Lower Myostatin Naturally for Maximum Muscle Growth and Fat Loss
Lower Myostatin Naturally for Maximum Muscle Growth and Fat Loss
By Michael J. Rudolph, Ph.D.
Senior Science Editor
Out of all the molecules in the human body that directly influence muscle size, myostatin is certainly one of the more powerful ones, based on its potent ability to prevent muscle growth. Myostatin is a member of the transforming growth factor-beta (TGF-beta) super family of growth factors where, despite being a growth factor, it actually reduces muscle growth by initiating several pathways that inhibit muscle hypertrophy while stimulating muscle atrophy. More specifically, myostatin inhibits muscle growth by inhibiting the formation of new muscle fibers, a process known as myogenesis1, while decreasing mTOR-driven protein synthesis in muscle cells.2
In addition to myostatin’s ability to stop muscle growth, additional scientific evidence highlights myostatin’s capacity to increase body fat, primarily by decreasing sensitivity to the hormone leptin.3 Given that leptin is a signal to the brain that decreases appetite while simultaneously stimulating the rate of fatty acid oxidation, a decreased sensitivity to leptin brought on by myostatin increases food consumption while decreasing fat burning— causing the unwanted accumulation of body fat.
The “fat increasing” characteristic of myostatin represents one more bona fide reason to want to decrease myostatin function, especially for anyone trying to build a more lean and muscular physique. Interestingly, a number of innovative ways have been discovered that inhibit myostatin activity, conceivably enhancing muscle growth and fat loss in remarkable ways.
Low-Intensity Aerobic Exercise
As expected, lifting weights has been shown to decrease myostatin levels, representing one of the many ways that intense weightlifting triggers muscle growth. However, a study by Hittel et al.4 unexpectedly showed that low-intensity aerobic exercise can also considerably decrease the amount of myostatin— establishing a unique way to manipulate myostatin, supporting muscle growth.
In the above study, researchers found that myostatin levels decreased by approximately 37 percent after all 10 male subjects performed cardiovascular training at a pretty low intensity level that only burned approximately 1,200 calories per week. Interestingly, this study also showed that when myostatin levels decreased there was a substantial increase in insulin sensitivity. Because insulin is an extremely anabolic hormone that has the ability to drastically increase muscle protein synthesis, enhancing muscle growth, this finding represents an additional mechanism by which myostatin reduction, due to low-intensity aerobic training, could enhance muscle growth.
Creatine
Creatine is a well-characterized compound that has been clearly shown to enhance muscle size and strength. Although creatine’s exact mechanism of action is unknown, research scientists have heavily examined it and some of its functional details have been elucidated.
In addition to creatine’s obvious function as a primary energy storage molecule used to regenerate muscle ATP, thus prolonging muscle contraction, creatine has also been shown to stimulate muscle cell formation5 and muscle growth by stimulating the production of muscle proteins such as myosin.6 A study by Saremi et al.7 demonstrated that creatine consumption causes a decrease in myostatin levels in muscle cells, leading to significant muscle growth.
In a double-blind study, 27 healthy males performed resistance training or resistance training supplemented with creatine (0.3 grams of creatine for every kilogram of the subject’s bodyweight per day for the first week loading phase, followed by 0.05 grams of creatine for every kilogram of the subject’s bodyweight for the rest of the study) for a total of eight weeks. Both groups showed decreased levels of myostatin, but the group that performed resistance training and consumed creatine had a considerably larger decrease in myostatin levels along with greater gains in muscle mass and strength.
Although the precise molecular interactions between creatine and myostatin are still unknown, this study clearly demonstrates creatine as an ergogenic aid that regulates myostatin levels— improving muscle growth and strength.
Vitamin D
Vitamin D is a fat-soluble steroid-like vitamin that functions as a prohormone, aiding many different processes such as the absorption and metabolism of calcium and phosphorous— promoting bone health. Vitamin D also has several muscle-promoting properties associated with the ability to boost testosterone levels.
A study by Garcia et al.8 uncovered another interesting influence that vitamin D has on muscle growth. Researchers showed that vitamin D exposure decreases the amount of myostatin found in isolated muscle cells, generating greater muscle growth. In addition to the decrease in myostatin, this study showed that vitamin D triggers an increase in follistatin, which is a powerful inhibitor of myostatin— which increases muscle mass by inhibiting myostatin.9
Ultimately, this study indicates that the decrease in myostatin level and activity caused by vitamin D significantly increased muscle fiber size— demonstrating vitamin D’s substantial ability to increase muscle mass.
Essential Amino Acids (EAAs)
Many different studies have previously reported that EAAs potently activate mTOR-stimulated muscle protein synthesis, leading to greater muscle size.10,11 However, a study by Drummond et al.12 demonstrated that EAAs possess the uniquely powerful ability to also decrease genetic expression of myostatin in muscle cells.
