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Dietary protein is a pre-requisite for the maintenance of skeletal muscle mass; stimulating increases in muscle protein synthesis (MPS), via essential amino acids (EAA), and attenuating muscle protein breakdown, via insulin. Muscles are receptive to the anabolic effects of dietary protein, and in particular the EAA leucine, for only a short period (i.e. about 2–3 h) in the rested state. Thereafter, MPS exhibits tachyphylaxis despite continued EAA availability and sustained mechanistic target of rapamycin complex 1 signalling. Other notable characteristics of this ‘muscle full’ phenomenon include: (i) it cannot be overcome by proximal intake of additional nutrient signals/substrates regulating MPS; meaning a refractory period exists before a next stimulation is possible, (ii) it is refractory to pharmacological/nutraceutical enhancement of muscle blood flow and thus is not induced by muscle hypo-perfusion, (iii) it manifests independently of whether protein intake occurs in a bolus or intermittent feeding pattern, and (iv) it does not appear to be dependent on protein dose per se. Instead, the main factor associated with altering muscle full is physical activity. For instance, when coupled to protein intake, resistance exercise delays the muscle full set-point to permit additional use of available EAA for MPS to promote muscle remodelling/growth. In contrast, ageing is associated with blunted MPS responses to protein/exercise (anabolic resistance), while physical inactivity (e.g. immobilisation) induces a premature muscle full, promoting muscle atrophy. It is crucial that in catabolic scenarios, anabolic strategies are sought to mitigate muscle decline. This review highlights regulatory protein turnover interactions by dietary protein, exercise, ageing and physical inactivity.
High-protein meals and foods are promoted for their beneficial effects on satiety, weight loss and glucose homeostasis. However, the mechanisms involved and the long-term benefits of such diets are still debated. We here review how the characterisation of intestinal gluconeogenesis (IGN) sheds new light on the mechanisms by which protein diets exert their beneficial effects on health. The small intestine is the third organ (in addition to the liver and kidney) contributing to endogenous glucose production via gluconeogenesis. The particularity of glucose produced by the intestine is that it is detected in the portal vein and initiates a nervous signal to the hypothalamic nuclei regulating energy homeostasis. In this context, we demonstrated that protein diets initiate their satiety effects indirectly via IGN and portal glucose sensing. This induction results in the activation of brain areas involved in the regulation of food intake. The μ-opioid-antagonistic properties of protein digests, exerted in the portal vein, are a key link between IGN induction and protein-enriched diet in the control of satiety. From our results, IGN can be proposed as a mandatory link between nutrient sensing and the regulation of whole-body homeostasis. The use of specific mouse models targeting IGN should allow us to identify several metabolic functions that could be controlled by protein diets. This will lead to the characterisation of the mechanisms by which protein diets improve whole-body homeostasis. These data could be the basis of novel nutritional strategies targeting the serious metabolic consequences of both obesity and diabetes.
Life expectancy in most developed countries has been rising over the past century. In the UK alone, there are about 12 million people over 65 years old and centenarians have increased by 85% in the past 15 years. As a result of the ageing population, which is due mainly to improvements in medical treatments, public health, improved housing and lifestyle choices, there is an associated increase in the prevalence of pathological conditions, such as metabolic disorders, type 2 diabetes, cardiovascular and neurodegenerative diseases, many types of cancer and others. Statistics suggest that nearly 54% of elderly people in the UK live with at least two chronic conditions, revealing the urgency for identifying interventions that can prevent and/or treat such disorders. Non-pharmacological, dietary interventions such as energetic restriction (ER) and methionine restriction (MR) have revealed promising outcomes in increasing longevity and preventing and/or reversing the development of ageing-associated disorders. In this review, we discuss the evidence and mechanisms that are involved in these processes. Fibroblast growth factor 1 and hydrogen sulphide are important molecules involved in the effects of ER and MR in the extension of life span. Their role is also associated with the prevention of metabolic and cognitive disorders, highlighting these interventions as promising modulators for improvement of health span.
Symposium Two: Novel methods for assessing protein metabolism
All tissues are in a constant state of turnover, with a tightly controlled regulation of protein synthesis and breakdown rates. Due to the relative ease of sampling skeletal muscle tissue, basal muscle protein synthesis rates and the protein synthetic responses to various anabolic stimuli have been well defined in human subjects. In contrast, only limited data are available on tissue protein synthesis rates in other organs. Several organs such as the brain, liver and pancreas, show substantially higher (basal) protein synthesis rates when compared to skeletal muscle tissue. Such data suggest that these tissues may also possess a high level of plasticity. It remains to be determined whether protein synthesis rates in these tissues can be modulated by external stimuli. Whole-body protein synthesis rates are highly responsive to protein intake. As the contribution of muscle protein synthesis rates to whole-body protein synthesis rates is relatively small considering the large amount of muscle mass, this suggests that other organ tissues may also be responsive to (protein) feeding. Whole-body protein synthesis rates in the fasted or fed state can be quantified by measuring plasma amino acid kinetics, although this requires the production of intrinsically labelled protein. Protein intake requirements to maximise whole-body protein synthesis may also be determined by the indicator amino acid oxidation technique, but the technique does not allow the assessment of actual protein synthesis and breakdown rates. Both approaches have several other methodological and inferential limitations that will be discussed in detail in this paper.
