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Background Probiotic Bacillus coagulans GBI-30, 6086 (BC30) has been shown to increase protein digestion in an in vitro model of the stomach and small intestine. Once active in the small intestine after germination, BC30 aids the digestion of carbohydrates and proteins. The extent to which BC30 administration may impact protein digestion and amino acid appearance in humans after protein ingestion is currently unknown. This study examined the impact of adding BC30 to a 25-g dose of milk protein concentrate on post-prandial changes in blood amino acids concentrations. Methods 14 males and 16 females (n = 30, 26.4 ± 6.5 years; 172.3 ± 10.8 cm; 78.2 ± 14.8 kg; 22.6 ± 7.2% fat) completed two supplementation protocols that each spanned two weeks separated by a washout period that lasted three weeks. Participants were instructed to track their dietary intake and ingest a daily 25-g dose of milk protein concentrate with (MPCBC30) or without (MPC) the addition of BC30. Body composition and demographics were assessed upon arrival to the laboratory. Upon ingestion of their final assigned supplemental dose, blood samples were taken at 0 (baseline), 30, 60, 90, 120, 180, and 240 min post-consumption and analyzed for amino acid concentrations. Results Arginine (p = 0.03) and Isoleucine (p = 0.05) revealed greater area-under-the curve (AUC) in MPCBC30 group compared to MPC. In addition, Arginine (p = 0.02), Serine (p = 0.01), Ornithine (p = 0.02), Methionine (p = 0.04), Glutamic Acid (p = 0.01), Phenylalanine (p = 0.05), Isoleucine (p = 0.04), Tyrosine (p = 0.02), Essential Amino Acids (p = 0.02), and Total Amino Acids (p Max) in MPCBC30 compared to MPC. Finally, time to reach CMax (TMax) was significantly faster for Glutamine (p p p = 0.04), Alanine (p = 0.02) in MPCBC30 when compared to MPC. Greater mean differences between groups for AUC and CMax in women when compared to the mean differences in men were found for several amino acids. Conclusion In concert with previous in vitro evidence of improved protein digestion and amino acid appearance, these results reveal that adding BC30 to protein sources such as milk protein concentrate can improve AUC, CMax, and faster TMax. Follow-up research should examine differences between gender and explore how aging can impact these outcomes. Retrospectively registered on June 11, 2020 at ClinicalTrials.gov as NCT04427020.

Introduction: The lipid messenger phosphatidic acid (PA) plays a critical role in the stimulation of mTOR signaling. However, the mechanism by which PA stimulates mTOR is currently unknown. Therefore, the purpose of this study was to compare the effects of various PA precursors and phospholipids on their ability to stimulate mTOR signaling and its ability to augment resistance training-induced changes in body composition and performance. Methods: In phase one, C2C12 myoblasts cells were stimulated with different phospholipids and phospholipid precursors derived from soy and egg sources. The ratio of phosphorylated p70 (P-p70-389) to total p70 was then used as readout for mTOR signaling. In phase two, resistance trained subjects (n = 28, 21 ± 3 years, 77 ± 4 kg, 176 ± 9 cm) consumed either 750 mg PA daily or placebo and each took part in an 8 week periodized resistance training program. Results: In phase one, soy-phosphatidylserine, soy-Lyso-PA, egg-PA, and soy-PA stimulated mTOR signaling, and the effects of soy-PA (+636%) were significantly greater than egg-PA (+221%). In phase two, PA significantly increased lean body mass (+2.4 kg), cross sectional area (+1.0 cm), and leg press strength (+51.9 kg) over placebo. Conclusion: PA significantly activates mTOR and significantly improved responses in skeletal muscle hypertrophy, lean body mass, and maximal strength to resistance exercise.