EAAs decrease myostatin levels by stimulating the production of a class of molecules known as micro-RNA that have the ability to strongly decrease the expression level of specific genes. The unique finding in this study was that several micro-RNA molecules were produced in human skeletal muscle following the ingestion of 10 grams of EAAs, which subsequently decreased myostatin expression by approximately 50 percent.
Interestingly, another study by Callis et al.13 also showed that myostatin was the target of micro-RNA regulation— where the micro-RNA molecule called miR-208a boosted muscle hypertrophy by suppressing myostatin expression.
Although further work is needed to elucidate the precise role that micro-RNA has in the regulation of myostatin and muscle mass following EAA consumption, taken together, these two investigations represent a completely novel and forceful way to decrease myostatin— conceivably initiating new approaches to trigger tremendous muscle size.
Maximizing Muscle Growth and Fat Loss
In summary, myostatin is an unbelievably responsive target where even the slightest reduction in its activity produces remarkable muscle growth while radically decreasing body fat. Moreover, scientific insight has shed light on a number of diverse ways to decrease myostatin activity— potentially transforming the capacity to pack on muscle while simultaneously reducing body fat. More precisely, a diet supplemented with creatine, vitamin D and EAAs in combination with low-intensity cardiovascular exercise at the end of your workout should potently inhibit myostatin’s physique-destroying capacity, while maximizing muscle growth and fat loss.
For most of Michael Rudolph’s career he has been engrossed in the exercise world as either an athlete (he played college football at Hofstra University), personal trainer or as a Research Scientist (he earned a B.Sc. in Exercise Science at Hofstra University and a Ph.D. in Biochemistry and Molecular Biology from Stony Brook University). After earning his Ph.D., Michael investigated the molecular biology of exercise as a fellow at Harvard Medical School and Columbia University for over eight years. That research contributed seminally to understanding the function of the incredibly important cellular energy sensor AMPK— leading to numerous publications in peer-reviewed journals including the journal Nature. Michael is currently a scientist working at the New York Structural Biology Center doing contract work for the Department of Defense on a project involving national security.
References:
1. Allen DL, Hittel DS, et al. Expression and function of myostatin in obesity, diabetes, and exercise adaptation. Med Sci Sports Exerc 1997;43(10): p. 1828-35.
2. Amirouche A, et al. Down-regulation of Akt/mammalian target of rapamycin signaling pathway in response to myostatin overexpression in skeletal muscle. Endocrinology 2009;150(1): p. 286-94.
3. Choi SJ, et al. Increased energy expenditure and leptin sensitivity account for low fat mass in myostatin-deficient mice. Am J Physiol Endocrinol Metab 2010;300(6): p. E1031-7.
4. Hittel D.S, et al. Myostatin decreases with aerobic exercise and associates with insulin resistance. Med Sci Sports Exerc 2010;42(11): p. 2023-9.
5. Willoughby DS and Rosene JM. Effects of oral creatine and resistance training on myogenic regulatory factor expression. Med Sci Sports Exerc 2003;35(6): p. 923-9.
6. Willoughby DS and Rosene J. Effects of oral creatine and resistance training on myosin heavy chain expression. Med Sci Sports Exerc 2001;33(10): p. 1674-81.
7. Saremi A, et al. Effects of oral creatine and resistance training on serum myostatin and GASP-1. Mol Cell Endocrinol 2009;317(1-2): p. 25-30.
8. Garcia LA, et al. 1,25(OH)2vitamin D3 stimulates myogenic differentiation by inhibiting cell proliferation and modulating the expression of promyogenic growth factors and myostatin in C2C12 skeletal muscle cells. Endocrinology 2011;152(8): p. 2976-86.
9. Cash JN, et al. Structure of myostatin•follistatin-like 3: N-terminal domains of follistatin-type molecules exhibit alternate modes of binding. J Biol Chem 2012;287(2): p. 1043-53.
10. Fujita, S, et al. Nutrient signalling in the regulation of human muscle protein synthesis. J Physiol 2007;582(Pt 2): p. 813-23.
11. Drummond MJ and Rasmussen BB. Leucine-enriched nutrients and the regulation of mammalian target of rapamycin signalling and human skeletal muscle protein synthesis. Curr Opin Clin Nutr Metab Care 2008;11(3): p. 222-6.
12. Drummond MJ, et al. Essential amino acids increase microRNA-499, -208b, and -23a and downregulate myostatin and myocyte enhancer factor 2C mRNA expression in human skeletal muscle. J Nutr 2009;139(12): p. 2279-84.
13. Callis TE, et al. MicroRNA-208a is a regulator of cardiac hypertrophy and conduction in mice. J Clin Invest 2009;119(9): p. 2772-86.
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