Rationale Dietary protein may attenuate the muscle atrophy experienced by patients in the Intensive Care Unit (ICU), yet protein handling is poorly understood. Objective To quantify protein digestion and amino acid absorption, and fasting and postprandial myofibrillar protein synthesis during critical illness. Methods Fifteen mechanically ventilated adults (12M; age 50±17y, Body Mass Index (BMI) 27±5kg·m-2) and 10 healthy controls (6M; 54±23y, BMI 27±4kg·m-2) received a primed intravenous L-[ring-2H5]-phenylalanine, L-[3,5-2H2]-tyrosine, and L-[1-13C]-leucine infusion over 9.5h, and a duodenal bolus of intrinsically-labelled (L-[1-13C]-phenylalanine and L-[1-13C]-leucine) intact milk protein (20g protein) over 60min. Arterial blood and muscle samples were taken at baseline (fasting) and for 6h following duodenal protein administration. Data are mean±SD; analysed with 2-way repeated measures ANOVA and independent samples t-test. Measurements and main results Fasting myofibrillar protein synthesis rates did not differ between ICU patients and healthy controls (0.023±0.013 vs 0.034±0.016%/h; P=0.077). Following protein administration, plasma amino acid availability did not differ between groups (ICU patients 54.2±9.1 vs healthy controls 61.8±13.1%; P=0.12), and myofibrillar protein synthesis rates increased in both groups (0.028±0.010 vs 0.043±0.018 %/h, main time effect P=0.046, P-interaction=0.584) with lower rates in ICU patients compared to healthy controls (main group effect P=0.001). Incorporation of protein-derived phenylalanine into myofibrillar protein was ~60% lower in ICU patients (0.007±0.007 vs 0.017±0.009 mole % excess (MPE); P=0.007). Conclusion The capacity for critically ill patients to use ingested protein for muscle protein synthesis is markedly blunted despite relatively normal protein digestion and amino acid absorption.
|Journal||American Journal of Respiratory and Critical Care Medicine|
|Early online date||18 May 2022|
|Publication status||Published - 18 May 2022|