Btw, here is the article on Anator-p70 - just in case you dont have a copy of the latest MD:
Muscular Development, April 2006
(
http://www.musculardevelopment.com/new/thismonth.html)
Sports Supplement Products Review
By Anssi Manninen, MHS
MuscleTech Anator-P70
Advanced Muscle Gene Activator
“If an elderly, but distinguished scientist says that something is possible, he is almost
certainly right; but if he says that it is impossible, he is very probably wrong.” —Arthur C. Clarke
MuscleTech is dedicated to developing the most effective dietary supplements in the
world. To date, they have funded over 80 research studies, including recent research trials at
Baylor University, the University of Nottingham, the University of Laval, St. Francis Xavier
University, McMaster University and the University of Toronto. Clearly, MuscleTech is committed
to innovation and they have developed some highly effective supplements for building muscle
and losing fat.
Their latest product is called Anator-P70. According to MuscleTech, Dr. Paul Greenhaff of the University of Nottingham has recently completed a research study on Anator-P70 with excellent results. We’ll
provide you with the details as soon as this study has been published. The active ingredients in
Anator-P70 are whey protein hydrolysate, leucine, phenylalanine, creatine monohydrate and
high-glycemic carbohydrates.
Whey Protein Hydrolysate: The Ultimate Source of Protein
Whey proteins particularly have been singled out as the ultimate source of protein based
on an excellent amino acid profile and rapidity of digestion. A recent scientific review by Drs. Hu
and Zemel, published in the Journal of Nutritional Biochemistry, concluded that whey protein
supplementation could enhance lean body mass in conjunction with appropriate training. The
investigators also pointed out that certain bioactive compounds from whey might improve immune
function and gastrointestinal health.
Protein can be hydrolyzed (pre-digested), producing small chains of amino acids called
peptides. This process mimics our own digestive actions thus making it an ideal way to process
protein. Studies indicate that protein hydrolysates containing mostly di- and tri-peptides are
absorbed more rapidly than free form amino acids and much more rapidly than intact (nonhydrolyzed)
proteins. Obviously, this is a desirable trait for serious athletes who wish to maximize
amino acid delivery to the muscle immediately after exercise. It’s the kinetics of the absorption
(rather than the net absorption of amino acids) that determines the greater nutritional value of the
protein hydrolysates.
The purpose of the recent study at the Copenhagen Muscle Research Center was to
determine the effects different protein-containing meals (protein hydrolysates versus intact
proteins) have on the magnitude and direction of insulin and glucagon responses. A further aim
was to determine the rate of appearance of amino acids. This study indicated that:
· Ingestion of glucose and protein hydrolysate results in a synergistic and fast
increase in blood insulin.
· Protein hydrolysates are absorbed at a faster rate from the small intestine than
are intact milk proteins.
· Whey protein hydrolysate elicited the greatest availability of amino acids during
the three-hour postprandial (occurring after a meal) period.
The authors suggested that the association of high levels of blood amino acids and
insulin might explain a superiority of protein hydrolysates over intact proteins in promoting better
nitrogen utilization (i.e., greater anabolism), especially when administered in combination with
glucose.
Protein Hydrolysate+Leucine+Phenylalanine=Strong Insulin Response
In a recent, well-controlled study by Dr. van Loon and colleagues, a total of 10 drinks
were tested in eight non-obese males after an overnight fast to investigate the insulinotropic
(stimulating the production of insulin) potential of several free amino acids, protein hydrolysates
and an intact protein. At zero, 30, 60 and 90 minutes, the subjects received a beverage 3.5 mL/kg
to ensure a given dose of 0.8 g/kg carbohydrate (50 percent as glucose and 50 percent as
maltodextrin) and 0.4 g/kg of an amino acid and protein hydrolysate mixture every hour. The
results of this study indicate that oral ingestion of some amino acid mixtures in combination with
carbohydrates can produce strong insulinotropic effects.
To compare the insulinotropic effect of the ingestion of the protein hydrolysates with that
of an intact protein, sodium-caseinate was provided in one of the drinks. This resulted in an
insulin response not significantly different from that found with the control trial (30 percent
greater) and tended to be less than the responses observed after ingestion of the protein
hydrolysates. After ingestion of the intact protein, blood amino acid responses over this two-hour
period were in general lower than the responses observed after ingestion of the protein
hydrolysates.
Furthermore, regression analysis of the insulin responses and the changes in the blood
amino acid concentrations over the two-hour period showed a strong positive correlation between
the observed insulin response and changes in blood leucine, phenylalanine and tyrosine
concentrations. Interestingly, the addition of free glutamine hardly influenced blood glutamine
levels. Also, this study clearly shows that oral ingestion of free arginine isn’t an effective means of
increasing plasma insulin concentrations and blood arginine concentrations. The authors
concluded that oral intake of protein hydrolysates and amino acids in combination with
carbohydrates can result in an insulinotropic effect as much as 100 percent greater than with the
intake of carbohydrates only.
In another excellent study by Dr. van Loon and co-workers, after an overnight fast, eight
male cyclists visited a laboratory on five occasions, during which a control and two different
beverage compositions in two different doses were tested. After they performed a glycogendepletion
exercise, subjects received a beverage (3.5 mL/kg) every 30 minutes ensuring an
intake of 1.2 g/kg/h carbohydrate and zero, 0.2 or 0.4 g/kg/h protein hydrolysate and amino acid
mixture.
