Home » Expert Guides » Supplements BCAA Supplements Guide: Powders, Benefits & Best Products 1. The Three BCAAs 3. BCAAs And Performance 4. Effects On Hormones 5. BCAAs And Fat Loss 6. BCAAs As Signaling Molecules This Guide Teaches You: What BCAAs are, and how they impact performance and muscle building.Why leucine, isoleucine, and valine are essential and must be obtained through diet.How studies back the effectiveness of BCAAs upon improving performance.How BCAAs positively impact testosterone levels when taken pre-workout.The benefits of supplementing with BCAAs during fat loss.The recommended daily BCAAs dosage.GNC Branched Chain Amino Acids 1800 (240 Caps) As a dietary supplement, take six capsules daily, either in the morning, evening or between meals on an empty stomach with a full glass of water. Use in conjuction with your strenuous exercise program. Serving Size 6 Soft Gel Capsules Servings Per Container 40 Vitamin E (as d-alpha Tocopherol)
** Daily Value (DV) not established Other Ingredients: Soybean Oil, Gelatin, Glycerin, Caramel Color, Titanium Dioxide (Natural Mineral Whitener) No Sugar, No Starch, No Artificial Color, No Artificial Flavors, No Preservatives, No Wheat, No Gluten, No Corn, No Dairy, Yeast Free Storage Instructions: Store in a cool dry place. Warning: After opening, keep tightly closed in refrigerator or other cool place. * These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure, or prevent any disease. GNC Women's Ultra Mega 50 Plus 1X90 Mini TabletsGNC PP 100% Whey Protein Amp Gold Adv Strawberry 1.98 LbsGNC Women's Hair Skin and Nails Formula (120 Caps)GNC Pump Fuel Powder V3 Raspberry Lemonade 1.9lbGNC Mega Men 50 Plus (120 Caps)GNC Amplified Mass XXX @ Vanilla (6 Lbs) • Growth, Performance & Recovery • AstraGin™ for Absorption Support What Makes BRANCHED CHAIN AMINO ACIDS BCAA™® Unique
SD Pharmaceuticals’ BRANCHED CHAIN AMINO ACIDS BCAA™ delivers a scientifically-validated BCAA ratio of 45% Leucine, 30% Valine and 25% Isoleucine. The precise 45:30:25 ratio is exactly what many clinical studies have used to support muscle growth and performance! In addition, SD Pharmaceuticals’ BRANCHED CHAIN AMINO ACIDS BCAA™ uses the clinically-tested absorption ingredient, AstraGin™ to support optimal absorption of the BCAAs! High-Quality Branched-Chain Amino Acids BCAAs are a group of essential amino acids that play a key role in protein synthesis (a.k.a. muscle growth) and energy production. BCAAs include L-leucine, L-Valine and L-Isoleucine. BCAAs make up 35 to 40% of essential amino acids in total body protein. Decreased Plasma BCAA Levels BCAAs are essential amino acids and cannot be made by the body. They must be ingested through food or supplementation. During exercise, BCAA metabolism in muscle tissue is increased. Therefore, after aerobic exercise (i.e., cardio) and anaerobic exercise (i.e., weight training) there is a significant decrease in plasma BCAA levels in muscle tissue.
Performance, Growth & Recovery Supplementation with BCAAs prevents the exercise-induced decline in plasma BCAAs and increases BCAA concentration in muscle tissue. BCAA’s are the only amino acids that are not readily degraded in the liver. Therefore, an increase in supplemental BCAA’s can reliably increase their concentration in blood and muscle tissue! The end results: better performance, growth and recovery support! Stack this product with Update your browser to view this website correctly.Update my browser now×Epidemiological and experimental data implicate branched-chain amino acids (BCAAs) in the development of insulin resistance, but the mechanisms that underlie this link remain unclear1, 2, 3. Insulin resistance in skeletal muscle stems from the excess accumulation of lipid species4, a process that requires blood-borne lipids to initially traverse the blood vessel wall. How this trans-endothelial transport occurs and how it is regulated are not well understood.
