Protein Zaps Belly Fat

In a sedentary, over-fed, yet undernourished society, the dissolution of abdominal fat with a magic bullet is an incessant quest.  First, we cut out the junk food.  Then we try to eat a balanced diet, the definition of which seems elusive.  After that, we add the foods we think are good for us.  Still, we can’t burn the belly.  Next, we look closer at the ads for products guaranteed to get rid of excess adiposity.  Only after these promises fail do we notice the small print that says the results you see are not typical, and that it must be accompanied by diet and exercise.  Oh, no, I have to work at it.  What happened to the magic bullet?

To be realistic about losing fat, we have to do something actively, not passively.  But that might be as simple as upping the ante on protein.  However, it just isn’t plain, old protein, but the quality of the protein that makes the difference.  Actually it’s the amino acids, the protein building blocks whose chemical properties determine the biological activity of the proteins of which they are a constituent.   Proteins catalyze many of the reactions in living cells—enzymes, hormones, antibodies.  The folding of proteins into three dimensional structures depends upon the information in the amino acid sequences.  Although several hundred kinds of amino acids have been found in nature, only twenty or so apply to human peptides (two or more aminos joined together) and proteins.  Low levels of certain amino acids telegraph as specific problems that include hormone imbalances, lack of concentration, irritability, and even depression.

Based on their individual characteristics, amino acids may be classified as essential, non-essential, or conditionally essential.  Essentiality does not bespeak importance, but acquisition.  The essential ones need to be acquired from diet because they can’t be made by the body.  Here’s a quick rundown of the essential amino acids, with some of their features:

Leucine — a BCAA (branched chain amino), is used for tissue repair after surgery, to build muscle mass, to balance blood sugar, to de-stress, to manufacture HGH (human growth hormone), and for protein synthesis.  It helps to maintain healthy bone, skin, and hemoglobin.

Isoleucine — a BCAA (branched chain amino), addresses mental disorders, tissue rebuild after surgery, energy, muscle, endurance, and blood hemoglobin.

Valine — a BCAA (branched chain amino), is used for mental and emotional disorders, for glycogen production, and in alcohol and drug recovery.  It’s used in muscle metabolism, where it contributes to the structure of proteins.

Lysine — absorbs and conserves calcium and maintains nitrogen balance.  It helps to make collagen, to manage cholesterol and triglycerides, and bolsters the immune system.  (People use this for fever blisters.)

Methionine — has been used to address schizophrenia, and the muscle weakness of Parkinson’s.  It helps to detoxify heavy metals, to form collagen, to prevent brittle hair and nails, to protect against radiation toxicity, and to control histamine levels that may affect cognitions.  Additionally, methionine is a strong antioxidant.

Phenylalanine — addresses chronic pain, helps to make endorphins, assists the manufacture of norepinephrine to direct nerve signals in the brain, promotes alertness and elevates mood, and has been used to treat arthritis, depression, migraines, and Parkinson’s disease.

Threonine — helps to maintain proper protein balance, is important to collagen, elastin, and tooth enamel, aids wound healing, may prevent fatty liver, and assists assimilation.

Tryptophan — is a natural relaxant that helps to alleviate insomnia.  It stabilizes mood, fights migraines and fibromyalgia, and may aid in weight control by reducing appetite.

Histidine — is conditional in adults, but deemed essential to infants and children, and is the immediate precursor to histamine (and carnosine).  Histidine is abundant in hemoglobin, and has been used in the treatment of arthritis, gastric disorders, and the maintenance of the myelin sheath.  It protects against heavy metals and radiation, and aids in the manufacture of red and white blood cells.

The remaining amino acids are non-essential, and are produced from the breakdown of proteins or from the essential ones.  They and a few of their jobs are:

Alanine — (the other component of carnosine) transfers nitrogen from peripheral tissue to the liver in glucose metabolism and guards against the buildup of toxins when muscle tissue is broken down to meet energy needs, as occurs in serious aerobic exercise.

Arginine — is considered the natural Viagra, relaxes blood vessels, supports thymus immunity activity, helps to neutralize ammonia, assists the release of growth hormones, and stimulates the pancreas to release insulin.

Aspartic Acid — from asparagine, is used to treat chronic fatigue and depression, aids the elimination of ammonia, rejuvenates cell activity, and helps to move minerals across the intestinal lining into the bloodstream.

