In addition to the proper amount of sleep, do not overdo your training regimen. While you might be tempted to think that "more is better," in fact the opposite is true. You can reach a point known as "over-training", in which you'll lose the ability to "pump" (engorge the muscles with oxygen-rich blood) your muscles, and this can even lead to muscle wasting—exactly the opposite of what you are trying to achieve. Here are some symptoms to be aware of if you think you may be falling into the over-training zone:
The US FDA reports 50,000 health problems a year due to dietary supplements  and these often involve bodybuilding supplements. For example, the "natural" best-seller Craze, 2012's "New Supplement of the Year" by bodybuilding.com, widely sold in stores such as Walmart and Amazon, was found to contain N,alpha-Diethylphenylethylamine, a methamphetamine analog. Other products by Matt Cahill have contained dangerous substances causing blindness or liver damage, and experts say that Cahill is emblematic for the whole industry.
Bodybuilders have THE BEST mind to muscle connection of any resistance-training athletes. Ask a seasoned bodybuilder to flex their lats or their rhomboids or their hamstrings and they will do it with ease. Ask other strength athletes and you will see them struggle and although they may tense up the target muscle they will also tense up about 15 other surrounding muscles. This is because strength athletes train MOVEMENTS. They don’t care about targeting their lats. They just want to do the most pull ups. They don’t worry about feeling their quads. They just want to squat maximum weight. Although this is an expected and positive thing for the most part, there are real benefits to being able to isolate and target muscles.
Make no mistake: Eating for muscle is just as important as lifting for muscle. The foods you grab in the morning on the way to work, the meals you pack for lunch and mid-afternoon, what you put into your body immediately following your workout, and your final meal of the day impact your results as much as, if not more than, the number of reps you squeeze out at the end of a set. But in reality, it can be tough to stick to a "clean" diet when you're busy. We know that adding another layer of complexity to life in the form of reading food labels and studying ingredient lists just isn't an option for most of us. Not to mention actually preparing all those healthy meals.
In muscle cells, the creatine transporter is predominantly localized to the sarcolemmal membrane. Western blot analysis of creatine transporter expression revealed the presence of two distinc protein bands, migrating at 55kDa and 70kDa on reducing SDS-PAGE gels. The 73kDa band has been reported to be the predominant band in humans, with no differences based on gender. A more recent report demonstrated that the 55kDa creatine transporter variant is glycosylated, forming the 73 kDa protein. Therefore, the 55 and 75kDa protein bands are actually immature and mature/processed forms of the creatine transporter protein, respectively.
There have been a few reported renal health disorders associated with creatine supplementation [73,74]. These are isolated reports in which recommended dosages are not followed or there is a history of previous health complaints, such as renal disease or those taking nephrotoxic medication aggravated by creatine supplementation . Specific studies into creatine supplementation, renal function and/or safety conclude that although creatine does slightly raise creatinine levels there is no progressive effect to cause negative consequences to renal function and health in already healthy individuals when proper dosage recommendations are followed [73-77]. Urinary methylamine and formaldehyde have been shown to increase due to creatine supplementation of 20 g/d; this however did not bring the production outside of normal healthy range and did not impact on kidney function [56,78]. It has been advised that further research be carried out into the effects of creatine supplementation and health in the elderly and adolescent [73,75]. More recently, a randomized, double blind, 6 month resistance exercise and supplementation intervention  was performed on elderly men and women (age >65 years) in which subjects were assigned to either a supplement or placebo group. The supplement group was given 5 g CM, 2 g dextrose and 6 g conjugated linoleic acid/d, whilst the placebo group consumed 7 g dextrose and 6 g safflower oil/d. CM administration showed significantly greater effects to improve muscular endurance, isokinetic knee extension strength, fat free mass and to reduce fat mass compared to placebo. Furthermore the supplement group had an increase in serum creatinine but not creatinine clearance suggesting no negative effect on renal function.
Similarly to complex training, contrast loading relies upon the enhanced activation of the nervous system and increased muscle fibre recruitment from the heavy set, to allow the lighter set to be performed more powerfully. Such a physiological effect is commonly referred to as post-activation potentiation, or the PAP effect. Contrast loading can effectively demonstrate the PAP effect: if a light weight is lifted, and then a heavy weight is lifted, and then the same light weight is lifted again, then the light weight will feel lighter the second time it has been lifted. This is due to the enhanced PAP effect which occurs as a result of the heavy lift being utilised in the subsequent lighter lift; thus making the weight feel lighter and allowing the lift to be performed more powerfully.
