Egg White Protein Promotes Developmental Growth in Rodent Muscle Independently of Leucine Content.

BACKGROUND: Leucine has unique anabolic properties, serving as a nutrient signal that stimulates muscle protein synthesis. OBJECTIVE: We tested whether the leucine concentration is the only factor determining protein quality for muscle development. METHODS: We selected 3 dietary proteins: casein (CAS), egg white protein (EWP), and albumin (ALB), representing the leucine concentrations of ∼8.3%, 7.7%, and 6.7% of the total protein (wt:wt), respectively. In the chronic feeding experiment, these proteins were pair-fed to growing male Wistar rats [110-135 g body weight (BW)] for 14 d as a protein source, providing 10% of total energy intake, after which soleus and extensor digitorum longus (EDL) muscles were used to estimate muscle growth. In the acute administration experiment, we injected CAS, ALB, and EWP to rats by oral gavage (0.3 g protein/100 g BW), and after 1 or 3 h EDL muscle was excised for capillary electrophoresis-MS-based metabolomics. In another chronic feeding experiment, rats were pair-fed either CAS or a CAS diet supplemented with arginine to the same level as in the EWP diet for 14 d. RESULTS: At the end of the 14-d feeding, soleus and EDL muscle weight was 20% and 17% higher, respectively, when rats were fed EWP as compared with CAS (P < 0.05). In addition, the 14-d EWP diet increased the expression of p70S6K by 117% compared with CAS (P < 0.05). These results suggest the possibility that some amino acids (excluding leucine), derived from EWP, promote muscle growth. Metabolomics analysis showed that muscle arginine concentration, following acute protein administration, appeared to match muscle growth over the 14-d feeding period. In addition, 14-d arginine supplementation to a CAS diet increased EDL muscle weight by 15% when compared with the plain CAS diet (P < 0.05). CONCLUSIONS: EWP promotes rat developmental muscle growth compared with CAS, which can be partly explained by the arginine-rich EWP.

Effects of Dietary Vitamin D Deficiency on Markers of Skeletal Muscle Mitochondrial Biogenesis and Dynamics.

We examined the effects of dietary vitamin D deficiency on markers of mitochondrial biogenesis and dynamics in rat soleus muscle. Male Wistar rats were fed a chow with no vitamin D (No-D; 0 IU/kg) or a moderate dose (Mod-D; 2,000 IU/kg) of vitamin D chow for 8 wk. Compared to the Mod-D group, at 8 wk the No-D group showed significantly lower serum 25(OH)D levels. Although vitamin D deficiency had no effect on body composition, the No-D rats showed significantly decreased levels of PGC-1α, a marker of skeletal muscle mitochondrial biogenesis, and DRP1, a marker of skeletal muscle mitochondrial fission. The change in the PGC-1α protein expression and the serum 25(OH)D concentrations were significantly correlated. The change in DRP1 protein expression and the serum 25(OH)D concentrations tended to be correlated. There was no significant between-group difference in markers of mitochondrial fusion (MFN2 and OPA1) and mitophagy (PARKIN) in soleus muscle, and no relationship with serum 25(OH)D concentrations. Collectively our findings suggest that dietary vitamin D deficiency decreased PGC-1α and DRP1 protein expression in rat soleus muscle.

Acute bout of exercise downregulates thioredoxin-interacting protein expression in rat contracting skeletal muscles.

We previously reported that in rat skeletal muscle, disuse (i.e., decreased muscle contractile activity) rapidly increases thioredoxin-interacting protein (TXNIP), which is implicated in the reduced glucose uptake. Accordingly, we sought herein to (a) determine the effect of exercise (i.e., increased muscle contractile activity) on muscle TXNIP protein expression, and (b) elucidate the mechanisms underlying the changes of TXNIP protein expression in response to exercise. Rat epitrochlearis and soleus muscles were dissected out after an acute bout of 3-hr swimming (without weight loading) or 3-hr treadmill running (15% grade at 9m/min). In a separate protocol, the isolated epitrochlearis and soleus muscles were incubated for 3 hr with AMP-dependent protein kinase activator AICAR. Immediately after the cessation of the 3-hr swimming, the TXNIP protein was decreased in epitrochlearis but not in soleus muscle. Conversely, 3-hr treadmill running decreased the TXNIP protein in soleus but not in epitrochlearis muscle. TXNIP protein was decreased concomitantly with reduced postexercise muscle glycogen, showing that a decrease in TXNIP protein expression occurs in muscles that are recruited during exercise. In addition, 3-hr incubation with AICAR decreased TXNIP protein in both isolated epitrochlearis and soleus muscles. Our results suggest that (a) an acute bout of exercise downregulates TXNIP protein expression in rat contracting skeletal muscles, and (b) the reduction in TXNIP protein expression in contracting muscles is probably mediated by AMPK activation, at least in part.