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- W2068647583 abstract "•Dietary protein is an essential nutrient that is required for health. •Variations in protein quality or quantity robustly alter food intake. •The intake of protein appears to be regulated independently of other nutrients. •Protein-specific mechanisms offer novel opportunities for the treatment of obesity. Free-feeding animals often face complex nutritional choices that require the balancing of competing nutrients, but the mechanisms driving macronutrient-specific food intake are poorly defined. A large number of behavioral studies indicate that both the quantity and quality of dietary protein can markedly influence food intake and metabolism, and that dietary protein intake may be prioritized over energy intake. This review focuses on recent progress in defining the mechanisms underlying protein-specific feeding. Considering the evidence that protein powerfully regulates both food intake and metabolism, uncovering these protein-specific mechanisms may reveal new molecular targets for the treatment of obesity and diabetes while also offering a more complete understanding of how dietary factors shape both food intake and food choice. Free-feeding animals often face complex nutritional choices that require the balancing of competing nutrients, but the mechanisms driving macronutrient-specific food intake are poorly defined. A large number of behavioral studies indicate that both the quantity and quality of dietary protein can markedly influence food intake and metabolism, and that dietary protein intake may be prioritized over energy intake. This review focuses on recent progress in defining the mechanisms underlying protein-specific feeding. Considering the evidence that protein powerfully regulates both food intake and metabolism, uncovering these protein-specific mechanisms may reveal new molecular targets for the treatment of obesity and diabetes while also offering a more complete understanding of how dietary factors shape both food intake and food choice. a transcription factor that induces the expression of stress response genes as part of the integrated stress response. ATF4 is downstream of GCN2/eIF2α and is activated by amino acid restriction. a kinase that is activated by cellular energy restriction that functions as a metabolic switch to coordinate diverse cellular responses to nutrient restriction. an area of the cortical brain that is classically associated with olfaction, but which is essential for the anorexia induced by deprivation of a single essential amino acid. a gut-derived hormone that reduces food intake in response to food ingestion. a neuropeptide, mainly produced in the hypothalamus, that is associated with the response to various stressors. a cellular protein that is phosphorylated by a variety of upstream kinases in response to cellular stress, including GCN2. eIF2α phosphorylation leads to the inhibition of cellular protein synthesis as well as to the specific activation of the integrated stress response. a kinase that serves as a primary intracellular signaling molecule mediating the cellular response to a variety of growth factors. a nutritionally regulated hormone which induces a broad range of beneficial metabolic effects. a serine/threonine kinase that is activated by essential amino acid restriction and which phosphorylates eIF2α to inhibit cellular protein translation and induce a series of cellular stress responses. a state-space modeling method that has been used to model the interacting effects of macronutrient intake on physiological endpoints. a gut-derived hormone that reduces food intake in response to food ingestion. a kinase that coordinates diverse cellular responses to variations in nutrient availability and growth factor signaling. receptor expressed on neurons within the brain associated with regulation of body weight, food intake, and energy expenditure. a gut-derived hormone that reduces food intake in response to food ingestion. a neuropeptide associated with the regulation of thyroid hormone, but which also acts on diverse neural systems. a kinase which phosphorylates ribosomal protein S6 in response to upstream activation by mTOR, coordinating the effect of growth factors and nutrients on cell growth." @default.
- W2068647583 created "2016-06-24" @default.
- W2068647583 creator A5018062539 @default.
- W2068647583 creator A5056001929 @default.
- W2068647583 date "2015-05-01" @default.
- W2068647583 modified "2023-09-23" @default.
- W2068647583 title "Protein-dependent regulation of feeding and metabolism" @default.
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