Multiple reviews have examined the impact of nutritional interventions in patients with burn injuries; however, discrepancies among results cast doubt about their validity. We implemented this review to assess the impact of various nutritional interventions in adult patients with burn injuries. We conducted a thorough search of PubMed, Scopus and Web of Science databases until 1 August 2024, to identify relevant meta-analyses of intervention trials, examining the impact of nutritional interventions on burn patients. We adopted the random-effect models to determine the pooled effect sizes while employing the Grading of Recommendations Assessment, Development, and Evaluation (GRADE) to examine evidence certainty. Thirty-three original intervention trials from eleven meta-analyses were entered in our review. Early enteral nutrition could substantially reduce overall mortality (relative risk (RR): 0·36, 95 % CI: 0·19, 0·68, GRADE = moderate certainty), hospital stay (mean difference (MD): −15·3, 95 % CI: −20·4, −10·2, GRADE = moderate certainty) and sepsis risk (RR: 0·23, 95 % CI: 0·11, 0·45, GRADE = moderate certainty). Glutamine showed a notable decrease in the length of hospital stay (MD: −6·23, 95 % CI: −9·53, −2·94, GRADE = low certainty). However, other nutritional interventions, including combined immunonutrition, branched-chain amino acids, fish oil, ornithine α-ketoglutarate and trace elements, did not significantly affect the assessed clinical outcomes. Early enteral nutrition might impose a beneficial effect on mortality, hospital stay length and incidence of sepsis with moderate evidence. Lower length of hospital stay was also seen in burn patients supplemented with glutamine, although the evidence was weak.

Plasma levels of branched-chain amino acids (BCAA) and their metabolites, branched-chain ketoacids (BCKA), are increased in insulin resistance. We previously showed that ketoisocaproic acid (KIC) suppressed insulin-stimulated glucose transport in L6 myotubes, especially in myotubes depleted of branched-chain ketoacid dehydrogenase (BCKD), the enzyme that decarboxylates BCKA. This suggests that upregulating BCKD activity might improve insulin sensitivity. We hypothesised that increasing BCAA catabolism would upregulate insulin-stimulated glucose transport and attenuate insulin resistance induced by BCKA. L6 myotubes were either depleted of BCKD kinase (BDK), the enzyme that inhibits BCKD activity, or treated with BT2, a BDK inhibitor. Myotubes were then treated with KIC (200 μM), leucine (150 μM), BCKA (200 μM), or BCAA (400 μM) and then treated with or without insulin (100 nM). BDK depletion/inhibition rescued the suppression of insulin-stimulated glucose transport by KIC/BCKA. This was consistent with the attenuation of IRS-1 (Ser612) and S6K1 (Thr389) phosphorylation but there was no effect on Akt (Ser473) phosphorylation. The effect of leucine or BCAA on these measures was not as pronounced and BT2 did not influence the effect. Induction of the mTORC1/IRS-1 (Ser612) axis abolished the attenuating effect of BT2 treatment on glucose transport in cells treated with KIC. Surprisingly, rapamycin co-treatment with BT2 and KIC further reduced glucose transport. Our data suggests that the suppression of insulin-stimulated glucose transport by KIC/BCKA in muscle is mediated by mTORC1/S6K1 signalling. This was attenuated by upregulating BCAA catabolic flux. Thus, interventions targeting BCAA metabolism may provide benefits against insulin resistance and its sequelae.

We aimed to investigate the intricate interplay between genetic predisposition and lifestyle factors on stroke. We conducted a comprehensive genome-wide association study to identify the genetic variants linked to stroke in the participants who experienced a stroke event (cases; n 672) and those with no stroke history (non-stroke; n 58 029) in a large hospital-based cohort. Using generalised multifactor dimensionality reduction, we identified genetic variants with interactive effects and constructed polygenic risk scores (PRS) by summing up the risk alleles from the genetic variants. Food intake was measured with a validated semi-quantitative FFQ. No significant differences in stroke incidence were seen in demographic variables between the two groups. Among the metabolic indicators, only serum TAG levels were higher in males with stroke than those without stroke. The daily nutrient intake, dietary inflammation index, glycaemic index, dietary patterns, alcohol consumption, exercise and smoking did not display associations with the OR for stroke. The stroke-linked genetic variants were related to the IL-18 pathway. After accounting for covariates, the PRS derived from the 5-, 6- and 7-SNP models were positively associated with stroke chance with 2·5-, 2·9- and 2·8-fold. Furthermore, interactions between genetic predisposition and dietary components, including energy, carbohydrates, n-3 fatty acids and branched-chain amino acids (BCAA), that affected OR for stroke were observed. A high intake of energy, carbohydrates and BCAA and a low intake of n-3 fatty acids were positively associated with the chances of stroke occurrence. In conclusion, understanding the interaction between genetic variants and lifestyle factors can assist in developing stroke prevention and management strategies.

