Boirie‌, Yves

It has been shown ingestion of whey protein (WP) results in rapid systemic appearance rates of amino acids (AA) but in higher amino acid (AA) oxidation and whole body protein synthesis than in with casein (cas) ingestion which inhibits protein breakdown. To determine whether combined ingestion of both cas and WP in a meal containing carbohydrate has any disparate effects on protein economy in splanchnic and muscle beds we studied 12 healthy volunteers who ingested intrinsically labeled WP and Cas protein fractions. Following ingestion of 0.625 g·kg FFM −1 each of [ 15 N]WP and [ 13 C]Cas and 0.9 g·kg FFM −1 of lactose; or 0.625 g·kg FFM −1 each of [ 13 C]WP and [ 15 N]CAS and 0.9 g·kg FFM −1 of lactose blood samples were collected from femoral artery and vein and hepatic vein at frequent intervals. At 80–120 min, the rate of appearance (PheRa) of Phe at hepatic vein from WP and Cas were similar (5.5 (0.9) vs 5.2 (0.7) μmol, min −1 , but at 220–260 min, PheRa from WP was slower than PheRa from Cas (2.4 (0.5) vs 5.3 (1.2) μmol, min −1 , P<0.05). Retention rates of Phe in muscle (PheRd) absorbed from WP and Cas were similar at 80–120 min (0.8 (0.1) vs 0.9 (0.2) μmol, min −1 , ns) but was significantly lower for WP than Cas at 220–260 min (0.5 (0.1) vs 1.1 (0.3) μmol, min −1 , P<0.05). In conclusion Cas has more sustained systemic effects and muscle protein accretion than WP. The different metabolic effects of co‐ingested protein fractions have potential implications in designing appropriate nutritional support.

When consumed separately, whey protein (WP) is more rapidly absorbed into circulation than casein (Cas), which prompted the concept of rapid and slow dietary protein. It is unclear whether these proteins have similar metabolic fates when coingested as in milk. We determined the rate of appearance across the splanchnic bed and the rate of disappearance across the leg of phenylalanine (Phe) from coingested, intrinsically labeled WP and Cas. Either [15N]Phe or [13C- ring C6]Phe was infused in lactating cows, and the labeled WP and Cas from their milk were collected. To determine the fate of Phe derived from different protein sources, 18 healthy participants were studied after ingestion of one of the following: 1) [15N]WP, [13C]Cas, and lactose; 2) [13C]WP, [15N]Cas, and lactose; 3) lactose alone. At 80–120 min, the rates of appearance (Ra) across the splanchnic bed of Phe from WP and Cas were similar [0.068 ± 0.010 vs. 0.070 ± 0.009%/min; not significant (ns)]. At time 220–260 min, Phe appearance from WP had slowed (0.039 ± 0.008%/min, P < 0.05) whereas Phe appearance from Cas was sustained (0.068 ± 0.013%/min). Similarly, accretion rates across the leg of Phe absorbed from WP and Cas were not different at 80–120 min (0.011 ± 0.002 vs. 0.012 ± 0.003%/min; ns), but they were significantly lower for WP (0.007 ± 0.002%/min) at 220–260 min than for Cas (0.013 ± 0.002%/min) at 220–260 min. Early after meal ingestion, amino acid absorption and retention across the leg were similar for WP and Cas, but as rates for WP waned, absorption and assimilation into skeletal muscle were better retained for Cas.

In vivo studies have reported conflicting effects of insulin on mixed tissue protein synthesis rates. To test the hypothesis that insulin has differential effects on synthesis rates of various protein fractions in different organs, we infused miniature swine (n = 8 per group) with saline, insulin alone (at 0.7 mU/kg−1 · min−1), or insulin plus an amino acid mixture for 8 h. Fractional synthesis rate (FSR) of mitochondrial and cytoplasmic proteins in liver, heart, and skeletal muscle, as well as myosin heavy chain (MHC) in muscle, were measured using l-[1-13C]leucine as a tracer. The FSR of mitochondrial and cytoplasmic proteins were highest in liver, followed by heart and then muscle. Mitochondrial FSR in muscle was higher during insulin and insulin plus amino acid infusions than during saline. Insulin had no significant effect on FSR of MHC in muscle. In contrast, FSR of both mitochondrial and cytoplasmic proteins were not stimulated by insulin in liver. Insulin also did not increase FSR of mitochondrial in heart, whereas insulin and amino acid stimulated FSR of cytoplasmic protein. In conclusion, insulin stimulates the synthesis of muscle mitochondrial proteins, with no significant stimulatory effect on synthesis of sarcoplasmic and MHC. These results demonstrate that insulin has different effects on synthesis rates of specific protein fractions in the liver, heart, and skeletal muscle.