NUTRIM School of Nutrition and Translational Research in Metabolism.
Top Institute Food and Nutrition (TIFN), Wageningen, The Netherlands.
J Nutr. 2019 Feb 1;149(2):221-230. doi: 10.1093/jn/nxy263.
Age-related decline in skeletal muscle mass is at least partly attributed to anabolic resistance to food intake. Resistance exercise sensitizes skeletal muscle tissue to the anabolic properties of amino acids.
The present study assessed protein digestion and amino acid absorption kinetics, whole-body protein balance, and the myofibrillar protein synthetic response to ingestion of different amounts of protein during recovery from resistance exercise in older men.
Forty-eight healthy older men [mean ± SEM age: 66 ± 1 y; body mass index (kg/m2): 25.4 ± 0.3] were randomly assigned to ingest 0, 15, 30, or 45 g milk protein concentrate after a single bout of resistance exercise consisting of 4 sets of 10 repetitions of leg press and leg extension and 2 sets of 10 repetitions of lateral pulldown and chest press performed at 75-80% 1-repetition maximum. Postprandial protein digestion and amino acid absorption kinetics, whole-body protein metabolism, and myofibrillar protein synthesis rates were assessed using primed, continuous infusions of l-[ring-2H5]-phenylalanine, l-[ring-2H2]-tyrosine, and l-[1-13C]-leucine combined with ingestion of intrinsically l-[1-13C]-phenylalanine and l-[1-13C]-leucine labeled protein.
Whole-body net protein balance showed a dose-dependent increase after ingestion of 0, 15, 30, or 45 g of protein (0.015 ± 0.002, 0.108 ± 0.004, 0.162 ± 0.008, and 0.215 ± 0.009 μmol Phe · kg-1 · min-1, respectively; P < 0.001). Myofibrillar protein synthesis rates were higher after ingesting 30 (0.0951% ± 0.0062%/h, P = 0.07) or 45 g of protein (0.0970% ± 0.0062%/h, P < 0.05) than after 0 g (0.0746% ± 0.0051%/h). Incorporation of dietary protein-derived amino acids (l-[1-13C]-phenylalanine) into de novo myofibrillar protein showed a dose-dependent increase after ingestion of 15, 30, or 45 g protein (0.0171 ± 0.0017, 0.0296 ± 0.0030, and 0.0397 ± 0.0026 mole percentage excess, respectively; P < 0.05).
Dietary protein ingested during recovery from resistance exercise is rapidly digested and absorbed. Whole-body net protein balance and dietary protein-derived amino acid incorporation into myofibrillar protein show dose-dependent increases. Ingestion of ≥30 g protein increases postexercise myofibrillar protein synthesis rates in older men. This trial was registered at Nederlands Trial Register as NTR4492.
与年龄相关的骨骼肌质量下降至少部分归因于食物摄入的合成代谢抵抗。阻力运动使骨骼肌组织对氨基酸的合成代谢特性敏感。
本研究评估了不同量的蛋白质在抵抗运动后恢复期间的蛋白质消化和氨基酸吸收动力学、全身蛋白质平衡以及肌原纤维蛋白合成反应在老年男性中的作用。
48 名健康的老年男性[平均±SEM 年龄:66±1 岁;体重指数(kg/m2):25.4±0.3]随机分为 0、15、30 或 45 g 牛奶蛋白浓缩物组,在单次抵抗运动后摄入,该运动由 4 组 10 次重复的腿推和腿伸展以及 2 组 10 次重复的侧下拉和卧推组成,强度为 75-80%的 1 次重复最大强度。使用经[ring-2H5]-苯丙氨酸、[ring-2H2]-酪氨酸和[l-1-13C]-亮氨酸的连续脉冲输注以及内在标记的[l-1-13C]-苯丙氨酸和[l-1-13C]-亮氨酸标记的蛋白质的摄入,评估了餐后蛋白质消化和氨基酸吸收动力学、全身蛋白质代谢和肌原纤维蛋白合成率。
摄入 0、15、30 或 45 g 蛋白质后,全身净蛋白质平衡呈剂量依赖性增加(分别为 0.015±0.002、0.108±0.004、0.162±0.008 和 0.215±0.009 μmol Phe·kg-1·min-1;P<0.001)。摄入 30(0.0951%±0.0062%/h,P=0.07)或 45 g 蛋白质(0.0970%±0.0062%/h,P<0.05)后的肌原纤维蛋白合成率高于 0 g(0.0746%±0.0051%/h)。饮食中蛋白质衍生氨基酸(l-[1-13C]-苯丙氨酸)掺入新合成的肌原纤维蛋白呈剂量依赖性增加,摄入 15、30 或 45 g 蛋白质后分别为 0.0171±0.0017、0.0296±0.0030 和 0.0397±0.0026 摩尔百分比过量(P<0.05)。
抵抗运动后恢复期间摄入的膳食蛋白质被迅速消化和吸收。全身净蛋白质平衡和饮食蛋白质衍生氨基酸掺入肌原纤维蛋白呈剂量依赖性增加。摄入≥30 g 蛋白质可增加老年男性运动后的肌原纤维蛋白合成率。本试验在荷兰临床试验注册中心注册为 NTR4492。