Egg protein

Whilst Anabolic Egg Matrix is a new unique formula which may contribute to muscle growth and recovery it is worth exploring the bases of product egg protein, unlike many proteins this not a by product of other food type production but a natural complete protein source with many co-factors which are potentially very interesting to any one interested in gain lean muscle mass.

Egg protein has always been the gold standard by which all other proteins are measured. Egg protein has a PDCAAS (Protein Digestibility Corrected Amino Acid Score) score of number 1 the highest value possible, it has a Bv (biological value) of 100 and a highly balanced amino acid profile. Meaning your body can not find a protein source with a better conversion rate to muscle! This is critical component in achieving phenomenal muscle growth, not surprising as eggs contain many naturally occurring highly anabolic substrates. When the protein levels and substrates are enhanced to optimise absorption you get a highly anabolic protein.

Egg protein has been a highly prized protein source for millennia from the humble hunter gathers who searched for this prized food through to the many mighty warrior tribes who have all held the egg high as a prized source of power for the human body. Egg protein has only reduced in popularity over the past few decades due to some bad press with regard to the fat content which would appear to be slightly misleading and rise purified milk proteins left over from cheese production.

As recently as the golden era of bodybuilding eggs have been highly valued by such notables a Vince Gironda, Rheo Blair and even old numero uno, Arnie (Quote: milk is for babies!). In fact back in the 70’s Vince Gironda was promoting the value of fertile eggs.

This is an interesting fact as recent research indicates that their are a few highly anabolic elements potentially present in egg protein Arachidonic Acid being one and the presence of follistatin being the other.

As the major percentage of fat in egg yolk is made of good fat when the eggs are from a good source it is very interesting to review recent research into the positive hormonal effects of these essential fatty acids Read more: Arachidonic Acid.

Whilst we are no way claiming to have extracted or increased the next substrate Follistin it is not surprising to find that the naturally occurring with in egg yolk. What is Follistatin? Read more: Follistatin, follistatin has been identified as a natural Myostatin Antagonist (blocker).

Mysotatin is TGF beta protein that inhibits muscle growth! http://en.wikipedia.org/wiki/Myostatin.

Our specific processing of our egg products, as egg protein specialists means you can rest assured that that all products do not experience any thermal degradation which may damage any amino acids, enzymes or substrates. We produce AEM with added co-factors to enhance absorption and optimise the anabolic nature of the product, naturally. Our eggs are from high end flocks and our solids gently filtered and dessicated via cool mist chambers creating what we call a fertile isolate powder. The easily dispersible powder is blended with additional co-factors and flavoured to creating a easily mixable great tasting superior protein source.

See Nutrient Absorption for information on additional added co-factors for increased absorption and Growth Factors for data on added elements for enhanced anabolic activity.

Arachidonic Acid, Inflammation, And Muscle Protein Synthesis

Arachidonic acid's role in muscle inflammation? the concept of the "no pain, no gain" is simple: a training stimulus that does not elicit localised inflammation and soreness will not yield optimal muscle growth.

Arachidonic acid (AA, 20:4n-6) is an essential Omega-6 (1-6) polyunsaturated fatty acid that is abundant in skeletal muscle membrane phospholipids (figure 2). It is also the body's principle building block for the production of prostaglandins, which are known to have various physiological roles including a close involvement in inflammation.

Arachidonic Acid

Recent evidence suggests that the prostaglandin isomer PGF2a has a potent ability to stimulate muscle growth. Arachidonic acid is a regulator of localized muscle inflammation, and may be a central nutrient controlling the intensity of the anabolic/tissue-rebuilding response to weight training.

Whilst the concept and feeling of post-exercise inflammation is familiar, post-training inflammation is indeed a bit more complex. Arachidonic acid is a very important compound due to its widespread role in the cell signalling that leads to growth.

There are certain pathways that start within skeletal muscle by the binding of exercise-related hormones (such as GH and/or IGF-1) to complementary receptors. These pathways up-regulate the expression of contractile proteins, thus increasing the fractional protein synthesis rate. This is of course, events that are essential of muscle growth.

Protein Synthesis

A process where by nitrogen from amino acids is arranged into structural proteins through the involvement of RNA and various enzymes. Protein synthesis is muscle growth. The more efficient this process the more efficiently you can build muscle.

Where does arachidonic acid fit in to all of this? This list shows what occurs to arachidonic acid after a muscle is damaged from exercise:

  • The activation of cytosolic phospholipase A2 (or cPLA2 which is an intramuscular enzyme) occurs.
  • cPLA2 causes the release of arachidonic acid into the cytoplasm (or internal portion) of the muscle cell.
  • An enzyme cyclooxygenase-2 (COX-2) catalyzes the multi-step synthesis of prostaglandins (i.e. PGE2, PGF2a) which are leached from the cell and initiate various physiological activity (i.e. vasodilation and inflammation).
  • Prostaglandins (specifically the PGF2a isomer) bind to prostanoid receptors on skeletal muscle and initiate signal transduction leading to muscle growth.

