Abstract

Dietary protein digestion and absorption plays an important role in modulating postprandial muscle protein synthesis. The impact of co-ingesting other macronutrients with dietary protein on protein digestion and absorption and the subsequent muscle protein synthetic response remains largely unexplored. This study investigated the impact of co-ingesting milk fat with micellar casein on dietary protein-derived amino acid appearance in the circulation and the subsequent postprandial muscle protein synthetic response in healthy older men. Twenty-four healthy, older males (age: 65±1y, BMI: 25.7±0.5kg/m2) received a primed continuous infusion of L-[ring-2H5]-phenylalanine and L-[1-13C]-leucine and ingested 20g intrinsically L-[1-13C]-phenylalanine and L-[1-13C]-leucine-labeled casein with (PRO+FAT; n=12) or without (PRO; n=12) 26.7g milk fat. Plasma samples and muscle biopsies were collected in both the postabsorptive and postprandial state. Release of dietary protein-derived phenylalanine into the circulation increased following protein ingestion (P<0.001) and tended to be higher in PRO compared with PRO+FAT (Time×Treatment P=0.076). No differences were observed in dietary protein-derived plasma phenylalanine availability (52±2 vs 52±3% in PRO vs PRO+FAT, respectively; P=0.868). Myofibrillar protein synthesis rates did not differ between treatments, calculated using either the L-[ring-2H5]-phenylalanine (0.036±0.003 vs 0.036±0.004 %/h after PRO vs PRO+FAT, respectively; P=0.933) or L-[1-13C]-leucine (0.051±0.004 vs 0.046±0.004 %/h, respectively; P=0.480) tracer. In accordance, no differences were observed in myofibrillar protein-bound L-[1-13C]-phenylalanine enrichments between treatments (0.018±0.002 vs 0.014±0.001 MPE, respectively; P=0.173). Co-ingesting milk fat with micellar casein does not impair protein-derived phenylalanine appearance in the circulation and does not modulate postprandial myofibrillar protein synthesis rates. NCT01680146 (http://www.clinicaltrials.gov/).

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