When you were a kid, did your mom use to dump a pile of spinach on your plate and expect you to eat it? Can you remember the foul smell and how gross the spinach looked and tasted? Were you always reminded, “If you want to be strong like Popeye, then eat your spinach!”
My Grandfather would eat spinach quite a bit and I can still smell that pungent odor and see in my mind that unpleasant bowl of glop sitting on the kitchen table!
And, yes, it is true, I was a big Popeye fan and I even have a cool Popeye t-shirt to this day that my little girl thinks is pretty cool! But I digress. Come to find out, Popeye did teach me a thing or two.
Remember when Popeye ate the spinach and he got stronger? Ever wonder why? 
Research published in Cell Metabolism shows just how powerful spinach is. Even though the exact mechanism is not clear, they found increasing your intake of spinach can make the body more efficient. The research found by eating spinach or other vegetables, which have higher levels of inorganic nitrates, can lead to the mitochondria working better. Result: lower oxygen demand during cardiovascular work! Impressive! There is more!
The most power-packed vegetable on the market today, spinach is a pile of nutrition. Spinach provides you with plenty of fiber, and is chock full of antioxidants, vitamins, and minerals helping the body function optimally.
Research is now coming out on how beneficial spinach can be, and the exact role it plays in our health.
When I am really hungry, the last thing on my mind is spinach. But research shows, incorporating spinach in combination with complex carbs and lean proteins helps you feel fuller longer due to the fiber found in spinach. The fiber has been linked to reducing blood sugar levels immediately following a meal – great news if you want to lose weight!
Spinach not only helps control appetite by improving the feeling of satisfaction, it can reduce blood pressure.
Spinach has inorganic nitrates. Once spinach enters our mouths, saliva starts to break down the spinach into a usable form of energy. After leaving the mouth, it enters the stomach where the acid and enzymes break down the nitrates into nitrite or nitric oxide.
What do nitrites and nitric oxide have to do with health?
The nitrite, or the nitric oxide, has been shown to reduce blood pressure by opening up the veins and arteries which might be constricted or narrowed. Nitric oxide acts is a vasodilator which can help lower blood pressure. How quickly? The inorganic nitrates start working in as little as 3-4 hours after you eat it! Some people think inorganic nitrates are bad for you. However, the inorganic nitrates found in spinach have more benefits than not eating it at all.
Spinach is one of the foods highest in inorganic nitrates. Spinach also has plenty of fiber, high levels of vitamins A and K, and plenty of Folate.
Spinach is also low in calories and high in nutrition.
So, if you are mixing up a nice salad, putting together a yummy sandwich, or whipping up a delicious smoothy (yes you can put spinach in your smoothies and I promise you you won’t notice any change in taste or texture), throw in some spinach leaves and reap the rewards!
Chuck Walker MA, LAT, ATC
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We are all looking for ways to add more muscle. Muscle is a very metabolically active tissue, and just like a big V-8 engine, it burns lots of fuel. More muscle creates a bigger metabolic demand even at rest! Sweet! Burn more calories while just hanging out? Sign me up!
The main method your body uses to take amino acids from the protein you eat to create bigger muscles is called muscle protein synthesis (MPS if you are a geek like me). The more we can ramp up muscle protein synthesis in your body, the more muscle you can build.
Sounds pretty easy so far, right? Unfortunately there is a catch….(and a solution).
The 2 Main Ways:
The two big triggers for increased protein synthesis (and more metabolically hungry muscle) for people of all ages are 1) weight training and 2) eating protein (2, 4, 6).
Many articles have been written about all the various ways to pick stuff up and put it down (which is very important), so we will focus on the second method of eating dietary protein.
Protein, when ingested, serves 2 main purposes: 1) raw building blocks for muscle and 2) turning on muscle protein synthesis (7, 9, 11). We need to optimize both processes for the maximal amount of muscle.
As long as you are eating some complete proteins like meats, dairy, eggs and even protein supplements with whey, you have all the raw materials covered.
Maximal Muscle Ahead!
To stimulate more muscle, we need to flip the switch to kick start the whole building process of assembling amino acids into muscle protein. Did you watch much TV as a kid? I know I did (ok, probably a bit too much). One show that sticks in my head was the Laverne and Shirley show. Yeah, I know, I know, I am dating myself now, but in the beginning of each episode, Laverne and Shirley are working at an assembly line.
Imagine that each item coming down the line is an amino acid on its way to becoming muscle tissue. If the assembly line grinds to a halt, no more muscle is going to be made.
Ideally, we want the assembly line running as often as possible creating more muscle. Remember that your body is constantly building up and tearing down muscle tissue. This turnover of proteins can be up to 25% of resting energy expenditure (12). Just like a big car burns lots of fuel, it takes lots of energy to keep this repair process going.