After the insulin response was expressed as the area under curve, only the ingestion of
the beverages containing protein hydrolysate, leucine and phenylalanine resulted in a marked
increase in insulin response compared with the carbohydrate-only trial. Further, a dose-related
effect existed because doubling the dose (0.2-0.4 g/kg/h) led to an additional rise in insulin
response. Blood leucine, phenylalanine and tyrosine concentrations showed strong correlations
with the insulin response.
In addition, blood amino acid concentrations were generally lower after the ingestion of
drinks containing protein hydrolysate+phenylalanine+leucine compared with the control drinks,
although in the latter, a considerable amount of protein and amino acids were ingested. This
strongly suggests that tissue amino acid uptake and post-exercise muscle protein anabolism
were increased after the ingestion of the protein hydrolysate-amino acid mixture.
Leucine: A Superstar of Amino Acids
The role of amino acids as substrates for protein synthesis (i.e., building blocks of
protein) is well established. However, a function for amino acids in modulating the signal
pathways that regulate muscle protein synthesis has only recently been described. The
stimulation of protein synthesis in skeletal muscle produced by an intake of a mixed meal is due
largely to branched-chain amino acids (leucine, isoleucine, valine; BCAAs). Of the three BCAAs,
leucine is clearly the most effective. In fact, a recent study at Baylor College of Medicine suggests
that the postprandial (occurring after meal) rise in leucine, but not isoleucine or valine, acts as a
nutrient signal to stimulate muscle protein synthesis.
Dr. Crowe and co-workers investigated the effects of leucine supplementation on the
exercise performance of outrigger canoeists. Thirteen canoeists underwent testing before and
after six weeks of supplementation with either leucine (45 mg/kg/day) or placebo. The conclusion
was that “leucine supplementation significantly improved endurance performance and upper body
power in outrigger canoeists.”
Finally, it was recently proposed that leucine is a key to the metabolic advantage of a
higher protein diet because of its unique role in the regulation of muscle protein synthesis, insulin
signaling and glucose re-cycling via alanine. Leucine appears to regulate the burning of glucose
by skeletal muscle through stimulation of glucose recycling via the glucose-alanine cycle. These
mechanisms produce muscle mass sparing and provide a stable blood sugar environment with
low insulin responses during energy-restricted diets.
Bottom Line
In order to make the very best use of the hypermetabolism that exists after strenuous
exercise, I highly recommend you ingest a serving of MuscleTech Anator-P70 immediately after
exercise. It should maximize protein anabolism and minimize catabolism.
The author of this article has no financial relationship with MuscleTech.
References:
1. Ha E., Zemel M.B. (2003) Functional properties of whey, whey components and
essential amino acids: mechanisms underlying health benefits for active people
(review). Journal of Nutritional Biochemistry, 14:251-8.
2. Di Pasquale, M.G. (1997) Amino Acids and Proteins for the Athlete. Boca Raton, FL:
CRC Press.
3. Bucci, L.R., Unlu, L. (2000) Protein and amino acid supplements in exercise and
sport. In: Energy-Yielding Macronutrients and Energy Metabolism in Sports Nutrition,
Eds. Wolinsky, I., Driskell, J.A. Boca Raton, FL: CRC Press, pp. 191-212.
4. Manninen A.H. (2004) Protein hydrolysates in sports and exercise: A brief review.
Journal of Sports Science and Medicine, 3:60-63.
5. van Loon, L.J., Saris, W.H.M., Verhagen, H., Wagenmakers, A.J. (2000) Plasma
insulin responses after ingestion of different amino acid or protein mixtures with
carbohydrate. American Journal of Clinical Nutrition, 72:96-105.
6. van Loon, L.J., Kruijshoop, M., Verhagen H. et al. (2000) Ingestion of protein
hydrolysate and amino acid-carbohydrate mixtures increases postexercise plasma
insulin responses in men. Journal of Nutrition, 130:2508-2513.
7. Calbet, J.A.L., MacLean, D.A. (2002) Plasma glucagons and insulin responses
depend on the rate of appearance of amino acids after ingestion of different protein
solutions in humans. Journal of Nutrition, 132:2174-2182.
8. Kimball, S.R., Jefferson, S.L. (2004) Amino acids as regulators of gene expression.
Nutrition & Metabolism, 1:3.
9. Kimball, S.R., Jefferson, S.L. (2006) Signaling pathways and molecular mechanisms
through which branched-chain amino acids mediate translational control of protein
synthesis. Journal of Nutrition, 136:227S-31S.
10. Escobar J., Frank, JW, Suryawan, A. et al. (2005) Regulation of cardiac and skeletal
muscle protein synthesis by individual branched-chain amino acids in neonatal pigs.
American Journal of Physiology: Endocrinology & Metabolism, Nov 8; [Epub ahead of
print].
11. Crowe M.J., Weatherson, J.N., Bowden, P.N. (2005) Effects of dietary leucine
supplementation on exercise performance. European Journal of Applied Physiology,
Oct 29; [Epub ahead of print].
12. Layman, D.K., Walker, D.A. (2006) Potential importance of leucine in treatment of
obesity and the metabolic syndrome. Journal of Nutrition, 136:319S-23S.
