Protein - More Is Not Always Better?

[kong]

I will continue.

Now, about the essential amino acids. There are a total of 23 amino acids, 15 our body makes, and eight we have to take from food; as far as I know, if insted of makeing meat your center meal you make beans and rice-preferably brown- your center meal you will have no problems. About fat, I don't worry I just eat avacado and some nuts so I think i'm okay.

I have said this more than once: here in the united states you have to be very carfull with what you eat because most of it is processed or something else has happened to it.

A good book I would recomend people to read is: Engine2 diet. I have only read a little myself, but it explanes sickness really good. The author seems to be a firefighter from texas and he tells the goods about eating vegetables.

btw it is a little dangerous to eat too many eggs because of the colestherol, is that why you mentioned red wine, I heard if you drink a little wine it helps lower colestherol.
Ther's a lot of controversy about weder eggs are healthy or not. In my oppinion I don't think eating eggs is very healthy, but if someone enjois them then they can still have them once in a while.

When I was hungry, I used to eat even eight eggs;nevertheless, if afood is not very healthy you should at the very least lower your consuption of the product.

I don't know exacly why, but people who have exess body fat seem to have more muscle even without working out than a thin person. This makes me think that to get bigger you need to consume a good amount of fat in order to get big muscles. Sumo wrestles are huge including their muscles; I don't know their diet but if you find what makes them grow so much you might find a way to get big muscles and then get ripped with the American style of burning fat so that all that you can see is muscle.

just out of couriosity, are you a bodybuilder fits?

[Al]

Read

[samurai69]

The amount of saturated fat in our diet exerts an effect on blood cholesterol that is several times greater than the relatively small amounts of dietary cholesterol.

i always thought that!!


.

[Scott]

Read

about time a study like this was done.

[Cookie]

By Jerry Brainum

Until recently, no one had bothered to test the notion that 30 grams of protein or less is about all the body can handle after weight training. A new study tackled that issue in particular. Six healthy young men, average age 22, on five separate occasions reported to a lab, where they did intense leg exercise. After trainin, the men received drinks containing zero, five, 10, 20 or 40 grams of whole-egg powder. The researchers measured protein synthesis and oxidation over a four-hour period after the training ended by tracing tagged leucine.

They also monitored factors involved in muscle protein synthesis that are affected by amino acid intake, particularly the branched-chain amino acids, such as leucine. The factors become activated when phosphate groups are attached to them; however, in this study they weren't affected by any amount of protein intake. The authors suggest that the exercise itself may have maximally stimulated the factors, which would obscure the effect produced by amino acids.

The study did find that both muscle protein and serum albumin synthesis were maximally stimulated with protein intakes of under 20 grams at one sitting. Eating more than 20 grams of protein at a time results in increased protein oxidation with no further increase in muscle protein synthesis. The 20 grams contain 8.6 grams of essential amino acides, which is about the same amount that has proved effective in boosting muscle protein synthesis following weight training. Maximal protein synthesis at rest requires only 10 grams of protein per meal.

[Cookie]

What’s better:?Whey protein or free-form aminos?

by Jeff S. Volek, Ph.D., R.D., F.A.C.N.
Protein researchers have known for years that only the essential amino acids (the ones our body cannot make) are needed to boost protein synthesis. This is one reason why whey protein is so effective because it has a high ratio of essential amino acids compared to other protein sources.

Prominent protein researchers decided to do a clever experiment. They compared three trials. One provided 15g of intact whey protein (regular whey protein powder). The other 2 trials provided either the individual essential amino acids (7g) or the individual non-essential amino acids (8g) found in whey. Protein balance was measured for 3.5 hours after ingestion.

They predicted that providing just the free-form essential amino acids typically found in whey would result in the same increase in protein synthesis as the whey protein powder. Yet, here’s what they found: The non-essential amino acid trial resulted in essentially no change in protein balance, whereas the essential amino acid trial resulted in a small increase. After the whey protein powder ingestion, protein balance was markedly increased.

The findings were somewhat surprising because it indicates that the essential amino acid content of whey is not solely responsible for the anabolic effects. The results have implications for formulation of protein supplements and suggest that intact whey protein powder has some benefits beyond what can be achieved by only providing its essential amino acids.


References: Katsanos CS, Chinkes DL, Paddon-Jones D, Zhang XJ, Aarsland A, Wolfe RR. Whey protein ingestion in elderly persons results in greater muscle protein accrual than ingestion of its constituent essential amino acid content. Nutr Res. 2008 Oct;28(10):651-8.

[Cookie]

Recent research into the nutritional requirements of athletes engaged in intense training have highlighted the importance of taking essential amino acids in increasing muscle protein synthesis. Of the eight amino acids considered to be essential, the branched-chain aminos-leucine, isoleucine and valine-are of considerable anabolic importance. In fact, some studies show that leucine can turn on various mechanisms in the body that lead to upgraded muscle protein synthesis. Despite that, BCAA supplements remain controversial. Some studies have found a definite anabolic response in those taking BCAAs, while others have found little or nothing.

