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The Effects of AstraGin® on Protein Absorption and Synthesis in Muscles

AstraGin®  / Uncategorized  / The Effects of AstraGin® on Protein Absorption and Synthesis in Muscles

The Effects of AstraGin® on Protein Absorption and Synthesis in Muscles

AstraGin® is a proprietary plant-derived nutraceutical ingredient developed by NuLiv Science. AstraGin® has shown in over a dozen In Vitro studies to improve the absorption of amino acids, peptides, folate, glucosamine and other nutrients in Caco-2 cell, the gold standard used by drug companies to study the absorption of new drugs.

AstraGin® also has shown in normal and TNBS-induced colitis rat models to enhance the expression levels of SGLT1 and CAT1 in jejunum and ileum, to increase the absorption of cationic amino acids, and to reduce the inflammation in colon bowel wall of colitis rat. Specifically, AstraGin® has shown to:

• Increases the steady-state absorption rate of arginine, agmatine, β-alanine, citrulline,
creatine, leucine, peptides and tryptophan by 67%, 36%, 25%,45%, 33%, 58%, 41% and 53%(1)
• Increase curcumin absorption by 92% (2)
• Increases vitamins absorption such as folate by 50% (3)
• Increases polyunsaturated fatty acid (derived from flax oil and fish oil) by 58% and 100%(4)
• Increase glucosamine absorption by 23% (5)
• Increases omega-7 fatty acid (Palmitoleic acid) by 39% (6)
• Increase ATP production in liver by 18% (7)
• Reduce intestinal wall inflammation by 73%(8)

These studies demonstrate when AstraGin® is added to protein, it increases the amount of protein in its digested forms of amino acids and peptides in the bloodstream that are transported to all cells in the body.

Furthermore, AstraGin® is capable of increasing protein synthesis in muscle to increase muscle growth (together with weight training) through enhanced leucine absorption as well as mTOR pathways(1, 11-21); promoting glucose metabolism and mitochondrial functions(22,23); regulating appetite(28-31); and promoting gut health, immune functions, and nutritional profile(8, 32, 33).

AstraGin® increases the absorption and bioavailability of amino acids and peptides in bloodstream

Protein plays a crucial role in almost all biological processes and amino acids are the building blocks of it. A large proportion of our cells, muscles, and tissue is made up of amino acids (9). They carry out many important bodily functions, such as giving cells their structure. Peptides have many biological functions, including antimicrobial, angiotensin-converting enzyme inhibition, antioxidant, opioid, and immunomodulation(10).

AstraGin® increases the absorption of many amino acids and peptides in the gut (1) so more are delivered to the bloodstream to all cells in the body.

AstraGin® increases protein synthesis in muscle

One of the most researched pathways of muscle growth is the mTOR pathway (mechanistic target of rapamycin), and leucine activates complex muscle-building pathways via mTOR. (11-18). AstraGin® has shown to increase intestinal leucine absorption by 58% in 15 minutes(1).

In addition, published papers have demonstrated that a key compound in AstraGin®, ginsenosides, activates mTOR signal pathway by regulating upstream kinases in muscle cells(20), and another key compound in AstraGin®, astragalosides, also affects mTOR pathway through its regulation on insulin levels(21).Lastly, AstraGin® increases intestinal arginine absorption by 67% that also triggers the mTOR pathway(1, 19).

AstraGin® promotes glucose metabolism and mitochondrial functions

FFA (free fatty acids) impairs glucose metabolism and mitochondrial functions while polyunsaturated fatty acids do not (22, 23). Impaired glucose metabolism and mitochondrial functions lead to decreased ATP synthesis, decreased mitochondrial respiration, and decreased oxidative phosphorylation(22-25). AstraGin® inhibits saturated fatty acid (Palmitic acid) absorption by 19% while increases the absorption of polyunsaturated fatty acids omega-7 fatty acid, flax oil, and fish oil by 39%, 58%, and 100% (4).

AstraGin® regulates appetite

Cholecystokinin, peptide YY, incretins gastric inhibitory peptide, and glucagon-like peptide are produced in the human body when glucose, amino acids, peptides, and fat are present in the gut(26, 27). These hormones potentiate insulin secretion from β-cells and are associated with regulation of food intake(26, 27). Tryptophan is a precursor of the neurotransmitter serotonin, which acts as an anorexigenic signal in the brain to stimulate satiety(28-31). AstraGin® up-regulates peptide absorption by 41% (1) and tryptophan absorption by 53% (1) to regulate appetite.

AstraGin® promotes gut health, immune functions, and nutritional profile

AstraGin® has a positive effect on gut health due to its ability to reduce inflammation in the intestinal wall by 73% in vivo(8). A healthy gut is beneficial for good bacteria growth and metabolites yields that have important effects on immune functions as well as the availability of many essential nutrients critical to human health, such as vitamin B12, K, etc., that are produced by gut bacteria(32,33).

