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-BCAAs verhogen de proteine synthese niet boven basale waarden, maar ze verminderen spierafbraak. Ze zijn waardevol tijdens het cutten en kunnen mogelijk zelfs de vetverbranding stimuleren. BCAAs zijn het perfecte supplement voor mensen die ervoor kiezen een "middernacht shake" te gebruiken. Ze geven maar een paar calorieen. (20 kcal. aangezien 5 g BCAAs waarschijnlijk al voldoende is), dus je hoeft niet bang te zijn voor de mogelijke vetmassa die je zou kunnen winnen bij een proteine shake in de nacht.
-Essentiele aminozuren kunnen daadwerkelijk proteine synthese verhogen boven basale waarden. Dit is wat je wilt gebruiken voor en na de training om spiermassa te winnen.
WAAROM BCAA'S VOOR HERSTEL:
A) bcaas voorkomen proteine afbraak, maar verhogen de proteine synthese niet.
B) Help bij vetverbranding tijdens cutten.
C) Voorkomen afname van glutamine.
D) Voorkomen voor een deel spierschade tijdens training.
1)BCAA oxidatie wordt gestimuleerd door training (E1, E106, T13).
2)Stimulering van vetverbranding verhoogt BCAA catabolisme (T13).
3)77 mg BCAAs/kg supplementatie voor de training resulteert in een sterkere afname in de afgifte van essentiele aminozuren. (531 +/- 70 mumol/kg) voor BCAA vs. (924 +/- 148 mumol/kg) voor de controle groep (E105).
4)Een cutting dieet hoog in BCAAs verhoogt verlies van lichaamsgewicht en % van vetverlies meer dan een hoog proteine dieet tijdens cutten (E7).
5)Geen giftige effecten van BCAAs zijn bemerkd bij een dosering van 2.5 g/kg/dag voor 3 maanden, of 1.25 g/kg/dag voor een jaar. Er zijn geen gerapporteerde giftigheidsverschijnselen betreffende BCAAs in relatie tot training en sport (E106).
bcaas voorkomen proteine afbraak, maar verhogen de proteine synthese niet
-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).
Help bij vetverbranding tijdens cutten
-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).
Voorkomen afname van 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).
Voorkomen voor een deel spierschade tijdens training
-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).
WAAROM ESSENTIELE AMINOZUREN (EAAs) VOOR HERSTEL:
A) EAAs verhogen proteine synthese boven basale waarden.
B) Voorkomen van spierpijn
1)Niet-essentiele aminozuren zijn niet nodig voor stimuleren van de netto spier-proteine balans (6 g EAAs geven een 2 x zo sterk resultaat als 3 g EAAs en 3 g niet-essentiele aminozuren) (E12).
2)40 g EAAs verhogen de proteine balans niet meer dan 20 g EAAs (E15).
3)Inname van orale EAAs veroorzaken een verandering van netto spier proteine afbraak naar netto spier proteine synthese na zware krachttraining in mensen vergelijkbaar met EAAs supplementatie via een infuus (E15).
EAAs verhogen proteine synthese boven basale waarden
-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).
Voorkomen van spierpijn
-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).
REFERENTIES
(B1)http://www.ncbi.nlm.nih.gov/entrez....ry_hl=1
(B2)http://www.ncbi.nlm.nih.gov/entrez....bstract
(B3)http://www.ncbi.nlm.nih.gov/entrez....bstract
(E1) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E4) http://www.ncbi.nlm.nih.gov/entrez....bstract
(E5) http://ajpendo.physiology.org/cgi/co...ull/281/2/E365
(E7) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E8) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E12) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E14) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E15) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E23) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E102) http://ajpendo.physiology.org/cgi/co...act/281/2/E197
(E105) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E106)http://www.nutrition.org/cgi/content/full/134/6/1583S
(G12) http://www.ncbi.nlm.nih.gov/entrez....ry_hl=1
(G13) http://www.ncbi.nlm.nih.gov/entrez....ry_hl=1
(K24) http://www.ncbi.nlm.nih.gov/entrez....bstract
(T13) http://www.ncbi.nlm.nih.gov/entrez....nalLink
-Essentiele aminozuren kunnen daadwerkelijk proteine synthese verhogen boven basale waarden. Dit is wat je wilt gebruiken voor en na de training om spiermassa te winnen.
WAAROM BCAA'S VOOR HERSTEL:
A) bcaas voorkomen proteine afbraak, maar verhogen de proteine synthese niet.
B) Help bij vetverbranding tijdens cutten.
C) Voorkomen afname van glutamine.
D) Voorkomen voor een deel spierschade tijdens training.
1)BCAA oxidatie wordt gestimuleerd door training (E1, E106, T13).
2)Stimulering van vetverbranding verhoogt BCAA catabolisme (T13).
3)77 mg BCAAs/kg supplementatie voor de training resulteert in een sterkere afname in de afgifte van essentiele aminozuren. (531 +/- 70 mumol/kg) voor BCAA vs. (924 +/- 148 mumol/kg) voor de controle groep (E105).
4)Een cutting dieet hoog in BCAAs verhoogt verlies van lichaamsgewicht en % van vetverlies meer dan een hoog proteine dieet tijdens cutten (E7).
5)Geen giftige effecten van BCAAs zijn bemerkd bij een dosering van 2.5 g/kg/dag voor 3 maanden, of 1.25 g/kg/dag voor een jaar. Er zijn geen gerapporteerde giftigheidsverschijnselen betreffende BCAAs in relatie tot training en sport (E106).
bcaas voorkomen proteine afbraak, maar verhogen de proteine synthese niet
-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).
Help bij vetverbranding tijdens cutten
-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).
Voorkomen afname van 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).
Voorkomen voor een deel spierschade tijdens training
-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).
WAAROM ESSENTIELE AMINOZUREN (EAAs) VOOR HERSTEL:
A) EAAs verhogen proteine synthese boven basale waarden.
B) Voorkomen van spierpijn
1)Niet-essentiele aminozuren zijn niet nodig voor stimuleren van de netto spier-proteine balans (6 g EAAs geven een 2 x zo sterk resultaat als 3 g EAAs en 3 g niet-essentiele aminozuren) (E12).
2)40 g EAAs verhogen de proteine balans niet meer dan 20 g EAAs (E15).
3)Inname van orale EAAs veroorzaken een verandering van netto spier proteine afbraak naar netto spier proteine synthese na zware krachttraining in mensen vergelijkbaar met EAAs supplementatie via een infuus (E15).
EAAs verhogen proteine synthese boven basale waarden
-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).
Voorkomen van spierpijn
-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).
REFERENTIES
(B1)http://www.ncbi.nlm.nih.gov/entrez....ry_hl=1
(B2)http://www.ncbi.nlm.nih.gov/entrez....bstract
(B3)http://www.ncbi.nlm.nih.gov/entrez....bstract
(E1) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E4) http://www.ncbi.nlm.nih.gov/entrez....bstract
(E5) http://ajpendo.physiology.org/cgi/co...ull/281/2/E365
(E7) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E8) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E12) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E14) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E15) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E23) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E102) http://ajpendo.physiology.org/cgi/co...act/281/2/E197
(E105) http://www.ncbi.nlm.nih.gov/entrez....nalLink
(E106)http://www.nutrition.org/cgi/content/full/134/6/1583S
(G12) http://www.ncbi.nlm.nih.gov/entrez....ry_hl=1
(G13) http://www.ncbi.nlm.nih.gov/entrez....ry_hl=1
(K24) http://www.ncbi.nlm.nih.gov/entrez....bstract
(T13) http://www.ncbi.nlm.nih.gov/entrez....nalLink
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