Genetic deficiencies in the creatine biosynthetic pathway lead to various severe neurological defects. Clinically, there are three distinct disorders of creatine metabolism. Deficiencies in the two synthesis enzymes can cause L-arginine:glycine amidinotransferase deficiency caused by variants in GATM and guanidinoacetate methyltransferase deficiency, caused by variants in GAMT. Both biosynthetic defects are inherited in an autosomal recessive manner. A third defect, creatine transporter defect, is caused by mutations in SLC6A8 and inherited in a X-linked manner. This condition is related to the transport of creatine into the brain.
^ Jump up to: a b c Brioche T, Pagano AF, Py G, Chopard A (April 2016). "Muscle wasting and aging: Experimental models, fatty infiltrations, and prevention". Mol. Aspects Med. 50: 56–87. doi:10.1016/j.mam.2016.04.006. PMID 27106402. In conclusion, HMB treatment clearly appears to be a safe potent strategy against sarcopenia, and more generally against muscle wasting, because HMB improves muscle mass, muscle strength, and physical performance. It seems that HMB is able to act on three of the four major mechanisms involved in muscle deconditioning (protein turnover, apoptosis, and the regenerative process), whereas it is hypothesized to strongly affect the fourth (mitochondrial dynamics and functions). Moreover, HMB is cheap (~30– 50 US dollars per month at 3 g per day) and may prevent osteopenia (Bruckbauer and Zemel, 2013; Tatara, 2009; Tatara et al., 2007, 2008, 2012) and decrease cardiovascular risks (Nissen et al., 2000). For all these reasons, HMB should be routinely used in muscle-wasting conditions especially in aged people. ... 3 g of CaHMB taken three times a day (1 g each time) is the optimal posology, which allows for continual bioavailability of HMB in the body (Wilson et al., 2013).
Creatine is involved indirectly in whole body methylation processes. This is due to creatine synthesis having a relatively large methyl cost, as the creatine precursor known as guanidinoacetate (GAA) requires a methyl donation from S-adenosyl methionine (SAMe) in order to produce creatine. This may require up to half of the methyl groups available in the human body.
One limitation of many free weight exercises and exercise machines is that the muscle is working maximally against gravity during only a small portion of the lift. Some exercise-specific machines feature an oval cam (first introduced by Nautilus) which varies the resistance, so that the resistance, and the muscle force required, remains constant throughout the full range of motion of the exercise.
In addition to improving athletic performance and muscle strength, creatine is taken by mouth for creatine deficiency syndromes that affect the brain, aging, bone density, chronic obstructive pulmonary disease (COPD), congestive heart failure (CHF), depression, diabetes, exercise tolerance, fibromyalgia, Huntington's disease, disease that cause inflammation in the muscles (idiopathic inflammatory myopathies), Parkinson's disease, diseases of the muscles and nerves, multiple sclerosis, muscle atrophy, muscle cramps, breathing problems in infants while sleeping, head trauma, Rett syndrome, an eye disease called gyrate atrophy, inherited disorders that affect the senses and movement, schizophrenia, muscle breakdown in the spine, and recovery from surgery. It is also taken by mouth to slow the worsening of amyotrophic lateral sclerosis (ALS, Lou Gehrig's disease), osteoarthritis, rheumatoid arthritis, McArdle's disease, and for various muscular dystrophies.
It is known that intracellular energy depletion (assessed by a depletion of ATP) stimulates AMPK activity in order to normalize the AMP:ATP ratio, and when activated AMPK (active in states of low cellular energy and colocalizes with creatine kinase in muscle tissue) appears to inhibit creatine kinase via phosphorylation (preserving phosphocreatine stores but attenuating the rate that creatine buffers ATP). While phosphocreatine technically inhibits AMPK, this does not occur in the presence of creatine at a 2:1 ratio. It seems that if the ratio of phosphocreatine:creatine increases (indicative of excess cellular energy status) that AMPK activity is then attenuated, since when a cell is in a high energy status, there is less AMP to directly activate AMPK.