Glutamine Heavy Exercise & Leaky Gut

Glutamine is one of the most important amino acids for building and maintaining muscles in the human body. Glutamine is also the most common amino acid found in human muscles. If you go through the medical literature you will find studies showing that both physical stress from heavy exercise and emotional stress can cause a glutamine deficiency. The literature also shows that heavy exercise increases intestinal permeability in humans. These studies indicate that heavy exercise should be complemented with glutamine consumption. Researchers have proven that glutamine helps to maintain muscle integrity and to prevent intestinal permeability because it is an essential building block of both.

 

The following is an example of a common chain of events to be careful of. People who exercise heavily will often take non-steroidal anti-inflammatory drugs to deal with the discomfort from injuries induced by the exercise. What these people may not realize is that the anti-inflammatory drugs can cause damage to the intestinal tract leading to intestinal permeability. A person may already be glutamine deficient from the exercise. If they are not supplementing with glutamine they will not have enough in their body to repair the damage done in the intestinal tract from the drug. This results in increased intestinal permeability. The increased intestinal permeability, also known as leaky gut syndrome, causes food particles that have not been fully broken down to get absorbed. Those food particles cause a rise in inflammation inside the body. The rise in inflammation may delay the healing of the injured body part and cause a vicious cycle. In summary, the anti-inflammatory drugs cause the person to become more deficient in glutamine leading to more pain and an increasing desire to take more of the anti-inflammatory drugs.

 

Glutamine supplementation is important for those who choose to exercise heavily. Many books have been written explaining how numerous problematic health conditions arise in the intestinal tract.  If you are undergoing any type of stress I strongly suggest that you make sure that you consume adequate protein and glutamine in your diet and that you avoid anti-inflammatory drugs. There are many anti-inflammatory herbs such as turmeric that do not have harmful side effects but instead have many beneficial properties.

 

We can make glutamine inside our body from other amino acids provided we have enough of the mineral zinc. That is why they call glutamine a non-essential amino acid. However, zinc deficiencies are very common in all types of individuals. Men are especially prone to zinc deficiencies because men loose zinc with every ejaculation.

 

Intestinal permeability can be repaired by glutamine supplementation, adequate mineral intake and probiotics. My assurance that I consume enough glutamine comes from SUNWARRIOR protein. I know that what I am doing is working because I took the micronutrient test from SpectraCell laboratories and found that both my glutamine level and my mineral levels were excellent. Just one serving of the Warrior Blend provides 3,470 mg of highly absorbable and utilizable glutamic acid which is another name for glutamine.

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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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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.2012.01.004PMC 3334849PMID 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.2011.03.003PMID 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.3001845PMC 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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