This review outlines the current use of magnetic resonance (MR) techniques to study digestion and highlights their potential for providing markers of digestive processes such as texture changes and nutrient breakdown. In vivo digestion research can be challenging due to practical constraints and biological complexity. Therefore, digestion is primarily studied using in vitro models. These would benefit from further in vivo validation. NMR is widely used to characterise food systems. MRI is a related technique that can be used to study both in vitro model systems and in vivo gastro-intestinal processes. MRI allows visualisation and quantification of gastric processes such as gastric emptying and coagulation. Both MRI and NMR scan sequences can be configured to be sensitive to different aspects of gastric or intestinal contents. For example, magnetisation transfer and chemical exchange saturation transfer can detect proton (1H) exchange between water and proteins. MRI techniques have the potential to provide molecular-level and quantitative information on in vivo gastric (protein) digestion. This requires careful validation in order to understand what these MR markers of digestion mean in a specific digestion context. Combined with other measures they can be used to validate and inform in vitro digestion models. This may bridge the gap between in vitro and in vivo digestion research and can aid the optimisation of food properties for different applications in health and disease.
Symposium Three: Physiological determinants for protein requirements
In parallel with increased public awareness of the health and environmental benefits of consuming a plant-based diet, the numbers of people who identify as vegan has increased sharply. The question of whether vegetarian and vegan diets are appropriate for children is a longstanding and unresolved controversy. The more restrictive the diet and the younger the child, the greater the risk of nutritional deficiency. Nutrients of potential concern are protein quantity and quality, iron, zinc, selenium, calcium, riboflavin, vitamins A, D, B12 and essential fatty acids. Although intakes and status of some nutrients (e.g. vitamin D and iron) are low in many children, vegan children are particularly susceptible due to inadequate supply and/or excess dietary fibre as well as other components that limit bioavailability. Although position papers from North America state that well-planned vegetarian and vegan diets, supplemented appropriately, are suitable for all life stages, European statements include strong recommendations to parents that vegan diets should not be adopted by children without medical and dietetic supervision. Case histories of malnutrition and serious harm persist, including irreversible neurological damage due to vitamin B12 deficiency among un-supplemented children. The evidence available to evaluate the nutritional appropriateness of vegetarian diets for children is inadequate and dated. Although nutritionally adequate vegetarian diets are more easily achieved, successful provision of a complete vegan diet for a young child requires substantial commitment, expert guidance, planning, resources and supplementation.
The present paper reviews published literature on the relationship between dietary protein and bone health. It will include arguments both for and against the anabolic and catabolic effects of dietary protein on bone health. Adequate protein intake provides the amino acids used in building and maintaining bone tissue, as well as stimulating the action of insulin-like growth factor 1, which in turn promotes bone growth and increases calcium absorption. However, the metabolism of dietary sulphur amino acids, mainly from animal protein, can lead to increased physiological acidity, which may be detrimental for bone health in the long term. Similarly, cereal foods contain dietary phytate, which in turn contains phosphate. It is known that phosphate consumption can also lead to increased physiological acidity. Therefore, cereal products may produce as much acid as do animal proteins that contain sulphur amino acids. The overall effect of dietary protein on physiological acidity, and its consequent impact on bone health, is extremely complex and somewhat controversial. The consensus is now moving towards a synthesised approach. Particularly, how anabolic and catabolic mechanisms interact; as well as how the context of the whole diet and the type of protein consumed is important.
The composition and metabolic activity of the bacteria that inhabit the large intestine can have a major impact on health. Despite considerable inter-individual variation across bacterial species, the dominant phyla are generally highly conserved. There are several exogenous and gut environmental factors that play a role in modulating the composition and activities of colonic bacteria including diet with intakes of different macronutrients, including protein, accounting for approximately 20% of the microbial variation. Certain bacterial species tend to be considered as generalists and can metabolise a broad range of substrates, including both carbohydrate- and protein-derived substrates, whilst other species are specialists with a rather limited metabolic capacity. Metabolism of peptides and amino acids by gut bacteria can result in the formation of a wide range of metabolites several of which are considered deleterious to health including nitrosamines, heterocyclic amines and hydrogen sulphide as some of these products are genotoxic and have been linked to colonic disease. Beneficial metabolites however include SCFA and certain species can use amino acids to form butyrate which is the major energy source for colonocytes. The impact on health may however depend on the source of these products. In this review, we consider the impact of diet, particularly protein diets, on modulating the composition of the gut microbiota and likely health consequences and the potential impact of climate change and food security.