The latest study on the matter featured 10 healthy college-aged men. In a double-blind design, subjects were given either a BCAA supplement or a placebo for three weeks, followed by a week of weight training-four workouts-with continued supplementation. Blood tests were done before and after three weeks of BCAA use, and also after two and four days of training, with the final test done 36 hours after the final training session.

Those in the BCAA group showed significantly higher testosterone counts, along with lower counts of cortisol and creatine kinase, an enzyme that, when elevated, points to amplified muscle damage. That indicates a definite anabolic effect, along with an anticatabolic effect, as reflected in the drops in cortisol and creatine kinase.

The researchers concluded that "use of a post exercise supplementation product high in BCAAs would be useful for a trained individual wishing to increase strength and lean muscle mass, as well as enhance recovery time between workouts."

Jerry Brainum

Sharp, C.P.M., et al. (2008). Amino acids and recovery from high-intensity resistance training: The role of commercially available branched-chain amino acid supplementation. J Str Cond Res. 22:114.

[Cookie]

By Robbie Durand, MA

Leucine has the unique ability to stimulate muscle protein synthesis independent of insulin. The anabolic actions of leucine are though signaling pathways via mammalian target of rapamycin (mTOR). The mTOR pathway facilitates cell growth. Scientists have discovered that this is the single most important amino acid for stimulating protein synthesis.

Strength Training Slows the Absorption of Leucine and BCAAs

Many bodybuilders know that consumption of a pre-exercise mixture of BCAAs or leucine before resistance exercise enhances anabolic effects, but new research suggests that strength training can slow the absorption of both BCAA and leucine. Researchers measured peak concentration of three amino acids (BCAA, leucine, and glutamine) during rest and before intense resistance exercise. The subjects took 50mg/kg of bodyweight of leucine (4 grams), BCAA (4 grams of leucine, 1 gram isoleucine, 1 gram valine), or glutamine (4 grams) immediately before performing a standardized resistance training protocol to stimulate muscle hypertrophy. The ingestion of 4 grams of leucine is similar to eating 230 grams of beef. Here are the results:

Peak Concentrations in Blood

Leucine rest: 67 minutes
Leucine before resistance exercise: 90 minutes
(23-minute delay)

BCAA rest: 72 minutes
BCAA before resistance exercise: 78 minutes
(6-minute delay)

Glutamine rest: 60 minutes
Glutamine before resistance exercise: 57 minutes

The researchers speculated that the delay in peak concentrations of leucine and BCAA was due to delayed gastric emptying, which means that blood flow is diverted to exercising muscle and away from the stomach, which slows the digestive process. The researchers were puzzled at why peak appearance of glutamine in the blood was not affected; they speculated that glutamine is metabolized differently and resistance exercise does not slow absorption kinetics. The important take-home point is that taking leucine should probably occur at least 90 minutes before exercise so that when you reach the gym you have peak concentrations of leucine in your blood.
Mero A, Leikas A, Knuutinen J, Hulmi JJ, Kovanen V. Effect of strength-training session on plasma amino acid concentration following oral ingestion of leucine, BCAAs or glutamine in men. Eur J Appl Physiol. 2008 Oct 21.

Leucine May Be The Perfect Supplement Using Low-Carb Diets

Previous research has shown that leucine is a stimulator of insulin, but how much of an impact this would have on fat metabolism remains undetermined. Some bodybuilders have questioned using leucine while dieting. The effect of leucine on protein synthesis is via insulin independent mechanisms, although basal insulin levels are important for maximal effect. How leucine brings about its metabolic effects has not been fully elucidated. Researchers wanted to compare the insulin and glucose responses of leucine (7 grams) or leucine (7 grams) plus glucose (25 grams). The amount of leucine would be equivalent to a 350-gram steak.

The researchers found that leucine by itself resulted in a modest increase in insulin; however, the rise in insulin was small compared to when leucine was ingested with glucose. The combination of leucine and glucose resulted in a greater insulin spike than glucose alone. The insulin response was 72 percent greater with glucose and leucine compared to glucose alone. Leucine administration alone also resulted in a large increase in glucagon concentration but did not result in changes in glucose.

The key point is that for bodybuilders following a low-carb diet, the addition of leucine may be a great way to maintain anabolism in a calorie deficit and maintain a ketogenic state as it does not stimulate glucose, modestly affects insulin response, increases glucagon, and results in large blood concentrations of leucine. Another interesting finding was that leucine tended to produce a greater degree of fullness!

Kalogeropoulou D, Lafave L, Schweim K, Gannon MC, Nuttall FQ. Leucine, when ingested with glucose, synergistically stimulates insulin secretion and lowers blood glucose.
Metabolism. 2008 Dec; 57(12): 1747-52.