Here we leveraged PPARGC1a (also known as PGC-1α; encoded by Ppargc1a), a transcriptional coactivator that regulates broad programs of fatty acid consumption, to identify 3-hydroxyisobutyrate (3-HIB), a catabolic intermediate of the BCAA valine, as a new paracrine regulator of trans-endothelial fatty acid transport. We found that 3-HIB is secreted from muscle cells, activates endothelial fatty acid transport, stimulates muscle fatty acid uptake in vivo and promotes lipid accumulation in muscle, leading to insulin resistance in mice. Conversely, inhibiting the synthesis of 3-HIB in muscle cells blocks the ability of PGC-1α to promote endothelial fatty acid uptake. 3-HIB levels are elevated in muscle from db/db mice with diabetes and from human subjects with diabetes, as compared to those without diabetes. These data unveil a mechanism in which the metabolite 3-HIB, by regulating the trans-endothelial flux of fatty acids, links the regulation of fatty acid flux to BCAA catabolism, providing a mechanistic explanation for how increased BCAA catabolic flux can cause diabetes.
Mechanisms of disease Molecular biology Type 2 diabetes (a) Experimental strategy (top), representative images (bottom) and quantification (right) of Bodipy-FA (2–16 μM) uptake by endothelial cells (ECs) after exposure to control Dulbecco's modified Eagle's medium (DMEM) culture, conditioned media (CM) from control myotubes expressing GFP (Ct-CM) or myotubes expressing PGC-1α (α-CM). Scale bars, 50 μm. Bodipy-FA (8 μM) uptake by HUVECs treated with Ct-CM or α-CM at different time points (b), or in the presence of the indicated concentrations of unlabeled oleic acid for 5 min (c). (d) Staining by oil red O (ORO) of intracellular neutral lipids in HUVECs after prolonged exposure (24 h) to α-CM. Representative images (left) and quantification of ORO-positive lipid vesicles (middle) and Bodipy-positive lipid vesicles (right) are shown. Red scale bars, 50 μm; white scale bars, 10 μm. (e) Uptake of the indicated concentrations of Bodipy-FA by HUVECs after incubation with either Ct-CM (Ct) or α-CM (α) for the indicated durations.
(f) Experimental strategy (left). Quantification of Bodipy-FA (8 μM) transport across a tight endothelial cell monolayer treated with either Ct-CM or α-CM, with or without the fatty acid transport inhibitor SSO (middle). Representative images of myotubes that have taken up Bodipy-FA (green) transported through the monolayer (right). Scale bars, 10 μm. *P < 0.05 versus control; #P < 0.05 versus α-CM for all panels. Two-way analysis of variance (ANOVA) was used for f. Data are mean ± s.d. (s.d.) of at least three biological replicates. (a) Uptake of the indicated concentrations of Bodipy-FA by HUVECs after incubation with conditioned media from myotubes expressing GFP (Ct-CM) or PGC-1α (α-CM), after treatment of the endothelial cells with sFlt1 or SU11248 (SU). (b) Uptake of the indicated concentrations of Bodipy-FA by HUVECs after incubation with Ct-CM or with CM from PGC-1α–expressing myotubes treated with control siRNA (Ct si) or Vegfb siRNA (VB si). (c) Uptake of Bodipy-FA (2 μM) by endothelial cells (EC) isolated from Flt1flox/flox or Flt1flox/flox;
Kdrflox/flox mice, followed by infection with adenovirus expressing GFP (Ct) or Cre recombinase (Flt1−/− or Flt1−/−;Kdr−/−), and subsequent incubation with Ct-CM or α-CM. (d–f) Uptake of the indicated concentrations of Bodipy-FA by HUVECs after incubation with size-exclusion chromatography fractions of α-CM (d), α-CM that had been heat-inactivated at the indicated temperature (e) or α-CM treated with trypsin (f). Ct-CM and α-CM were used as negative and positive controls, respectively. In d, protein levels of the fractions are shown in the inset. Silver staining of Ct-CM, α-CM and α-CM treated with trypsin is shown in f (left). (g) Uptake of Bodipy-FA (8 μM) by HUVECs after incubation with HILIC fractions of conditioned medium from PGC-1α–expressing myotubes that had been treated with vehicle (Veh) or the indicated inhibitors. (h) Selective ion monitoring (SIM) of m/z = 103.1 in HILIC fraction 27 of conditioned medium from PGC-1α–expressing myotubes that had been treated with vehicle (Veh) or the indicated inhibitors.
