Francis B Stephens's Lab
Featured research (2)
To mitigate the age-related decline in skeletal muscle quantity and quality, and the associated negative health outcomes, it has been proposed that dietary protein recommendations for older adults should be increased alongside an active lifestyle and/or structured exercise training. Concomitantly, there are growing environmental concerns associated with the production of animal-based dietary protein sources. The question therefore arises as to where this dietary protein required for meeting the protein demands of the rapidly aging global population should (or could) be obtained. Various non-animal–derived protein sources possess favorable sustainability credentials, though much less is known (compared with animal-derived proteins) about their ability to influence muscle anabolism. It is also likely that the anabolic potential of various alternative protein sources varies markedly, with the majority of options remaining to be investigated. The purpose of this review was to thoroughly assess the current evidence base for the utility of alternative protein sources (plants, fungi, insects, algae, and lab-grown “meat”) to support muscle anabolism in (active) older adults. The solid existing data portfolio requires considerable expansion to encompass the strategic evaluation of the various types of dietary protein sources. Such data will ultimately be necessary to support desirable alterations and refinements in nutritional guidelines to support healthy and active aging, while concomitantly securing a sustainable food future.
Background: Mycoprotein is a fungal-derived sustainable protein-rich food source, and its ingestion results in systemic amino acid and leucine concentrations similar to that following milk protein ingestion. Objective: We assessed the mixed skeletal muscle protein synthetic response to the ingestion of a single bolus of mycoprotein compared with a leucine-matched bolus of milk protein, in rested and exercised muscle of resistance-trained young men. Methods: Twenty resistance-trained healthy young males (age: 22 ± 1 y, body mass: 82 ± 2 kg, BMI: 25 ± 1 kg·m-2) took part in a randomized, double-blind, parallel-group study. Participants received primed, continuous infusions of L-[ring-2H5]phenylalanine and ingested either 31 g (26.2 g protein: 2.5 g leucine) milk protein (MILK) or 70 g (31.5 g protein: 2.5 g leucine) mycoprotein (MYCO) following a bout of unilateral resistance-type exercise (contralateral leg acting as resting control). Blood and m. vastus lateralis muscle samples were collected before exercise and protein ingestion, and following a 4-h postprandial period to assess mixed muscle fractional protein synthetic rates (FSRs) and myocellular signaling in response to the protein beverages in resting and exercised muscle. Results: Mixed muscle FSRs increased following MILK ingestion (from 0.036 ± 0.008 to 0.052 ± 0.006%·h-1 in rested, and 0.035 ± 0.008 to 0.056 ± 0.005%·h-1 in exercised muscle; P <0.01) but to a greater extent following MYCO ingestion (from 0.025 ± 0.006 to 0.057 ± 0.004%·h-1 in rested, and 0.024 ± 0.007 to 0.072 ± 0.005%·h-1 in exercised muscle; P <0.0001) (treatment × time interaction effect; P <0.05). Postprandial FSRs trended to be greater in MYCO compared with MILK (0.065 ± 0.004 compared with 0.054 ± 0.004%·h-1, respectively; P = 0.093) and the postprandial rise in FSRs was greater in MYCO compared with MILK (Delta 0.040 ± 0.006 compared with Delta 0.018 ± 0.005%·h-1, respectively; P <0.01). Conclusions: The ingestion of a single bolus of mycoprotein stimulates resting and postexercise muscle protein synthesis rates, and to a greater extent than a leucine-matched bolus of milk protein, in resistance-trained young men. This trial was registered at clinicaltrials.gov as 660065600.