EAAs or BCAAs. When to take them and why!

-BCAAs do not increase protein synthesis above basal levels, but they do decrease protein breakdown. They are very benificial while cutting and even may increase fat loss then. BCAAs seem to be the perfect supplement to use for people as a "midnight shake". It only gives you a few kcals. (20 kcal. since 5 g will probably suffice) so you don't need to be afraid to gain fat mass compared to a midnight protein shake.
-EAAs do increase protein synthesis above basal levels. This is what you want to use pre/post workout to increase muscle growth.

WHY BCAA'S FOR RECOVERY:
A) bcaas prevent protein breakdown, but do not increase protein synthesis.
B) Helps in fat loss while cutting.
C) Prevents a decrease in glutamine
D) Prevents muscle damage.

1)It is known that BCAA oxidation is promoted by exercise (E1, E106, T13).
2)Promotion of fatty acid oxidation upregulates the BCAA catabolism (T13).
3) 77 mg BCAAs/kg supplementation before exercise results in a large decrease in release of EAA, (531 +/- 70 mumol/kg) for BCAA vs. (924 +/- 148 mumol/kg) for control (E105).
4) A cutting diet high in BCAAs increases body weight loss and % of fat loss more than a calorie restricted high protein cutting diet (E7).
5)No toxic effects of BCAAs were observed at a dose of 2.5 g·kg-1·d-1 for 3 mo or 1.25 g·kg-1·d-1 for 1 y. There are no reports concerning BCAA toxicity in relation to exercise and sports (E106).

BCAAs prevent protein breakdown, but do not increase protein synthesis.
-Since 1978 a variety of studies have been performed in humans where BCAAs or leucine alone was administrated in varying amounts and durations. An anabolic effect of leucine and the branched-chain amino acids (BCAAs) on reduction of muscle protein breakdown was found in these studies, with no measured effect upon muscle protein synthesis. In addition, no untoward effects have been reported in any of these studies from infusion of the BCAAs at upward 3 times basal flux or 6 times normal dietary intake during the fed portion of the day (B1).
-BCAA infusion in 10 postabsorptive normal subjects causes a 4-fold rise in arterial BCAA levels. Plasma insulin levels were unchanged from basal levels. Whole-body phenylalanine flux, an index of proteolysis, was significantly suppressed by BCAA infusion. Despite the rise in whole-body non-oxidative leucine disposal, and in forearm leucine uptake and disposal, forearm phenylalanine disposal, an index of muscle protein synthesis, was not stimulated by infusion of branched-chain amino acids (B2).
-BCAAs during 1h cycle exercise and a 2h recovery period does not influence the rate of exchange of the aromatic AAs during exercise. In the recovery period, a faster decrease in the muscle concentration of aromatic AAs was found (46% compared with 25% in the placebo condition). There was also a tendency to a smaller release (an average of 32%) of these amino acids from the legs. The results suggest that BCAA have a protein-sparing effect during the recovery after exercise (E5)
-7.5-12 g BCAAs during intense exercise (a 30 km cross-country race and a full marathon) increases BCAA plasma and muscle concentration. In the placebo group plasma BCAA decreased and left muscle levels unchanged. The placebo group showed a 20-40% increase in the muscle concentration of aromatic AAs. BCAA supplementation prevented this increase in aromatic AAs in both muscle and plasma. These results suggest that an intake of BCAAs during exercise can prevent or decrease the net rate of protein degradation caused by heavy exercise (E8).
-77 mg BCAAs/kg supplementation before exercise resulted in a doubling (P < 0.05) of the arterial BCAA levels before exercise (339 +/- 15 vs. 822 +/- 86 microM). During the 60 min of exercise, the total release of BCAA was 68 +/- 93 vs. 816 +/- 198 mumol/kg (P < 0.05) for the BCAA and control trials, respectively. Furthermore, the increased intramuscular and arterial BCAA levels before and during exercise result in a suppression of endogenous muscle protein breakdown during exercise.(E105).

Helps in fat loss while cutting
-BCAA supplementation (76% leucine) in combination with moderate energy restriction has been shown to induce significant and preferential losses of visceral adipose tissue and to allow maintenance of a high level of performance (E14).
-In adipocytes from fed rats, the rate of fatty acid synthesis in the presence of glucose and insulin was inhibited 40% by valine (5 mm) (E4).
-Twenty-five competitive wrestlers restricted their caloric intake (28 kcal.kg-1.day-1) for 19 days. A high-BCAA diet provided 4 kg of weight loss, and 17,3% decrease in fat loss. There was no change in aerobic (VO2max) (p > 0.75) and anaerobic capacities (Wingate test) (p > 0.81), and in muscular strength (p > 0.82). (E7).

Prevents a decrease in glutamine
-Following an exercise bout, a decrease in plasma glutamine concentration can be observed, which is completely abolished by BCAA supplementation (G12).
-BCAA supplementation during a triathlon completely prevents the decrease in plasma glutamine (G13).

Prevents muscle damage
-We hypothesized that BCAA supplementation would reduce the serum activities of intramuscular enzymes associated with muscle damage. 120 minutes exercise on a cycle ergometer significantly increases serum creatine kinase (CK) and lactate dehydrogenase (LDH) up to 5d postexercise.
12 g BCAAs for 14d in 16 men (the exercise on day 7) significantly reduces this change in LDH and CK (B3).

WHY ESSENTIAL AMINO ACIDS (EAAs) FOR RECOVERY:
A) EAAs increase protein synthesis above basal levels
B) Prevents muscle soreness

1) Nonessential amino acids are not necessary for stimulation of net muscle protein balance (6 g EAAs provides double the response of 3 g EAA and 3 g of nonessentail AA) (E12).
2) 40 g EAAs does not increase net protein balance more than 20 g EAAs (E15).
2) Ingestion of oral essential amino acids results in a change from net muscle protein degradation to net muscle protein synthesis after heavy resistance exercise in humans similar to that seen when the amino acids were infused (E15).

EAAs increase protein synthesis above basal levels
-EEAs (essential amino acids) increases net muscle protein balance. 2 x 6 g provides double the response of 2 x 3 g (E12).
-Consumption of 40 g EAAs after heavy resistance training results in a change from net protein degradation (-50 +/- 23 nmol. min-1. 100 ml leg volume-1) to net protein synthesis (29 +/- 14 nmol. min-1. 100 ml leg volume-1; P < 0.05) (E15).
-A 0.15 g/kg/h AA infusion for 3 h in 6 normal men increases muscle protein synthesis by 141%. After exerecise this increase is 291%. Muscle protein breakdown was not significantly affected (E23).
-Consumption of 6 g EAA + 35 g sucrose immediately before exercise elevates response of net muscle protein synthesis more than consumption following exercise. Total net phenylalanine uptake across the leg was greater (P = 0.0002) during PRE (209 ± 42 mg) than during POST (81 ± 19) (E102).
-6 g amino acids consumed at 1 and 2 h after resistance exercise increases protein synthesis (total net uptake of phenylalanine across the leg) (71 +/- 13 mg x leg x 3h). Prior intake of amino acids and carbohydrate does not diminish the metabolic response to a second comparable dose ingested 1h later (K24).

Prevents muscle soreness
-3.6 g AAs before and after exercise + 2 doses/d for 4 d after the exercise suppresses the rise in serum creatine kinase activity. This also diminished muscle soreness (E106).