Symposium Four: Protein sources: impact on environment and sustainability
Global population growth, increased life expectancy and climate change are all impacting world's food systems. In industrialised countries, many individuals are consuming significantly more protein than needed to maintain health, with the majority being obtained from animal products, including meat, dairy, fish and other aquatic animals. Current animal production systems are responsible for a large proportion of land and fresh-water use, and directly contributing to climate change through the production of greenhouse gases. Overall, approximately 60% of the global protein produced is used for animal and fish feed. Concerns about their impact on both human, and planetary health, have led to calls to dramatically curb our consumption of animal products. Underutilised plants, insects and single-cell organisms are all actively being considered as alternative protein sources. Each present challenges that need to be met before they can become economically viable and safe alternatives for food or feed. Many plant species contain anti-nutritional factors that impair the digestion and absorption of protein and micronutrients. Insects represent a potentially rich source of high-quality protein although, questions remain relating to digestibility, allergenicity and biosecurity. Algae, fungi and bacteria are also a rich source of protein and there is growing interest in the development of ‘cultured meat’ using stem cell technology. For the foreseeable future, it appears likely that the ‘protein-economy’ will remain mixed. The present paper reviews progress and future opportunities in the development of novel protein sources as food and animal feed.
Populations' diets typically fall short of recommendations. The implication of this on ill health and quality of life is well established, as are the subsequent health care costs. An area of growing interest within public health nutrition is food choice architecture; how a food choice is framed and its influence on subsequent food selection. In particular, there is an appeal to manipulating the choice architecture in order to nudge individuals' food choice. This review outlines the current understanding of food choice architecture, theoretical background to nudging and the evidence on the effectiveness of nudge strategies, as well as their design and implementation. Interventions emphasising the role of nudge strategies have investigated changes to the accessibility, availability and presentation of food and the use of prompts. Empirical studies have been conducted in laboratories, online and in real-world food settings, and with different populations. Evidence on the effectiveness of nudge strategies in shifting food choice is encouraging. Underpinning mechanisms, not yet fully explicated, are proposed to relate to salience, social norms and the principle of least effort. Emerging evidence points to areas for development including the effectiveness of choice architecture interventions with different and diverse populations, and the combined effect of multiple nudges. This, alongside further examination of theoretical mechanisms and guidance to engage and inspire across the breadth of food provision, is critical. In this way, the potential of choice architecture to effect meaningful change in populations' diets will be realised.
During ageing, skeletal muscle develops anabolic resistance towards the stimulation of protein synthesis induced by dietary amino acids. The stimulation of muscle protein synthesis after food intake remains insufficient, even with a protein intake recommended for healthy adults. This alteration is one of the mechanisms known to be responsible for the decrease of muscle mass and function during ageing, namely sarcopenia. Increasing dietary protein intake above the current RDA(0⋅83 g/kg/d) has been strongly suggested to overcome the anabolic resistance observed. It is also specified that the dietary protein ingested should be of good quality. A protein of good quality is a protein whose amino acid (AA) composition covers the requirement of each AA when ingested at the RDA. However, the biological value of proteins may vary among dietary sources in which AA composition could be unbalanced. In the present review, we suggest that the quality of a dietary protein is also related to several other determinants. These determinants include the speed of digestion of dietary proteins, the presence of specific AA, the food matrix in which the dietary proteins are included, the processes involved in the production of food products (milk gelation and cooking temperature), the energy supply and its nature, and the interaction between nutrients before ingestion. Particular attention is given to plant proteins for nutrition of the elderly. Finally, the timing of protein intake and its association with the desynchronized intake of energetic nutrients are discussed.
All human tissues are in a constant state of remodelling, regulated by the balance between tissue protein synthesis and breakdown rates. It has been well-established that protein ingestion stimulates skeletal muscle and whole-body protein synthesis. Stable isotope-labelled amino acid methodologies are commonly applied to assess the various aspects of protein metabolism in vivo in human subjects. However, to achieve a more comprehensive assessment of post-prandial protein handling in vivo in human subjects, intravenous stable isotope-labelled amino acid infusions can be combined with the ingestion of intrinsically labelled protein and the collection of blood and muscle tissue samples. The combined application of ingesting intrinsically labelled protein with continuous intravenous stable isotope-labelled amino acid infusion allows the simultaneous assessment of protein digestion and amino acid absorption kinetics (e.g. release of dietary protein-derived amino acids into the circulation), whole-body protein metabolism (whole-body protein synthesis, breakdown and oxidation rates and net protein balance) and skeletal muscle metabolism (muscle protein fractional synthesis rates and dietary protein-derived amino acid incorporation into muscle protein). The purpose of this review is to provide an overview of the various aspects of post-prandial protein handling and metabolism with a focus on insights obtained from studies that have applied intrinsically labelled protein under a variety of conditions in different populations.