Cysteine — (and cysteine) works as a potent antioxidant and protects against radiation and the toxins of tobacco smoke.  It promotes recovery from burns and promotes the burning of fats. Cystine is formed from the oxidation of two cysteines, but has the same character and activity.

Glutamic Acid — is an excitatory neurotransmitter that is called glutamine after coupling with ammonia, which is carried to the liver for disposal.  Free glutamic acid is important to the metabolism of fats and sugars, and helps to carry potassium into spinal fluid.

Glutamine — is structurally akin to glutamic acid.  It’s the most abundant amino found in muscles, which it helps to build and maintain, where it is useful for those confined to bed for long periods.  It helps to maintain acid-alkaline balance, and might be able to reduce cravings for sugar and alcohol.

Glycine — participates in the biosynthesis of hemoglobin, improves glycogen storage, and is part of the purine component of genetic material.

Ornithine — could be classed with “other” amino acids, helps to release growth hormones, which promotes the metabolism of excess body fat.  It detoxifies ammonia and may help insulin to function as an anabolic agent.  It’s formed from arginine.

Proline — improves skin texture via formation and salvation of collagen.  It works with vitamin C to promote healthy connective tissues.

Serine — is needed for the metabolism of fats and fatty acids, and for participation in the biosynthesis of genetic compounds important to RNA and DNA.

Taurine — is also among the “others.”  It boosts the heart muscle and vision, where it helps to deal with macular degeneration.  Taurine is a key component of bile, and may prevent cardiac arrhythmia.

Tyrosine — is important to overall metabolism, and is a precursor to norepinephrine and dopamine, which regulate mood.  It may suppress appetite and helps to reduce body fat.  Tyrosine affects thyroid hormones.

In a weight management study described in the January, 2012, issue of Nutrition and Metabolism, researchers were able to determine a relationship between the amount of quality protein ingested and central abdominal fat.  They especially paid attention to the number of times that approximately ten grams of essential amino acids (EAA) were consumed in a meal.  Noting that the dietary reference intake (DRI) has no specific recommendations for the types of dietary protein consumed or the distribution of protein throughout the day (Layman, 2009) (Drewnowski, 2001), these scientists drew their conclusion based on maximal stimulation of muscle protein synthesis, thereby arriving at the ~10 gram level, adding that greater amounts do not improve the outcome. (Loenneke, 2012)

Calculating the amount of essential amino acids (EAA) in a meal requires more labor than many of us are able or willing to perform, mostly because we lack the immediate resources needed to find out the base levels of each food in the meal.  There are books and websites that can help with this venture if you are so inclined.  However, eating a quality protein at each meal should do the job.  That usually includes meat, fish, eggs, and dairy, which are complete proteins, meaning that they have all the essential amino acids.   (Egg whites are excellent protein foods.)  Because grains and nuts lack lysine, and legumes lack methionine, it’s a good idea to combine them, as in rice and beans.  Combining essential aminos is not necessary at every meal, but it is in the course of the day.

Whey protein has been shown to stimulate a considerable rise in muscle protein synthesis and results in greater muscle cross-sectional area, especially if combined with a little resistance training—and it enhances recovery after exercise.  (Hulmi, 2010)  Older people show a decreased anabolic sensitivity to essential amino acids, probably because of declining intramuscular expression and receptor activation that are associated with slower anabolic signaling.  (Cuthbertson, 2005)   Among the countermeasures under investigation is regular resistance exercise, regardless of intensity or duration.  In physiological studies at the U. of TX, it was found that the only difference between young and old is the rapidity of the positive response to EAA’s.  (Drummond, 2008)  Timing of EAA ingestion for exercisers makes a difference.  Consume them afterwards.

