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      Effects of Pre-Sleep Whey vs. Plant-Based Protein Consumption on Muscle Recovery Following Damaging Morning Exercise

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          Abstract

          Pre-sleep whey protein intake has been shown to improve overnight muscle protein synthesis, muscle size and strength, and muscle recovery. Despite a growing interest in alternative protein sources, such as plant-based protein, there is no evidence regarding the efficacy of plant-based proteins consumed pre-sleep. Therefore, we aimed to compare whey vs. plant-based pre-sleep protein dietary supplementation on muscle recovery in middle-aged men. Twenty-seven recreationally active, middle-aged men performed 5 sets of 15 repetitions of maximal eccentric voluntary contractions (ECC) for the knee extensors (ext) and flexors (flex), respectively, in the morning. Participants consumed 40 g of either whey hydrolysate (WH, n = 9), whey isolate (WI, n = 6), rice and pea combination (RP, n = 6), or placebo (PL, n = 6) 30 min pre-sleep on the day of ECC and the following two nights. Catered meals (15% PRO, 55% CHO, 30% Fat) were provided to participants for 5 days to standardize nutrition. Plasma creatine kinase (CK), interleukin-6 (IL-6), and interleukin-10 (IL-10) were measured at pre, immediately post (+0), +4, +6, +24, +48, and +72 h post-ECC. Isometric (ISOM) and isokinetic (ISOK) maximal voluntary contraction force were measured at pre, immediately post (+0), +24, +48, and +72 h post-ECC. Muscle soreness, thigh circumference, and HOMA-IR were measured at pre, +24, +48, and +72 h post-ECC. CK was increased at +4 h post-ECC, remained elevated at all time points compared to baseline ( p < 0.001), and was significantly greater at +72 h compared to all other time points ( p < 0.001). IL-6 was increased at +6 h ( p = 0.002) with no other time differing from baseline. ISOMext was reduced after ECC ( p = 0.001) and remained reduced until returning to baseline at +72 h. ISOMflex, ISOKext, and ISOKflex were reduced after ECC and remained reduced at +72 h ( p < 0.001). Muscle soreness increased post-ECC ( p < 0.001) and did not return to baseline. Thigh circumference ( p = 0.456) and HOMA-IR ( p = 0.396) did not change post-ECC. There were no significant differences between groups for any outcome measure. These data suggest that middle-aged men consuming 1.08 ± 0.02 g/kg/day PRO did not recover from damaging eccentric exercise at +72 h and that pre-sleep protein ingestion, regardless of protein source, did not aid in muscle recovery when damaging eccentric exercise was performed in the morning.

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          Protein content and amino acid composition of commercially available plant-based protein isolates

          The postprandial rise in essential amino acid (EAA) concentrations modulates the increase in muscle protein synthesis rates after protein ingestion. The EAA content and AA composition of the dietary protein source contribute to the differential muscle protein synthetic response to the ingestion of different proteins. Lower EAA contents and specific lack of sufficient leucine, lysine, and/or methionine may be responsible for the lower anabolic capacity of plant-based compared with animal-based proteins. We compared EAA contents and AA composition of a large selection of plant-based protein sources with animal-based proteins and human skeletal muscle protein. AA composition of oat, lupin, wheat, hemp, microalgae, soy, brown rice, pea, corn, potato, milk, whey, caseinate, casein, egg, and human skeletal muscle protein were assessed using UPLC–MS/MS. EAA contents of plant-based protein isolates such as oat (21%), lupin (21%), and wheat (22%) were lower than animal-based proteins (whey 43%, milk 39%, casein 34%, and egg 32%) and muscle protein (38%). AA profiles largely differed among plant-based proteins with leucine contents ranging from 5.1% for hemp to 13.5% for corn protein, compared to 9.0% for milk, 7.0% for egg, and 7.6% for muscle protein. Methionine and lysine were typically lower in plant-based proteins (1.0 ± 0.3 and 3.6 ± 0.6%) compared with animal-based proteins (2.5 ± 0.1 and 7.0 ± 0.6%) and muscle protein (2.0 and 7.8%, respectively). In conclusion, there are large differences in EAA contents and AA composition between various plant-based protein isolates. Combinations of various plant-based protein isolates or blends of animal and plant-based proteins can provide protein characteristics that closely reflect the typical characteristics of animal-based proteins.
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            Rhabdomyolysis.

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              Aging, exercise, and muscle protein metabolism.

              Aging is accompanied by a progressive loss of skeletal muscle mass and strength, leading to the loss of functional capacity and an increased risk of developing chronic metabolic disease. The age-related loss of skeletal muscle mass is attributed to a disruption in the regulation of skeletal muscle protein turnover, resulting in an imbalance between muscle protein synthesis and degradation. As basal (fasting) muscle protein synthesis rates do not seem to differ substantially between the young and elderly, many research groups have started to focus on the muscle protein synthetic response to the main anabolic stimuli, i.e., food intake and physical activity. Recent studies suggest that the muscle protein synthetic response to food intake is blunted in the elderly. The latter is now believed to represent a key factor responsible for the age-related decline in skeletal muscle mass. Physical activity and/or exercise stimulate postexercise muscle protein accretion in both the young and elderly. However, the latter largely depends on the timed administration of amino acids and/or protein before, during, and/or after exercise. Prolonged resistance type exercise training represents an effective therapeutic strategy to augment skeletal muscle mass and improve functional performance in the elderly. The latter shows that the ability of the muscle protein synthetic machinery to respond to anabolic stimuli is preserved up to very old age. Research is warranted to elucidate the interaction between nutrition, exercise, and the skeletal muscle adaptive response. The latter is needed to define more effective strategies that will maximize the therapeutic benefits of lifestyle intervention in the elderly.
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                Author and article information

                Journal
                Nutrients
                Nutrients
                nutrients
                Nutrients
                MDPI
                2072-6643
                10 July 2020
                July 2020
                : 12
                : 7
                : 2049
                Affiliations
                [1 ]Department of Nutrition, Food and Exercise Sciences, Institute of Sports Sciences and Medicine, Florida State University, Tallahassee, FL 32306, USA; pgs16@ 123456fsu.edu (P.G.S.); saylor16@ 123456live.unc.edu (H.E.S.); brh17b@ 123456my.fsu.edu (B.R.H.); rhickner@ 123456fsu.edu (R.C.H.); jkim6@ 123456fsu.edu (J.-S.K.)
                [2 ]Discipline of Biokinetics, Exercise and Leisure Sciences, University of KwaZulu-Natal, Durban 4041, South Africa
                Author notes
                [* ]Correspondence: mormsbee@ 123456fsu.edu
                Article
                nutrients-12-02049
                10.3390/nu12072049
                7400837
                32664290
                41d4f830-9d91-4bdf-975e-679ce8f1523b
                © 2020 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 04 June 2020
                : 06 July 2020
                Categories
                Article

                Nutrition & Dietetics
                dietary protein,plant-based protein,muscle damage,muscle recovery,exercise,strength

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