(i) SIM of m/z = 103.1 in HP-HILIC fractions (top left) and tandem-mass spectrometry (MS2) analysis (right) and uptake of Bodipy-FA by HUVECs after incubation with HP-HILIC fractions (bottom left). Red box (left) highlights the paracrine activity. (j) Uptake of Bodipy-FA (2 μM) by HUVECs after incubation with the indicated concentrations of 3-HIB for 1 h. Student's t test; *P < 0.05 versus control for all panels. Data are mean ± s.d. of at least three biological replicates. (a) Schematic of the valine catabolism pathway. BCKDH, branched-chain α-keto acid dehydrogenase; BCKDK, branched-chain ketoacid dehydrogenase kinase; PPM1K, protein phosphatase Mg2+/Mn2+-dependent 1K; ACADSB, short/branched chain acyl-CoA dehydrogenase; HADHA, hydroxyacyl-CoA dehydrogenase alpha subunit. (b) Chemical structures of 13C-labeled valine (top left) and 13C-labeled 3-HIB derived from 13C-labeled valine (top right). The relative abundance of 12C–3-HIB and 13C-labeled 3-HIB in conditioned medium from PGC-1α–expressing myotubes incubated with 12C-valine (bottom left) and 13C-labeled valine (bottom right).
(c) qPCR analysis of valine metabolic gene expression in myotubes expressing either PGC-1α or a GFP control. (d) Representative images of HUVECs that have taken up Bodipy-FA (left) and quantification (right) after exposure of the cells to conditioned medium from GFP-expressing myotubes (Ct-CM) or from PGC-1α–expressing myotubes (α-CM) that had been treated with Hibch siRNA or Hibadh siRNA. (e) Immunoblot for HIBADH in mouse skeletal muscle after injection of intact animals with control (Ct si) or Hibadh (Hibadh si) siRNA (left); quantification of HIBADH abundance (middle); and muscle triacylglyceride (TAG) levels (right). n = 8 per group. Two-way ANOVA for d. Data are mean ± s.d. of at least three biological replicates. (a,b) qPCR analysis of valine metabolic enzyme expression (a; n = 6 per group) and measurement of 3-HIB levels (b; n = 3 per group) in muscle from wild-type (WT) or PGC-1α–muscle specific transgenic mice (MCK-α). (c) Schematic of the fatty acid (FA) uptake assay in vivo (left).
Representative images (middle) and quantification (right, n = 4 per group) of fatty acid uptake in the thigh of luciferase transgenic (Luc) or Luc;Dashed circles indicate the heart and thigh regions used for quantification. Scale bar, 1 cm. (d) Representative images (left) and quantification (right, n = 4) of fatty acid uptake in the thigh of Luc mice fed with vehicle (Veh) or 3-HIB in a food paste for 1.5 h. Scale bar, 1 cm. (e–i) Measurements of triacylglyceride (e; n = 3 per group); total diglyceride (DAG; left in f; n = 4 per group) and specific DAG species (right in f; n = 4 per group); PKC-θ membrane translocation (g; n = 4 per group); levels of phosphorylated AKT (pAKT) and AKT1 as assessed by immunoblotting (h; n = 4 per group) in muscle; and systemic glucose tolerance (i; n = 8) of mice provided with vehicle (Veh) or 3-HIB in the drinking water for 2 weeks. (j) Measurements of 3-HIB levels in muscle of WT (Ct) and db/db mice (left; n = 10 per group) and in muscle biopsies of nondiabetic control (Ct) and people with type 2 diabetes (T2D) (right).