Layman Donald K, Anthony Tracy G, Rasmussen Blake B, Adams Sean H, Lynch Christopher J, Brinkworth Grant D, Davis Teresa A
From the Department of Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, Urbana, IL (DKL); the Department of Nutritional Sciences, Rutgers University, New Brunswick, NJ (TGA); the Department of Nutrition and Metabolism, Division of Rehabilitation Science, and Sealy Center on Aging, University of Texas Medical Branch, Galveston, TX (BBR); Arkansas Children's Nutrition Center and Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock, AR (SHA); the Department of Cellular and Molecular Physiology, the Pennsylvania State University College of Medicine, Hershey, PA (CJL); the Commonwealth Scientific and Industrial Research Organization-Food and Nutritional Sciences, Adelaide, Australia (GDB); and the USDA-Agricultural Research Service Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, TX (TAD).
Am J Clin Nutr. 2015 Jun;101(6):1330S-1338S. doi: 10.3945/ajcn.114.084053. Epub 2015 Apr 29.
Dietary protein provides essential amino acids (EAAs) for the synthesis of new proteins plus an array of other metabolic functions; many of these functions are sensitive to postprandial plasma and intracellular amino acid concentrations. Recent research has focused on amino acids as metabolic signals that influence the rate of protein synthesis, inflammation responses, mitochondrial activity, and satiety, exerting their influence through signaling systems including mammalian/mechanistic target of rapamycin complex 1 (mTORC1), general control nonrepressed 2 (GCN2), glucagon-like peptide 1 (GLP-1), peptide YY (PYY), serotonin, and insulin. These signals represent meal-based responses to dietary protein. The best characterized of these signals is the leucine-induced activation of mTORC1, which leads to the stimulation of skeletal muscle protein synthesis after ingestion of a meal that contains protein. The response of this metabolic pathway to dietary protein (i.e., meal threshold) declines with advancing age or reduced physical activity. Current dietary recommendations for protein are focused on total daily intake of 0.8 g/kg body weight, but new research suggests daily needs for older adults of ≥1.0 g/kg and identifies anabolic and metabolic benefits to consuming at least 20-30 g protein at a given meal. Resistance exercise appears to increase the efficiency of EAA use for muscle anabolism and to lower the meal threshold for stimulation of protein synthesis. Applying this information to a typical 3-meal-a-day dietary plan results in protein intakes that are well within the guidelines of the Dietary Reference Intakes for acceptable macronutrient intakes. The meal threshold concept for dietary protein emphasizes a need for redistribution of dietary protein for optimum metabolic health.
膳食蛋白质为新蛋白质的合成提供必需氨基酸(EAA)以及一系列其他代谢功能;其中许多功能对餐后血浆和细胞内氨基酸浓度敏感。最近的研究集中在氨基酸作为代谢信号,影响蛋白质合成速率、炎症反应、线粒体活性和饱腹感,通过包括哺乳动物/雷帕霉素复合物1(mTORC1)、一般控制非抑制2(GCN2)、胰高血糖素样肽1(GLP-1)、肽YY(PYY)、血清素和胰岛素在内的信号系统发挥作用。这些信号代表了基于膳食蛋白质的反应。这些信号中研究得最清楚的是亮氨酸诱导的mTORC1激活,它会在摄入含蛋白质的餐后刺激骨骼肌蛋白质合成。随着年龄增长或身体活动减少,这种代谢途径对膳食蛋白质的反应(即膳食阈值)会下降。目前关于蛋白质的膳食建议侧重于每日总摄入量为0.8克/千克体重,但新研究表明老年人的每日需求量≥1.0克/千克,并确定了在每餐摄入至少20 - 30克蛋白质的合成代谢和代谢益处。抗阻运动似乎能提高EAA用于肌肉合成代谢的效率,并降低刺激蛋白质合成的膳食阈值。将这些信息应用于典型的一日三餐饮食计划,蛋白质摄入量完全在可接受宏量营养素摄入的膳食参考摄入量指南范围内。膳食蛋白质的膳食阈值概念强调了为实现最佳代谢健康而重新分配膳食蛋白质的必要性。