advise using caution if driving or operating heavy machinery. Plant protein has not been linked to drowsiness or sedation.[16]

References 

 [1] Arnaldez F, Helman L (June 2012). "Targeting the insulin growth factor receptor 1". Hematol. Oncol. Clin. North Am. 26 (3): 527–42, vii–viii.doi: 10.1016/j.hoc.2012.01.004. PMC 3334849. PMID 22520978.

[2] McCarty M (1999). "Vegan proteins may reduce risk of cancer, obesity, and cardiovascular disease by promoting increased glucagon activity". Med. Hypotheses 53 (6): 459–85. doi:10.1054/mehy.1999.0784.PMID 10687887.

[3] Gallagher E, LeRoith D (April 2011). "Is growth hormone resistance/IGF-1 reduction good for you?". Cell Metab. 13 (4): 355–6.doi:10.1016/j.cmet.2011.03.003. PMID 21459318.

[4]  Guevara-Aguirre, J; Balasubramanian, P; Guevara-Aguirre, M; Wei, M; Madia, F; Cheng, CW; Hwang, D; Martin-Montalvo, A et al. (2011). "Growth Hormone Receptor Deficiency Is Associated with a Major Reduction in Pro-Aging Signaling, Cancer, and Diabetes in Humans". Science Translational Medicine 3 (70): 70ra13.doi:10.1126/scitranslmed.3001845. PMC 3357623.PMID 21325617.

[5] Bai, Nina. "Defective Growth Gene in Rare Dwarfism Disorder Stunts Cancer and Diabetes". Scientific American. Retrieved17 February 2011.

[6] Winerman, Lea. "Study: Dwarfism Gene May Offer Protection From Cancer, Diabetes". PBS. Retrieved 17 February 2011.

[7] Dermatology. 2012; 225(3):256-8. doi: 10.1159/000345102. Epub 2012 Dec 13. http://www.ncbi.nlm.nih.gov/pubmed/23257731

[8] Nestle Nutr Workshop Ser Pediatr Program. 2011; 67: 131-45. doi: 10.1159/000325580. E pub 2011 Feb 16. PMID: 21335995  http://www.ncbi.nlm.nih.gov/pubmed/21335995 

[9] Lactose Intolerance". Johns Hopkins Health Library. Retrieved 2014-02-18. 

[10] General guidelines for milk allergy". Oregon Health & Science University.

[11] Lactose Intolerance". National Digestive Diseases Information Clearinghouse (NDDIC). NIDDK. Retrieved 29 November 2011.

[12] Davidson, M, Kugler, MM, Baue, CH. Diagnosis and management in children with severe and protracted constipation and obstipation. J PEDIATR. 1963;62:261–275.

[13] Lothe, L, Lindberg, T. Cow's milk whey protein elicits symptoms of infantile colic in colicky formula-fed infants: a double- blind, crossover study. Pediatrics. 1989;83:262–266.

[14] Abrahamian, FP, Lloyd-Still, JD. Chronic constipation in childhood: a longitudinal study of 186 patients. J Pediatr Gastroenterol Nutr. 1984;3:460–467.

[15] J Nutr Biochem. 2014 Jan;25(1):36-43. doi: 10.1016/j.jnutbio.2013.08.012. Epub 2013 Oct 5.

[16] http://www.mayoclinic.org/drugs-supplements/whey-protein/safety/hrb-20060532
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The ‘What’, ‘Where’ and ‘Why’ of Carnitine

Carnitine is found in the bodies of all mammals and many other living organisms. Carnitine’s most well-known function is transporting fatty acids into each cell’s mitochondria (the energy center of the cell) for breakdown into energy.

The word carnitine is composed of the root word carne, meaning flesh. Red meat is a good source of carnitine but according to the National Institutes of Health (NIH), eating red meat can shorten your life span.[1]

Fortunately carnitine can be found in commonly consumed plants. There are a variety of sources including nuts and seeds. The following list has been compiled using radioisotopic technology to determine the carnitine content in common foods.[2] This list is by no means complete.

Listing higher sources first:

  • Tempeh 100 g contain 19.5 mg
  • Cod fish 100 g contain 5.6 mg
  • Chicken breast 100 g contain 3.9 mg
  • Whole milk 100 ml contain 3.3 mg
  • Potatoes 100 g contain 2.4 mg
  • Lentils 100 g contain 2.1 mg
  • Avocado one medium sized contains 2 mg
  • Sweet Potatoes 100 g contain 1.1 mg
  • Cottage cheese 100 g contain 1.1 mg
  • Raisins 100 g contain 0.8 mg
  • Whole wheat bread 100 g contain 0.36 mg
  • Carrots 100 g contain 0.3 mg
  • Bananas 100 g contain 0.2 mg
  • Apples (without skin) 100 g contain 0.2 mg
  • Asparagus 100 g contain 0.195 mg
  • White bread 100 g contain 0.147 mg
  • Peanut butter 100 g contain 0.083 mg
  • Rice 100 g contain 0.0449 mg
  • Egg 100 g contain 0.0121 mg
  • Orange juice 100 ml contain 0.0019 mg