Leucine: The Ultimate Anti-Catabolic Supplement

Leucine may be the perfect “competition” supplement as it elicits potent anti-catabolic actions. Leucine is an essential amino acid, which is capable of producing anabolic effects on muscle tissue; moreover, when administered in large dosages it is capable of promoting important anti-catabolic actions as well. Leucine has been shown to attenuate skeletal muscle catabolism during weight loss, facilitate muscle healing and improve skeletal muscle protein turnover in aged individuals. In a recent review article published in the Journal of Nutrition and Metabolism, researchers discussed the potent anti-catabolic actions of leucine in humans.

Summing up, in human studies, leucine supplementation clearly induces an inhibition in skeletal muscle proteolysis (anti-catabolic actions) and there are several studies suggesting that the leucine concentration capable of preventing protein breakdown may be larger than that capable of maximally stimulating protein synthesis, especially under catabolic conditions. Under catabolic conditions, muscle tends to become leucine-resistant; however, leucine prevents muscle tissue breakdown.

Zanchi NE, Nicastro H, Lancha AH Jr.
Potential antiproteolytic effects of L-leucine:
Observations of in vitro and in vivo studies.
Nutr Metab (Lond), 2008 Jul 17;5:20

[Cookie]

Branched-Chain Amino Acids Promote Protein Synthesis After Exercise

The branched-chain amino acids (BCAA) include leucine, isoleucine and valine. They are essential amino acids, which mean they must be consumed in the diet. They make up 33 percent of skeletal muscle and turn over rapidly during exercise. They are also essential for muscle protein synthesis. Many bodybuilders and other athletes take BCAA supplements to promote protein synthesis and recovery from exercise. BCAAs serve as the building blocks of proteins and activate signaling proteins in muscles that turn on protein synthesis and increase muscle fiber size.

Chemicals called ribosomal protein S6 kinase and the target of rapamycin (mTOR) are important cell-signaling molecules for protein synthesis. They are sensitive to BCAAs (particularly leucine) and work like biological computer programs to line up amino acids needed to produce new muscle tissue. Bodybuilders should consume carb/amino acid supplements high in BCAAs, before and after training to maximize protein synthesis.

They activate signaling pathways inside the cells that promote protein synthesis in the muscles and modify muscle protein breakdown, remodeling and repair. While they promote recovery and immune function, BCAA supplements do not seem to increase athletic performance or serve as a significant fuel source during exercise.

J Sports Med Phys Fitness, 48: 347-351, 2008
Am J Physiol Endocrinol Metab, 294: E392-E400, 2008
Am J Physiol Endocrinol Metab, 281: E365-E374, 2001
J.Nutr, 136: 533S-S537, 2006

[kong]

Our body uses protein for a bunch of different things and it is essential for life, yet too much will toxicate you; just as too much oxygen will hurt you by making more free radicals, which is one of the resons we age.

As for the study on the eggs, be carefull. Studys such as that one might be true, or they might be paid by an egg company. I'm not saying the study is wrong; I'm just saying that you must use your logic. For example you have all seen the comercials in tv with doctors or former athletes saying that what they are selling is indeed the best and most efficient way to get in good shape.

Listing one: Abb rocket. In that comercial they have a former football player saying, that machine is the real deal, and they also seem to have a university working for them.

The truth is that they are compering their machine to the crunch and sit-up exercses.
sit-ups and crunches aren't the best exercises to burn belly fat, or to give you functunal abbs.
If you whant to get your abbs in good condition there are a bunch of exercises: The abb weel (which you can also use with a paper or a towel), the plank, hanging fom some place and lifting your legs, leg lifts, hoping to a box, reverse pushup bridge, bear crawl, table maker, crab walk, leg trust (burpies), and even regular pushups work better than that machine.

[kong]

As I was saying, you have to use your logic. So far the only system that I have seen on tv that makes sance would be P90x.

For eating healthy a good rule would be that if something smells really bad you should't eat it. My reason is that if something smells really bad in your kitchen then it will smell bad in your stomich and intestines.

There is a reason why I would vote against meat: If you leave chicken out of the refrigirator for one night it will go bad and in my point of view I am not sure if it is safe in the long run to be eating dead animals;eitherway, if you do eat dead animals you should at the very least chew it very well.

Can you imagine how much food we would have to eat if we were to follow the daily intake recomended.

people that know logic, know that line to be true, and that type of people are the same people that created suplements. I want to make clear that I think that if you are truly healthy you don't need suplements, but if you are of those people that want to eat junk, or microwave food and don't care what kind or in which combinations the food is eaten; then you should deffinetely use supplements.

Too much protein, too much fat, too much carbohydrates, too much anything and you will have to pay for it.

[Al]

Dead animals eh? I see where you're going.