Background Co-ingesting creatine (5 g) with large amounts of glucose (e.g., 95 g) has been shown to enhance creatine and carbohydrate storage in muscle. It has been speculated that creatine transport is mediated in part by glucose and insulin. The increases in creatine retention are accompanied by an undesired caloric load and as a result, additional research has been undertaken to assess the effect of co-ingesting creatine with nutrients that may enhance insulin sensitivity. Co-ingestion of creatine (Cr) with an antihyperglycemic extract of Artemisia dracunculus (Russian tarragon (RT)), has been shown to influence plasma Cr levels comparable to co-ingestion of Cr and glucose [1]. However, other research has shown that short term (5 days) co-ingestion of Cr and RT (Cr+RT) did not enhance whole body creatine retention or muscle free creatine content [2]. The purpose of this on-going investigation was to compare the long-term effects of resistance training in combination wit he ither Cr+RT, or Cr with carbohydrate (Cr+CHO), or carbohydrate (PL) ingestion. Methods

Background The mammalian target of rapamycin (mTOR) has been shown to regulate rates of muscle protein synthesis, and one novel nutritional activator of mTOR is the phospholipid Phosphatidic Acid (PA). We have recently found that PA supplementation over 8 weeks of resistance training augmented responses in skeletal muscle hypertrophy and strength. However, we are unaware of research investigating the safety of PA in human subjects. Therefore the purpose of this study was to investigate the effects of 8 weeks of 750 mg per day of PA supplementation on safety parameters in healthy college aged males.

Background A protein kinase called the mechanistic target of rapamycin (mTOR) is a well-known regulator of cellular growth. In fact, several studies have indicated that the kinase activity of mTOR is required for mechanicallyinduced increases in skeletal muscle protein synthesis and hypertrophy. Previous studies have also determined that the lipid messenger phosphatidic acid (PA) plays a critical role in the stimulation of mTOR signaling and, an increase in PA concentration is sufficient for the activation of mTOR signaling. However, the mechanism by which PA stimulates mTOR is currently unknown. A primary target of mTOR includes the phosphorylation of p70 on the threonine 389 residue (P-p70-389), and thus, is a commonly accepted readout for the activation of mTOR. PA can be synthesized from a variety of reactions via multiple reactants. Therefore, the purpose of this study was to compare the effects of various PA precursors on their ability to stimulate mTOR signaling and determine if any other phospholipid species are also capable of stimulating mTOR signaling. Methods C2C12 myoblasts were plated at approximately 30% confluence and grown for 24 hours in 10% FBS High Glucose DMEM. Cells were switched to 2mL/well serum free high glucose DMEM (no antibiotics) for 16 hours prior to the experiment. Cells were approximately 70% confluent at the time of the experiment. Cells were then stimulated for 20 minutes with vehicle (Control) or 10, 30 or 100µM of soy-derived phosphatidylserine (S-PS, SerinAid, Chemi Nutra, White Bear Lake, MN), phosphatidylinositol (S-PI), phosphatidylethanolamine (S-PE), phosphatidylcholine (S-PC), PA (S-PA, Mediator, Chemi Nutra, White Bear Lake, MN), lysophosphatidic acid (S-LPA), diacylglycerol (DAG), glycerol3-phosphate (G3P), and egg-derived PA (E-PA). Cells were harvested in lysis buffer and subjected to immunoblotting. The ratio of P-p70-389 to total p70 was used as readout for mTOR signaling. Results S-PI, S-PE, S-PC, DAG, and G3P elicited no increase in the ratio of P-p70-389 to total p70 compared to vehicle stimulated cells. In contrast, elevated mTOR signaling was observed at all tested concentrations of S-PS (529, 588, and 457%), S-LPA (649, 866, and 1,132%), and S-PA (679, 746, and 957%; P

Position Statement The following seven points related to the intake of protein for healthy, exercising individuals constitute the position stand of the Society. They have been approved by the Research Committee of the Society. 1) Vast research supports the contention that individuals engaged in regular exercise training require more dietary protein than sedentary individuals. 2) Protein intakes of 1.4 – 2.0 g/kg/day for physically active individuals is not only safe, but may improve the training adaptations to exercise training. 3) When part of a balanced, nutrient-dense diet, protein intakes at this level are not detrimental to kidney function or bone metabolism in healthy, active persons. 4) While it is possible for physically active individuals to obtain their daily protein requirements through a varied, regular diet, supplemental protein in various forms are a practical way of ensuring adequate and quality protein intake for athletes. 5) Different types and quality of protein can affect amino acid bioavailability following protein supplementation. The superiority of one protein type over another in terms of optimizing recovery and/or training adaptations remains to be convincingly demonstrated. 6) Appropriately timed protein intake is an important component of an overall exercise training program, essential for proper recovery, immune function, and the growth and maintenance of lean body mass. 7) Under certain circumstances, specific amino acid supplements, such as branched-chain amino acids (BCAA's), may improve exercise performance and recovery from exercise.