Reply to LTE: Does caffeine truly raise muscle carnitine in humans?

This is the final version. Available from Wiley via the DOI in this record. University of Exete

Mycoprotein represents a bioavailable and insulinotropic non-animal-derived dietary protein source: a dose-response study

This is the final version of the article. Available from CUP via the DOI in this record.The anabolic potential of a dietary protein is determined by its ability to elicit postprandial rises in circulating essential amino acids and insulin. Minimal data exist regarding the bioavailability and insulinotropic effects of non-animal-derived protein sources. Mycoprotein is a sustainable and rich source of non-animal-derived dietary protein. We investigated the impact of mycoprotein ingestion, in a dose-response manner, on acute postprandial hyperaminoacidaemia and hyperinsulinaemia. In all, twelve healthy young men completed five experimental trials in a randomised, single-blind, cross-over design. During each trial, volunteers consumed a test drink containing either 20 g milk protein (MLK20) or a mass matched (not protein matched due to the fibre content) bolus of mycoprotein (20 g; MYC20), a protein matched bolus of mycoprotein (40 g; MYC40), 60 g (MYC60) or 80 g (MYC80) mycoprotein. Circulating amino acid, insulin and uric acid concentrations, and clinical chemistry profiles, were assessed in arterialised venous blood samples during a 4-h postprandial period. Mycoprotein ingestion resulted in slower but more sustained hyperinsulinaemia and hyperaminoacidaemia compared with milk when protein matched, with overall bioavailability equivalent between conditions (P>0·05). Increasing the dose of mycoprotein amplified these effects, with some evidence of a plateau at 60-80 g. Peak postprandial leucine concentrations were 201 (sem 24) (30 min), 118 (sem 10) (90 min), 150 (sem 14) (90 min), 173 (sem 23) (45 min) and 201 (sem 21 (90 min) µmol/l for MLK20, MYC20, MYC40, MYC60 and MYC80, respectively. Mycoprotein represents a bioavailable and insulinotropic dietary protein source. Consequently, mycoprotein may be a useful source of dietary protein to stimulate muscle protein synthesis rates.The project was sponsored by Marlow Foods Ltd (B. T. W. as grant holder). The University of Exeter (B. T. W.) were responsible for the study design, data collection and analysis, decision to publish and preparation of the manuscript. The private partners have contributed to the project through regular discussion. M. V. D. is supported through the aforementioned grant, S. P. K. is supported from an internal studentship grant in collaboration with Maastricht University

Editorial: Sarcopenic Obesity: Mechanisms and Countermeasures

This is the final version. Available on open access from Frontiers Media via the DOI in this recordNational Institute of Agin

Rebuttal from Marlou L. Dirks, Benjamin T. Wall and Francis B. Stephens

This is the final version. Available on open access from Wiley via the DOI in this recordThis article is part of a CrossTalk debate. Click the links to read the other articles in this debate: https://doi.org/10.1113/JP278219, https://doi.org/10.1113/JP279714, https://doi.org/10.1113/JP27822

Neuromuscular electrical stimulation prevents muscle disuse atrophy during leg immobilization in humans