Branched-chain amino acids (BCAA: leucine, isoleucine and valine) are three of the nine indispensable amino acids, and are frequently consumed as a dietary supplement by athletes and recreationally active individuals alike. The popularity of BCAA supplements is largely predicated on the notion that they can stimulate rates of muscle protein synthesis (MPS) and suppress rates of muscle protein breakdown (MPB), the combination of which promotes a net anabolic response in skeletal muscle. To date, several studies have shown that BCAA (particularly leucine) increase the phosphorylation status of key proteins within the mechanistic target of rapamycin (mTOR) signalling pathway involved in the regulation of translation initiation in human muscle. Early research in humans demonstrated that BCAA provision reduced indices of whole-body protein breakdown and MPB; however, there was no stimulatory effect of BCAA on MPS. In contrast, recent work has demonstrated that BCAA intake can stimulate postprandial MPS rates at rest and can further increase MPS rates during recovery after a bout of resistance exercise. The purpose of this evidence-based narrative review is to critically appraise the available research pertaining to studies examining the effects of BCAA on MPS, MPB and associated molecular signalling responses in humans. Overall, BCAA can activate molecular pathways that regulate translation initiation, reduce indices of whole-body and MPB, and transiently stimulate MPS rates. However, the stimulatory effect of BCAA on MPS rates is less than the response observed following ingestion of a complete protein source providing the full complement of indispensable amino acids.

The benefits of branched-chain amino acid (BCAA) administration after hepatic intervention in patients with liver diseases remain unclear. We conducted a systematic review and meta-analysis to evaluate the effects of BCAA on patients undergoing hepatectomy, trans-arterial embolisation and radiofrequency ablation. Relevant randomised controlled trials (RCT) were obtained from PubMed, EMBASE and Cochrane Library databases. A meta-analysis was performed to calculate the pooled effect size by using random-effects models. The primary outcomes were survival and tumour recurrence. The secondary outcomes were hospital stay, nutrition status, biochemistry profile, complication rate of liver treatment and adverse effect of BCAA supplementation. In total, eleven RCT involving 750 patients were included. Our meta-analysis showed no significant difference in the rates of tumour recurrence and overall survival between the BCAA and control groups. However, the pooled estimate showed that BCAA supplementation in patients undergoing hepatic intervention significantly increased serum albumin (mean difference (MD): 0·11 g/dl, 95 % CI: 0·02, 0·20; 5 RCT) at 6 months and cholinesterase level (MD: 50·00 U/L, 95 % CI: 21·08, 78·92; 1 RCT) at 12 months and reduced ascites incidence (risk ratio: 0·39, 95 % CI: 0·21, 0·71; 4 RCT) at 12 months compared with the control group. Additionally, BCAA administration significantly increased body weight at 6 months and 12 months and increased arm circumference at 12 months. In conclusion, BCAA supplementation significantly improved the liver function, reduced the incidence of ascites and increased body weight and arm circumference. Thus, BCAA supplementation may beneficial for selected patients undergoing liver intervention.

The branched-chain amino acid (BCAA) is a group of essential amino acids that are involved in maintaining the energy balance of a human being as well as the homoeostasis of GABAergic, glutamatergic, serotonergic and dopaminergic systems. Disruption of these systems has been associated with the pathophysiology of autism while low levels of these amino acids have been discovered in patients with autism. A pilot open-label, prospective, follow-up study of the use of BCAA in children with autistic behaviour was carried out. Fifty-five children between the ages of 6 and 18 participated in the study from May 2015 to May 2018. We used a carbohydrate-free BCAA-powdered mixture containing 45·5 g of leucine, 30 g of isoleucine and 24·5 g of valine in a daily dose of 0·4 g/kg of body weight which was administered every morning. Following the initiation of BCAA administration, children were submitted to a monthly psychological examination. Beyond the 4-week mark, BCAA were given to thirty-two people (58·18 %). Six of them (10·9 %) discontinued after 4–10 weeks owing to lack of improvement. The remaining twenty-six children (47·27 %) who took BCAA for longer than 10 weeks displayed improved social behaviour and interactions, as well as improvements in their speech, cooperation, stereotypy and, principally, their hyperactivity. There were no adverse reactions reported during the course of the treatment. Although these data are preliminary, there is some evidence that BCAA could be used as adjunctive treatment to conventional therapeutic methods for the management of autism.