Have more questions about AstraGin improving protein absorption? Simply contact us.

We’re happy to support you in the continuous improvements of your formulations.



1. AstraGin® product dossier, sections 6.4 – 6.17.
2. AstraGin® product dossier, section 6.9.
3. AstraGin® product dossier, sections 6.10.
4. AstraGin® product dossier, section 6.11 – 6.12.
5. AstraGin® product dossier, sections 6.13.
6. AstraGin® product dossier, section 6.15.
7. AstraGin® product dossier, sections 6.18.
8. AstraGin® product dossier, sections 7.4.
9. Lubert Stryer. Biochemistry, 5th edition, Chapter 3 : Protein Structure and Function. 10.Giacometti J, et al. Peptidomics as a tool for characterizing bioactive milk peptides. Food Chem. 2017;230:91-98.
11.Anthony JC, et al. Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway. J Nutr. 2000;130(10):2413-2419.
12.Bolster DR, et al. AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J Biol Chem. 2002;277(27):23977-23980.
13.Katsanos CS, et al. A high proportion of leucine is required for optimal stimulation of the rate of muscle protein synthesis by essential amino acids in the elderly. Am J Physiol Endocrinol Metab. 2006;291(2):E381-387.
14.Luiking YC, et al. Postprandial muscle protein synthesis is higher after a high whey protein, leucine-enriched supplement than after a dairy-like product in healthy older

15.Koopman R, et al. Combined ingestion of protein and free leucine with carbohydrate increases postexercise muscle protein synthesis in vivo in male subjects. Am J Physiol Endocrinol Metab. 2005;288(4):E645-653.
16.Churchward-Venne TA, et al. Leucine supplementation of a low-protein mixed macronutrient beverage enhances myofibrillar protein synthesis in young men: a double-blind, randomized trial. Am J Clin Nutr. 2014;99(2):276-286.
17.Katsanos, Christos S., et al. “Aging is associated with diminished accretion of muscle proteins after the ingestion of a small bolus of essential amino acids.” The American Journal of Clinical Nutrition 82.5 (2005): 1065-1073.
18.Castellino, P., et al. “Effect of insulin and plasma amino acid concentrations on leucine metabolism in man. Role of substrate availability on estimates of whole body protein synthesis.” Journal of Clinical Investigation 80.6 (1987):1784.

19.Carroll B., et al. Control of TSC2-Rheb signaling axis by arginine regulates mTORC1 activity. Elife. 2016;5. pii: e11058
20.Li F., et al. Ginsenoside Rg1 prevents starvation-induced muscle protein degradation via regulation of AKT/mTOR/FoxO signaling in C2C12 myotubes. Exp Ther Med. 2017; 14(2):1241-1247.
21.Lu L., et al. Astragalus polysaccharides decrease muscle wasting through Akt/mTOR, ubiquitin proteasome and autophagy signaling in 5/6 nephrectomised rats. J Ethnopharmacol. 2016;186:125-135
22.Sandro M., et al. Saturated Fatty Acid-Induced Insulin Resistance Is Associated With Mitochondrial Dysfunction in Skeletal Muscle Cells. J. Cell. Physiol. 2010; 222:187–194.
23.Egnatchik RA., et al.ER calcium release promotes mitochondrial dysfunction and hepatic cell lipotoxicity
in response to palmitate overload. Mol Metab. 2014;3(5):544-53.
24. Silveira LR., et al. Updating the effects of fatty acids on skeletal muscle. J Cell Physiol. 2008;217(1):1-12.
25.Devarshi PP., et al. Skeletal Muscle Nucleo-Mitochondrial Crosstalk in Obesity and Type 2 Diabetes.Int J Mol Sci. 2017;18(4). pii: E831. 26. Kevin G., et al. Gut Peptides in the Regulation of Food Intake and Energy Homeostasis. Endocrine Reviews, 2006; 27(7):719–727
27.Marić G., et al. The role of gut hormones in appetite regulation. Acta Physiol Hung. 2014;101(4):395-407.
28. Le N., et al. Tryptophan metabolism, from nutrition to potential therapeutic applications Amino Acids. 2011 ;41(5):1195-205.
29.Strasser B., et al. Diet Versus Exercise in Weight Loss and Maintenance: Focus on Tryptophan.Int J Tryptophan Res. 2016;9:9-16.
30.Cervenka I., et al. Kynurenines: Tryptophan’s metabolites in exercise, inflammation, and mental health Science. 2017;357(6349). pii: eaaf9794

31.Namkung J., Peripheral Serotonin: a New Player in Systemic Energy Homeostasis.Mol Cells. 2015;38(12):1023-8.

32.LIU YY., et al. The Effects of Ginsenoside on the Intestinal Microbiota of Mice. Prog. Modern Biomed. 2015;15(6):1041-5.
33.Ha CW., et al. Mechanistic links between gut microbial community dynamics, microbial functions and metabolic health. World J Gastroenterol. 2014;20(44):16498-517.

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