Co-ingesting milk fat with micellar casein does not affect postprandial protein handling in healthy older men

Clin Nutr. 2017 Apr;36(2):429-437. doi: 10.1016/j.clnu.2015.12.011. Epub 2015 Dec 24.

Abstract

Background & aim: 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.

Methods: Twenty-four healthy, older males (age: 65 ± 1 y, BMI: 25.7 ± 0.5 kg/m2) received a primed continuous infusion of L-[ring-2H5]-phenylalanine and L-[1-13C]-leucine and ingested 20 g intrinsically L-[1-13C]-phenylalanine and L-[1-13C]-leucine-labeled casein with (PRO + FAT; n = 12) or without (PRO; n = 12) 26.7 g milk fat. Plasma samples and muscle biopsies were collected in both the postabsorptive and postprandial state.

Results: 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).

Conclusion: 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.

Clinical trial registration number: NCT01680146 (http://www.clinicaltrials.gov/).

Keywords: Casein; Fat; Leucine; Muscle protein synthesis; Sarcopenia.

Publication types

  • Randomized Controlled Trial

MeSH terms

  • Aged
  • Animals
  • Blood Glucose / metabolism
  • Body Mass Index
  • Caseins / administration & dosage*
  • Caseins / pharmacokinetics
  • Diet
  • Dietary Proteins / administration & dosage
  • Dietary Proteins / pharmacokinetics
  • Exercise
  • Glycolipids / administration & dosage*
  • Glycolipids / pharmacokinetics
  • Glycoproteins / administration & dosage*
  • Glycoproteins / pharmacokinetics
  • Humans
  • Leucine / blood
  • Lipid Droplets
  • Male
  • Micelles
  • Middle Aged
  • Milk / chemistry
  • Muscle Proteins / biosynthesis
  • Muscle, Skeletal / metabolism
  • Phenylalanine / blood
  • Postprandial Period*
  • Protein Biosynthesis

Substances

  • Blood Glucose
  • Caseins
  • Dietary Proteins
  • Glycolipids
  • Glycoproteins
  • Micelles
  • Muscle Proteins
  • milk fat globule
  • Phenylalanine
  • Leucine

Associated data

  • ClinicalTrials.gov/NCT01680146