Eat Multiple Times Per Day?I am sure you have heard the advice that you need to eat protein multiple times during the day to keep protein synthesis (the building up process) chugging along.
While this is true……there is a catch.
In an experiment conducted by Bohe et al. (3) they used an IV infusion of protein to keep levels very high for many hours. The common assumption is that protein synthesis would also stay elevated too.
But physiology is not always that logical. After about 3-4 hours, DESPITE elevated blood levels of amino acids, muscle protein synthesis DROPPED.
Uh oh.
The protein building process has been halted! Someone pulled the plug on the assembly line, even though we had plenty of raw material present! In humans it has been shown that after eating a protein meal, protein synthesis will stay elevated for about 2 hours and then drops off (1, 10).
Prolonged Protein Synthesis:We now know that elevating amino acids in the blood all the time is not enough to keep adding more muscle. Perhaps there is a way to keep the assembly line marching along longer?
BCAAs to the rescue!
In a new study conducted by Wilson, GJ et al. (13) in our fury tailed friends, they tested an intervention of leucine (an amino acid), carbohydrates, and a combination of leucine and carbohydrates after a standard protein meal in regards to protein synthesis.
In the study (13), the rats were trained to eat 3 times per day. Then on test day did not consume any food for 12 hours (fasted) while blood was checked at 0, 90, or 180 minutes after a standard meal.
At 135 minutes after the meal, the rats got one of 4 items 1) carbohydrates only, 2) the amino acid leucine only or 3) combination of leucine and carbohydrates or or 4) water (served as a control group).
The goal was to extend the time protein synthesis stayed active beyond the standard 2 hour period.
Did It Work?
The researchers found that the critters given leucine, carbohydrates, or the combination of both did see an extension of muscle protein synthesis.
Awesome!
The assembly line process on the way to more muscle did not come to halt at the usual two-hour mark, but continued on!
All three interventions (leucine, carbs, or leucine + carbs) did the trick, which begs the follow-up question; which one is the best?
In the same study (13), they also measured insulin. Remember that insulin can be thought of as a “fuel selector switch” where high levels of insulin shift the body away from burning fat and towards using carbohydrates. While this is great before an intense weight training session, it is not a good thing to keep insulin levels jacked sky high all day as it impedes burning fat (5)!
The intervention of the carbohydrate only or in combination with leucine showed elevated levels of insulin. However, this was not seen in the leucine only group as insulin was not elevated.
Therefore, taking leucine only (without carbs) about 2 hours after a meal keeps the muscle building assembly going, but allows insulin levels to go back down and not imped the fat burning process in the body!
A two for one!
Leucine Is The Winner, Right?
Good thought, but not quite so fast. While taking leucine only works, as shown by the experiment above, it also depletes other important amino acids at the same time.. In the present study (13), isoleucine and valine were reduced by about 50-150% when taking leucine. Leucine, isoleucine, and valine are commonly known as branched chain amino acids or BCAAs. Since taking leucine alone depletes the other 2, taking BCAAS may be better than leucine alone.
While an exact human dosage has not been determined, about 5-10 grams of BCAAs 2 hours after a protein-containing meal is a great place to start.
Summary:
Today, you learned an advanced tip to keep the muscle building process continuing on even longer for more muscle and an increased metabolic rate.
Just like a big car takes lots of gas even when it idles, more muscle not only looks better but also takes more energy to keep it humming along.
Protein serves two main purposes 1) raw material for muscle 2) to kick start the protein building process. To optimize both processes, include about 20-40 grams of protein at each meal and add approximately 5-10 grams of BCAAs about 2 hours post meal to keep the protein synthesis process continuing beyond the typically drop off point at 2 hours (8, 13).
Keep in mind that its not entirely necessary to take this extra step of adding BCAAs 2 hours after a meal in order to lose weight or see results from your resistance training. However, it might be that extra lift you need to reach your ultimate goals (this clearly depends on what your goals happen to be). Just make sure you aren’t greatly increasing fat intake and exceeding caloric needs in order to get those BCAAs into your diet. That would definitely be counter-productive to you.
Want a little bit more info on BCAAs and foods that contain them? You’re in luck! Today I also posted information on this blog that gives you some ideas of what foods contain good sources of BCAAs. You should see that information just below this post.
Malinda Walker M. Ed., ATC
Imagine Fitness
Prairie du Sac, WI 53578
References
1. Atherton PJ, T Etheridge, PW Watt, et al. Muscle full effect after oral protein: time-dependent concordance and discordance between human muscle protein synthesis and mTORC1 signaling. Am J Clin Nutr. 2010.
2. Beelen M, R Koopman, AP Gijsen, et al. Protein coingestion stimulates muscle protein synthesis during resistance-type exercise. Am J Physiol Endocrinol Metab. 2008; 295(1):E70-7.