Stimulating muscle protein synthesis is important to body composition.  If you multiply your body weight in kilograms (2.2 pounds) by 0.8, you’ll arrive at the number of grams of protein you need every day.  (You could also multiply pounds by 0.37.  Why didn’t we say that in the first place?)  More than 30 grams of protein in a single meal does not enhance protein synthesis.  This translates that 113 grams (about 4 oz.) of beef is enough, at 220 calories and 30 grams of protein.  (Symons, 2009)  Therefore, that 12-ounce steak from your favorite eatery isn’t doing much more than filling you up.  While you’re at that restaurant, skip the simple carbs if you’re looking to lose a few inches.  There’s a positive association between girth and consumption of potatoes, refined grains (including alcohol) and simple sugars, but a negative association with protein.  (Halkjaer, 2006)

Protein intake has added benefit—satiety.  If you feel full longer, you’ll eat less and, therefore, consume fewer calories.  Protein increases satiety to a greater degree than fats or carbohydrates (although fats beat carbs), and higher-protein diets result in thermogenesis, which augments energy expenditure.  And, if you have high triglycerides (from eating too many refined and starchy carbohydrates), complete protein is able to attenuate that while you change body composition to something more desirable.  (Clifton, 2009)  (Clifton, 2008)  Don’t forget to choose lean protein, to remove visible fat from your steaks and the skin from poultry, and to add legumes to your regimen.

Clifton PM, Keogh JB, Noakes M. Long-term effects of a high-protein weight-loss diet. Am J Clin Nutr. 2008 Jan;87(1):23-9.

Clifton PM, Bastiaans K, Keogh JB. High protein diets decrease total and abdominal fat and improve CVD risk profile in overweight and obese men and women with elevated triacylglycerol. Nutr Metab Cardiovasc Dis. 2009 Oct;19(8):548-54.

Cuthbertson D, Smith K, Babraj J, Leese G, Waddell T, Atherton P, Wackerhage H, Taylor PM, Rennie MJ. Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle. FASEB J. 2005 Mar;19(3):422-4.

Drewnowski A, Warren-Mears VA. Does aging change nutrition requirements? J Nutr Health Aging. 2001;5(2):70-4.

Drummond MJ, Dreyer HC, Pennings B, Fry CS, Dhanani S, Dillon EL, Sheffield-Moore M, Volpi E, Rasmussen BB. Skeletal muscle protein anabolic response to resistance exercise and essential amino acids is delayed with aging. J Appl Physiol. 2008 May;104(5):1452-61.

Fujita S, Dreyer HC, Drummond MJ, Glynn EL, Volpi E, Rasmussen BB. Essential amino acid and carbohydrate ingestion before resistance exercise does not enhance postexercise muscle protein synthesis. J Appl Physiol. 2009 May;106(5):1730-9.

Halkjaer J, Tjønneland A, Thomsen BL, Overvad K, Sørensen TI. Intake of macronutrients as predictors of 5-y changes in waist circumference. Am J Clin Nutr. 2006 Oct;84(4):789-97.

Hulmi JJ, Lockwood CM, Stout JR. Effect of protein/essential amino acids and resistance training on skeletal muscle hypertrophy: A case for whey protein. Nutr Metab (Lond). 2010 Jun 17;7:51.

Layman DK. Dietary Guidelines should reflect new understandings about adult protein needs. Nutr Metab (Lond). 2009 Mar 13;6:12.

Loenneke JP, Balapur A, Thrower AD, Syler G, Timlin M, Pujol TJ. Short report: Relationship between quality protein, lean mass and bone health. Ann Nutr Metab. 2010;57(3-4):219-20.

Loenneke JP, Wilson JM, Manninen AH, Wray ME, Barnes JT and Pujol TJ Quality protein intake is inversely associated with abdominal fat Nutrition and Metabolism. Jan, 2012; 9:5

Paddon-Jones D, Westman E, Mattes RD, Wolfe RR, Astrup A, Westerterp-Plantenga M. Protein, weight management, and satiety. Am J Clin Nutr. 2008 May;87(5):1558S-1561S.

Sites CK, Cooper BC, Toth MJ, Gastaldelli A, Arabshahi A, Barnes S. Effect of a daily supplement of soy protein on body composition and insulin secretion in postmenopausal women. Fertil Steril. 2007 Dec;88(6):1609-17.

Symons TB, Sheffield-Moore M, Wolfe RR, Paddon-Jones D. A moderate serving of high-quality protein maximally stimulates skeletal muscle protein synthesis in young and elderly subjects. J Am Diet Assoc. 2009 Sep;109(9):1582-6.

Tipton KD, Gurkin BE, Matin S, Wolfe RR. Nonessential amino acids are not necessary to stimulate net muscle protein synthesis in healthy volunteers. J Nutr Biochem. 1999 Feb;10(2):89-95.