This is the author accepted manuscript. The final version is available from Wiley via the DOI in this recordAIM: Short periods of muscle disuse, due to illness or injury, result in substantial skeletal muscle atrophy. Recently, we have shown that a single session of neuromuscular electrical stimulation (NMES) increases muscle protein synthesis rates. The aim was to investigate the capacity for daily NMES to attenuate muscle atrophy during short-term muscle disuse. METHODS: Twenty-four healthy, young (23 ± 1 year) males participated in the present study. Volunteers were subjected to 5 days of one-legged knee immobilization with (NMES; n = 12) or without (CON; n = 12) supervised NMES sessions (40-min sessions, twice daily). Two days prior to and immediately after the immobilization period, CT scans and single-leg one-repetition maximum (1RM) strength tests were performed to assess quadriceps muscle cross-sectional area (CSA) and leg muscle strength respectively. Furthermore, muscle biopsies were taken to assess muscle fibre CSA, satellite cell content and mRNA and protein expression of selected genes. RESULTS: In CON, immobilization reduced quadriceps CSA by 3.5 ± 0.5% (P < 0.0001) and muscle strength by 9 ± 2% (P < 0.05). In contrast, no significant muscle loss was detected following immobilization in NMES although strength declined by 7 ± 3% (P < 0.05). Muscle MAFbx and MuRF1 mRNA expression increased following immobilization in CON (P < 0.001 and P = 0.07 respectively), whereas levels either declined (P < 0.01) or did not change in NMES, respectively. Immobilization led to an increase in muscle myostatin mRNA expression in CON (P < 0.05), but remained unchanged in NMES. CONCLUSION: During short-term disuse, NMES represents an effective interventional strategy to prevent the loss of muscle mass, but it does not allow preservation of muscle strength. NMES during disuse may be of important clinical relevance in both health and disease

Skeletal muscle disuse atrophy is not attenuated by dietary protein supplementation in healthy older men

This is the author accepted manuscript. The final version is available from OUP via the DOI in this recordShort successive periods of muscle disuse, due to injury or illness, can contribute significantly to the loss of muscle mass with aging (sarcopenia). It has been suggested that increasing the protein content of the diet may be an effective dietary strategy to attenuate muscle disuse atrophy. We hypothesized that protein supplementation twice daily would preserve muscle mass during a short period of limb immobilization. Twenty-three healthy older (69 ± 1 y) men were subjected to 5 d of one-legged knee immobilization by means of a full-leg cast with (PRO group; n = 11) or without (CON group; n = 12) administration of a dietary protein supplement (20.7 g of protein, 9.3 g of carbohydrate, and 3.0 g of fat) twice daily. Two d prior to and immediately after the immobilization period, single-slice computed tomography scans of the quadriceps and single-leg 1 repetition maximum strength tests were performed to assess muscle cross-sectional area (CSA) and leg muscle strength, respectively. Additionally, muscle biopsies were collected to assess muscle fiber characteristics as well as mRNA and protein expression of selected genes. Immobilization decreased quadriceps' CSAs by 1.5 ± 0.7% (P < 0.05) and 2.0 ± 0.6% (P < 0.05), and muscle strength by 8.3 ± 3.3% (P < 0.05) and 9.3 ± 1.6% (P < 0.05) in the CON and PRO groups, respectively, without differences between groups. Skeletal muscle myostatin, myogenin, and muscle RING-finger protein-1 (MuRF1) mRNA expression increased following immobilization in both groups (P < 0.05), whereas muscle atrophy F-box/atrogen-1 (MAFBx) mRNA expression increased in the PRO group only (P < 0.05). In conclusion, dietary protein supplementation (∼20 g twice daily) does not attenuate muscle loss during short-term muscle disuse in healthy older men. This trial was registered at clinicaltrials.gov as NCT01588808

Aging Is Accompanied by a Blunted Muscle Protein Synthetic Response to Protein Ingestion.

Published onlineJournal ArticleThis is the final version of the article. Available from Public Library of Science via the DOI in this record.PURPOSE: Progressive loss of skeletal muscle mass with aging (sarcopenia) forms a global health concern. It has been suggested that an impaired capacity to increase muscle protein synthesis rates in response to protein intake is a key contributor to sarcopenia. We assessed whether differences in post-absorptive and/or post-prandial muscle protein synthesis rates exist between large cohorts of healthy young and older men. PROCEDURES: We performed a cross-sectional, retrospective study comparing in vivo post-absorptive muscle protein synthesis rates determined with stable isotope methodologies between 34 healthy young (22±1 y) and 72 older (75±1 y) men, and post-prandial muscle protein synthesis rates between 35 healthy young (22±1 y) and 40 older (74±1 y) men. FINDINGS: Post-absorptive muscle protein synthesis rates did not differ significantly between the young and older group. Post-prandial muscle protein synthesis rates were 16% lower in the older subjects when compared with the young. Muscle protein synthesis rates were >3 fold more responsive to dietary protein ingestion in the young. Irrespective of age, there was a strong negative correlation between post-absorptive muscle protein synthesis rates and the increase in muscle protein synthesis rate following protein ingestion. CONCLUSIONS: Aging is associated with the development of muscle anabolic inflexibility which represents a key physiological mechanism underpinning sarcopenia