3. Bohe J, JF Low, RR Wolfe, MJ Rennie. Latency and duration of stimulation of human muscle protein synthesis during continuous infusion of amino acids. J Physiol. 2001; 532(Pt 2):575-9.
4. Drummond MJ, HC Dreyer, CS Fry, EL Glynn, BB Rasmussen. Nutritional and contractile regulation of human skeletal muscle protein synthesis and mTORC1 signaling. J Appl Physiol. 2009; 106(4):1374-84.
5. Kelley DE. Skeletal muscle fat oxidation: timing and flexibility are everything. J Clin Invest. 2005; 115(7):1699-702.
6. Mayhew DL, JS Kim, JM Cross, AA Ferrando, MM Bamman. Translational Signaling Responses Preceding Resistance Training-Mediated Myofiber Hypertrophy in Young and Old Humans. J Appl Physiol. 2009.
7. Miyazaki M, KA Esser. Cellular mechanisms regulating protein synthesis and skeletal muscle hypertrophy in animals. J Appl Physiol. 2009; 106(4):1367-73.
8. Moore DR, MJ Robinson, JL Fry, et al. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men. Am J Clin Nutr. 2009; 89(1):161-8.
9. Murgas Torrazza R, A Suryawan, MC Gazzaneo, et al. Leucine Supplementation of a Low-Protein Meal Increases Skeletal Muscle and Visceral Tissue Protein Synthesis in Neonatal Pigs by Stimulating mTOR-Dependent Translation Initiation. J Nutr. 2010; 140(12):2145-52.
10. Norton LE, DK Layman, P Bunpo, TG Anthony, DV Brana, PJ Garlick. The leucine content of a complete meal directs peak activation but not duration of skeletal muscle protein synthesis and mammalian target of rapamycin signaling in rats. J Nutr. 2009; 139(6):1103-9.
11. Suryawan A, RA Orellana, ML Fiorotto, TA Davis. Leucine acts as a nutrient signal to stimulate protein synthesis in neonatal pigs. J Anim Sci. 2010.
12. Welle S, KS Nair. Relationship of resting metabolic rate to body composition and protein turnover. Am J Physiol. 1990; 258(6 Pt 1):E990-8.
13. Wilson GJ, DK Layman, CJ Moulton, et al. Leucine or carbohydrate supplementation reduces AMPK and eEF2 phosphorylation and extends postprandial muscle protein synthesis in rats. Am J Physiol Endocrinol Metab. 2011.
Posted in Boot Camp by .
Oct 11
3
Foods Containing BCAAs
After posting the article, Melt More Fat Sitting At Your Desk, I wanted to post a little bit of information on where you can find Branched Chain Amino Acids (BCAAs). Here you go!
Foods containing BCAAs:
Meats
Red meat is highest in BCAAs. Other meats are also high in BCAAs because they are primarily protein; all sources of protein contain BCAAs. Choose lean cuts of meat to avoid the saturated fats that can increase your risk for developing heart disease, advises the MayoClinic.com.
Poultry is another source of BCAAs and a popular option for beef. Choose breast meat without the skin for a low-fat protein source of BCAAs. It is also a heart healthy choice, according to the American Heart Association. (Reference 6) Eggs are packed with nutrition and BCAAs. They are also low calorie and easy to incorporate into your daily diet. Eggs can be added to shakes, hard-boiled for a snack or just scrambled for a quick bite.
Dairy
Dairy products also are good protein sources and contain high amounts of BCAAs. Some healthy choices in dairy include low-fat or nonfat milk, low-fat cottage cheese, low-fat yogurt, frozen yogurt, sour cream and low-fat cheeses. MayoClinic.com recommends reducing the amount of saturated fats in your diet.
Additional dairy options include butter, cheese, cream, crème fraiche, eggnog, ghee and half-and-half. Some dairy products, such as ice cream, contain whey protein, which is loaded with BCAAs.
Liquid & Powder Protein
Many bodybuilders use liquid protein drinks as sources of BCAAs before, during or after workouts. One advantage to protein powders and drinks is that you can mix your shake to have any amount of BCAAs. Milk added to protein powder shakes boosts the amount of BCAAs in the shake.
Whey protein shakes are popular because they are easily digested. Whey is separated from milk in the process of making cheese.
Soy protein is a complete protein and a source of BCAAs. It is not as high in BCAAs as whey protein, but it is a good option for people who are lactose intolerant or vegetarian; soy protein comes from soybeans and not from animals. Drinking soy protein can also help lower cholesterol, according to John Erdmand, University of Illinois professor of nutrition, in a 2000 advisory to the American Hearth Association.
Chuck Walker MA, LAT, ATC
Imagine Fitness
Prairie du Sac, WI
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