The primary aim of this review is to evaluate the efficacy of essential amino acid (EAA) supplementation as a strategy to increase dietary protein intake and improve muscle mass, strength and function in older adults. A sufficient daily protein intake is widely recognised to be fundamental for the successful management of sarcopenia in older undernourished adults. In practice, optimising protein intakes in older adults is complex, requiring consideration of the dose and amino acid composition (i.e. a complete EAA profile and abundant leucine content) of ingested protein on a per meal basis, alongside the age-related decline in appetite and the satiating properties of protein. Recent studies in older adults demonstrate that EAA-based supplements are non-satiating and can be administered alongside food to enhance the anabolic properties of a meal containing a suboptimal dose of protein; an effect magnified when combined with resistance exercise training. These findings support the notion that EAA supplementation could serve as an effective strategy to improve musculoskeletal health in older adults suffering from non-communicable diseases such as sarcopenia. Compliance is critical for the long-term success of complex interventions. Hence, aspects of palatability and desire to eat are important considerations regarding EAA supplementation. In conclusion, EAA-based supplements enriched with l-leucine offer an alternative strategy to whole protein sources to assist older adults in meeting protein recommendations. In practice, EAA supplements could be administered alongside meals of suboptimal protein content, or alternatively between meals on occasions when older adults achieve their per meal protein intake recommendations.
The development and maintenance of body composition and functions require an adequate protein intake with a continuous supply of amino acids (AA) to tissues. Body pool and AA cellular concentrations are tightly controlled and maintained through AA supply (dietary intake, recycled from proteolysis and de novo synthesis), AA disposal (protein synthesis and other AA-derived molecules) and AA losses (deamination and oxidation). Different molecular regulatory pathways are involved in the control of AA sufficiency including the mechanistic target of rapamycin complex 1, the general control non-derepressible 2/activating transcription factor 4 system or the fibroblast growth factor 21. There is a tight control of protein intake, and human subjects and animals appear capable of detecting and adapting food and protein intake and metabolism in face of foods or diets with different protein contents. A severely protein deficient diet induces lean body mass losses and ingestion of sufficient dietary energy and protein is a prerequisite for body protein synthesis and maintenance of muscle, bone and other lean tissues and functions. Maintaining adequate protein intake with age may help preserve muscle mass and strength but there is an ongoing debate as to the optimal protein intake in older adults. The protein synthesis response to protein intake can also be enhanced by prior completion of resistance exercise but this effect could be somewhat reduced in older compared to young individuals and gain in muscle mass and function due to exercise require regular training over an extended period.
The present paper aims to contribute to the contentious debate regarding the role of meat as part of a sustainable diet. It uses secondary data to examine the patterns of meat consumption across the globe, and drawing on academic and grey literature, it outlines some of the policy, market and social trends and issues influencing demand and supply of meat. It also presents an overview of the scientific evidence base regarding the pros and cons of meat consumption. The results show that consumption patterns are not homogeneous globally, nor across meat types, with overall meat consumption increasing strongly in developing countries but stagnating in developed countries, and demand for poultry increasing in most regions in contrast to beef. They also illustrate the evolving impact of factors such as income on consumption and the increasing impact of non-economic factors, such as social and policy influences relating to health and the environment, on food choice behaviours, to the extent that such behaviours are increasingly entering a moral space. Given the solid scientific evidence that simultaneously substantiates arguments to increase and decrease meat consumption, it is clear that dietary recommendations need to be context-specific. An important part of the context is the strategies being pursued by researchers and supply chain actors, from farmers through to processors, retailers and food service operators, to improve the sustainability credentials of livestock production. As new evidence emerges from such initiatives, the context will change which means that dietary guidelines will require continuous review.
A progressive decrement in muscle mass and muscle function, sarcopoenia, accompanies ageing. The loss of skeletal muscle mass and function is the main feature of sarcopoenia. Preventing the loss of muscle mass is relevant since sarcopoenia can have a significant impact on mobility and the quality of life of older people. Dietary protein and physical activity have an essential role in slowing muscle mass loss and helping to maintain muscle function. However, the current recommendations for daily protein ingestion for older persons appear to be too low and are in need of adjustment. In this review, we discuss the skeletal muscle response to protein ingestion, and review the data examining current dietary protein recommendations in the older subjects. Furthermore, we review the concept of protein quality and the important role that nutrient-dense protein (NDP) sources play in meeting overall nutrient requirements and improving dietary quality. Overall, the current evidence endorses an increase in the daily ingestion of protein with emphasis on the ingestion of NDP choices by older adults.