Low Handgrip Strength Is Not Associated with Type 2 Diabetes Mellitus and Hyperglycemia: a Population-Based Study.

This is the final version. Available from The Korean Society of Clinical Nutrition via the DOI in this record. Type 2 diabetes mellitus (DM) is commonly linked to muscle weakness and metabolic abnormalities which increase healthcare costs. The study was undertaken to investigate if low handgrip strength, as a marker of muscle weakness, is associated with hyperglycemia and/or DM in Brazilian subjects. In a cross-sectional design, 415 individuals of both sexes (46.7% male) were interviewed by a questionnaire and the DM diagnostic was self-reported. Anthropometric measurements, such as weight, height, body mass index (BMI), arm circumference, mid-arm and calf circumference and handgrip strength, were obtained by trained nutritionists. Blood glucose concentrations were determined by portable monitor analysis. Student's t-test was applied to compare DM cases with non-diabetic individuals, and logistic regression analysis was performed to verify the odds for becoming diabetic or having altered glycemia and p < 0.05 was considered as significant. From 415 subjects, 9.2% (n = 35) were classified as DM. DM patients had significantly higher age, BMI, casual glycemia and lower handgrip strength and normalized (to body weight) handgrip strength (NHS) when compared with non-diabetic patients. Individuals with low NHS have 2.7 odds ratio to DM without adjustment for covariate (crude model, p = 0.006) and have 2.7 times higher the likelihood of DM than individuals with high NHS after adjusting for age (model 1, p = 0.006); however, this association disappeared after further adjusting for sex. In conclusion, low handgrip strength normalized or not to body weight, was not associated with hyperglycemia and DM diagnosis.Cape

Food for our future: the nutritional science behind the sustainable fungal protein - mycoprotein. A symposium review.

This is the final version. Available from Cambridge University Press via the DOI in this record. Mycoprotein is a well-established and sustainably produced, protein-rich, high-fibre, whole food source derived from the fermentation of fungus. The present publication is based on a symposium held during the Nutrition Society Summer Conference 2022 in Sheffield that explored 'Food for our Future: The Science Behind Sustainable Fungal Proteins'. A growing body of science links mycoprotein consumption with muscle/myofibrillar protein synthesis and improved cardiometabolic (principally lipid) markers. As described at this event, given the accumulating health and sustainability credentials of mycoprotein, there is great scope for fungal-derived mycoprotein to sit more prominently within future, updated food-based dietary guidelines.Marlow Foods Ltd

A Parallel Elastic Haptic Thimble for Wide Bandwidth Cutaneous Feedback.

Design of wearable fingertip haptic devices is often a compromise between conflicting features: lightness and compactness, against rich and neat haptic feedback. On one side direct drive actuators (i.e. voice coils) provide a clean haptic feedback with high dynamics, with limited maximum output forces. On the other side mechanical transmissions with reduction can increase output force of micro sized motors, at the cost of slower and often noisy output signals. In this work we present a compact fingertip haptic device based on a parallel elastic mechanism: it merges the output of two differently designed actuators in a single, wide bandwidth haptic feedback. Each actuator is designed with a different role: one for rendering fast, high frequency force components, the other for rendering constant to low frequency components. In the work we present design and implementation of the device, followed by experimental characterization of its performance in terms of frequency response and rendering capabilities