Arachidonic acid and PGF2a have been shown to facilitate ribosomal assembly in smooth muscle tissue, activating downstream proteins of the phosphoinositol-3 kinase complex.

Ribosomes synthesize contractile proteins of skeletal muscle provided by messenger RNA transcripts may seem relatively insignificant, PGF2a signalling is similar to the IGF-1 signalling, which canm induce skeletal muscle hypertrophy.

A recent study conducted at Baylor University demonstrated that AA supplementation favourably reduced a circulating pro-inflammatory cytokine (interleukin-6) that is associated with cardiovascular disease and muscle protein breakdown, while causing trend increases in resting PGF2a and PGE2 levels.

The Baylor study found that AA supplementation didn't affect any of the safety markers, such as heart rate, blood pressure, lipid panel, blood count or liver and kidney profile when the supplement was taken at the maximum recommended dosage (1,000mg daily) for 50 days. If you do not fit the population described in the Baylor study (i.e. you have high blood pressure, cholesterol, inflammatory disease etc.) or you need reassurance, then it would be advised to consult your physician prior to including AA or increasing consumption of any supplement or food for that matter that is high in AA.

Conclusion

Post-exercise soreness; it's a great indicator of muscle growth.

Avoid over the counter anti-inflammatory medications after working out due to evidence demonstrating decreases in muscle protein synthesis.

It may be an idea to supplement your diet with arachidonic acid or increase your consumption of natural sources, eggs and peanuts being to good sources.

Research has shown that trained men presented a 42% decrement in the skeletal muscle cell membrane. Therefore an increase in activity levels depletes fatty acid levels from skeletal muscle that are required for prostaglandin synthesis, further suggesting increased arachidonic acid would be positive.

References:

Andersson, A., A. Sjodin, A. Hedman, R. Olsson, and B. Vessby. Fatty acid profile of skeletal muscle phospholipids in trained and untrained young men. Am J Physiol Endocrinol Metab. 279:E744-751, 2000.

Aronson, D., M. D. Boppart, S. D. Dufresne, R. A. Fielding, and L. J. Goodyear. Exercise stimulates c-Jun NH2 kinase activity and c-Jun transcriptional activity in human skeletal muscle. Biochem Biophys Res Commun. 251:106-110, 1998.

Boppart, M. D., D. Aronson, L. Gibson, R. Roubenoff, L. W. Abad, J. Bean, L. J. Goodyear, and R. A. Fielding. Eccentric exercise markedly increases c-Jun NH(2)-terminal kinase activity in human skeletal muscle. J Appl Physiol. 87:1668-1673, 1999.

Boppart, M. D., S. Asp, J. F. Wojtaszewski, R. A. Fielding, T. Mohr, and L. J. Goodyear. Marathon running transiently increases c-Jun NH2-terminal kinase and p38 activities in human skeletal muscle. J Physiol. 526 Pt 3:663-669, 2000.

Glass, D. J. Molecular mechanisms modulating muscle mass. Trends Mol Med. 9:344-350, 2003.

Griendling, K. K., D. Sorescu, B. Lassegue, and M. Ushio-Fukai. Modulation of protein kinase activity and gene expression by reactive oxygen species and their role in vascular physiology and pathophysiology. Arterioscler Thromb Vasc Biol. 20:2175-2183, 2000.

Levonen, A. L., R. P. Patel, P. Brookes, Y. M. Go, H. Jo, S. Parthasarathy, P. G. Anderson, and V. M. Darley-Usmar. Mechanisms of cell signaling by nitric oxide and peroxynitrite: from mitochondria to MAP kinases. Antioxid Redox Signal. 3:215-229, 2001.

Lu, J., T. A. McKinsey, R. L. Nicol, and E. N. Olson. Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. Proc Natl Acad Sci U S A. 97:4070-4075, 2000.

Rao, G. N., N. R. Madamanchi, M. Lele, L. Gadiparthi, A. C. Gingras, T. E. Eling, and N. Sonenberg. A potential role for extracellular signal-regulated kinases in prostaglandin F2alpha-induced protein synthesis in smooth muscle cells. J Biol Chem. 274:12925-12932, 1999.

Trappe, T. A., F. White, C. P. Lambert, D. Cesar, M. Hellerstein, and W. J. Evans. Effect of ibuprofen and acetaminophen on postexercise muscle protein synthesis. Am J Physiol Endocrinol Metab. 282:E551-556, 2002.

Wilborn, C, M Roberts, C Kerksick, M Iosia, L Taylor, B Campbell, T Harvey, R Wilson, M. Greenwood, D Willoughby and R Kreider. Exercise & Sport Nutrition Laboratory, Center for Exercise, Nutrition & Preventive Health Research, Baylor University, Waco, TX 76798-7313.

http://en.wikipedia.org/wiki/Arachidonic_acid

http://en.wikipedia.org/wiki/Prostaglandins

http://www.nutros.com/nsr-0502t.html#_101