When carnitine occurs in animal tissue, it is synthesized from the amino acids lysine and methionine. Humans synthesize carnitine in their bodies from these amino acids in the same manner that animals do.[3]

According to the National Institutes of Health, healthy children and adults do not need to consume carnitine from food or supplements because the liver and the kidneys produce sufficient amounts to meet daily needs.[4,5,6]

In 1989 The Food and Nutrition Board of the National Academies (formerly National Academy of Sciences) declared that carnitine was not an essential nutrient.[6]

Carnitine deficiencies are rare. Even strict vegetarians and vegans show no signs of carnitine deficiency.[7] The only time I have personally encountered a person deficient in carnitine was when they had been taking CoQ10 in doses of 200 mg a day for extended periods of time. This condition was easily corrected by taking a carnitine supplement and cutting back on CoQ10.

Studies that have been done using carnitine supplements to improve exercise performance show conflicting results. Some studies conclude no significant effect on exercise performance.[8][9] Other studies conclude a beneficial effect on training, competition and recovery from strenuous exercise.[10]

There are two main forms of carnitine supplements, L-carnitine and acetyl L-carnitine (also sometimes spelled acetylcarnitine or ALCAR).

The supplemental form called L-carnitine is usually taken by people trying to lose weight by converting their fat into energy. However, published studies showing the efficacy of using L-carnitine for weight loss are limited.

The form called acetyl L-carnitine is known to be more easily absorbed by the small intestine and is also known for its ability to pass through the blood brain barrier. Studies conclude that senior citizens with age related mental decline taking acetyl L-carnitine improved their mental functioning, especially in those with Alzheimer’s disease.[11][12]

In January of 2016 a meta-analysis of randomized controlled trials was published that showed a significant reduction of lipoprotein(a) levels following carnitine supplementation.[13] This is great news for those with genetically high Lp(a) levels because an elevated level of Lp(a) is a risk factor for heart disease and stroke.

One study found benefit for people with pancreatic cancer.[14]  Another study found benefit for people with diabetic peripheral neuropathy.[15]  Studies are ongoing about the use of carnitine supplements to treat various disease conditions.

Rare side effects of supplementing with carnitine include fishy body odor and rash. Taking large doses could result in nausea, diarrhea and cramps. People on prescription medication or those with heart disease, excessive, fatigue or a thyroid condition should talk to a doctor before taking carnitine.

For people who choose to supplement with carnitine I suggest using the product as directed on the label. No advantage appears to exist in taking an oral dose of carnitine greater than two grams at a time because absorption studies indicate saturation at this dose.[16]

By Craig B Sommers ND, CN

[1] http://www.nih.gov/news-events/nih-research-matters/risk-red-meat  

[2] Demarquoy, Jean; Georges, Béatrice; Rigault, Caroline; Royer, Marie-Charlotte; Clairet, Amélie; Soty, Maud; Lekounoungou, Serge; Le Borgne, Françoise (2004-06-01)."Radioisotopic determination of l-carnitine content in foods commonly eaten in Western countries". Food Chemistry 86 (1): 137–142. doi:10.1016/j.foodchem.2003.09.023

[3] http://www.ncbi.nlm.nih.gov/pubmed/21561431

[4] Rebouche CJ. Carnitine. In: Modern Nutrition in Health and Disease, 9th Edition (edited by Shils ME, Olson JA, Shike M, Ross, AC). Lippincott Williams and Wilkins, New York, 1999, pp. 505-12.

[5] The editors. Carnitine: lessons from one hundred years of research. Ann NY Acad Sci 2004;1033:ix-xi.

[6] National Research Council. Food and Nutrition Board. Recommended Dietary Allowances, 10th Edition. National Academy Press, Washington, DC, 1989.

[7] http://lpi.oregonstate.edu/infocenter/othernuts/carnitine/

[8] Brass EP. Supplemental carnitine and exercise. Am J Clin Nutr 2000;72:618S-23S.

[9] http://www.ncbi.nlm.nih.gov/pubmed/21561431

[10] http://www.ncbi.nlm.nih.gov/pubmed/15212755

[11] http://www.ncbi.nlm.nih.gov/pubmed/1944900

[12] http://www.ncbi.nlm.nih.gov/pubmed/18801359

[13] http://www.ncbi.nlm.nih.gov/pubmed/26754058

[14] http://www.ncbi.nlm.nih.gov/pubmed/22824168

[15] http://www.ncbi.nlm.nih.gov/pubmed/18940920

[16] Bain, Marcus A.; Milne, Robert W.; Evans, Allan M. (2006-10-01). "Disposition and metabolite kinetics of oral L-carnitine in humans". Journal of Clinical Pharmacology 46 (10): 1163–1170.doi:10.1177/0091270006292851. ISSN 0091-2700. PMID 16988205
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