As an internal time-keeping mechanism, circadian rhythm plays crucial role in maintaining homoeostasis when in response to nutrition change; meanwhile, branched-chain amino acids (BCAA) in skeletal muscle play an important role in preserving energy homoeostasis during fasting. Previous results from our laboratory suggested that fasting can influence peripheral circadian rhythm and BCAA metabolism in fish, but the relationship between circadian rhythm and BCAA metabolism, and whether circadian rhythm regulates BCAA metabolism to maintain physiological homoeostasis during fasting remains unclear. This study shows that the expression of fifteen core clock genes as well as KLF15 and Bcat2 is highly responsive to short-term fasting in fast muscle of Siniperca chuatsi, and the correlation coefficient between Clock and KLF15 expression is enhanced after fasting treatment. Furthermore, we demonstrate that the transcriptional expression of KLF15 is regulated by Clock, and the transcriptional expression of Bcat2 is regulated by KLF15 by using dual-luciferase reporter gene assay and Vivo-morpholinos-mediated gene knockdown technique. Therefore, fasting imposes a dynamic coordination of transcription between the circadian rhythm and BCAA metabolic pathways. The findings highlight the interaction between circadian rhythm and BCAA metabolism and suggest that fasting induces a switch in KLF15 expression through affecting the rhythmic expression of Clock, and then KLF15 promotes the transcription of Bcat2 to enhance the metabolism of BCAA, thus maintaining energy homoeostasis and providing energy for skeletal muscle as well as other tissues.

Circulating branched-chain amino acids (BCAA), a subgroup of the nine essential amino acids, has been associated with pancreatic cancer risk. The aim of this study is to estimate the relation between BCAA intake from diet and pancreatic cancer risk. We analysed data from a multicentric Italian case–control study, including 326 pancreatic cancer cases and 652 controls, matched to cases by study centre, sex and age. A validated FFQ was used to collect the participants’ usual diet before cancer diagnosis (or hospital admission for controls) and to compute dietary intakes of various nutrients, including BCAA. OR and the corresponding CI were computed through logistic regression models conditioned on the matching variables and adjusted for major confounding factors, including total energy intake. We found a positive association between BCAA intake and pancreatic cancer risk (OR for the third quartile = 1·88, 95 % CI = 1·08, 3·26; OR for the fourth quartile = 2·17, 95 % CI = 1·17, 4·06), with a significant trend in risk. The association persisted after excluding subjects with diabetes and family history of pancreatic cancer and across strata of selected covariates. These data support and quantify the association between dietary BCAA and pancreatic cancer, previously suggested by studies on circulating BCAA.

Protein quality has an important role in increasing satiety. Evidence suggests that whey protein (WP) provides satiety via gastrointestinal hormone secretion. Hydrolysed collagen supplementation can also stimulate the production of incretins and influence satiety and food intake. Thus, we sought to compare the effect of acute supplementation of WP or hydrolysed collagen on post-intervention appetite and energy consumption. This was a randomised, double-blind, crossover pilot study with ten healthy adult women (22·4 years/old) who were submitted to acute intake (single dose) of a beverage containing WP (40 g of concentrated WP) or hydrolysed collagen (40 g). Subjective appetite ratings (feelings of hunger, desire to eat and full stomach) were measured using the Visual Analog Scale (VAS), energy intake was quantified by ad libitum cheese bread consumption 2 hours after supplementation and blood was collected for leptin and glucose determination. There was no difference between treatment groups in the perception of hunger (P = 0·983), desire to eat (P = 0·326), full stomach feeling (P = 0·567) or food consumption (P = 0·168). Leptin concentrations at 60 min post supplementation were higher when subjects received hydrolysed collagen (P = 0·006). Acute supplementation with hydrolysed collagen increased leptin levels in comparison with WP, but had no effect on appetite measured by feelings of hunger, desire to eat, full stomach feeling (VAS) or energy consumption.

The fish paste product, fish balls ‘tsumire’, is a traditional type of Japanese food made from minced fish as well as imitation crab, kamaboko and hanpen. Although tsumire is known as a high-protein and low-fat food, there is a lack of scientific evidence on its health benefits. Hence, we aimed to investigate the effects of tsumire intake on organ weight and biomarker levels in Sprague–Dawley rats for 84 d as a preliminary study. Six-week-old male Sprague–Dawley rats were divided into two groups: group I, fed normal diets, and group II, fed normal diets with 5 % dried tsumire. Throughout the administration period, we monitored their body weight and food intake; at the end of this period, we measured their organ weight and analysed their blood biochemistry. No significant differences were observed with respect to body weight, food intake, organ weight and many biochemical parameters between the two groups. It was found that inorganic phosphorus and glucose levels were higher in group II rats than in group I rats. On the other hand, sodium, calcium, amylase and cholinesterase levels were significantly lower in group II than in group I. Interestingly, we found that the levels of aspartate aminotransferase, alanine transaminase, lactate dehydrogenase and leucine aminopeptidase in group II were significantly lower than in group I, and that other liver function parameters of group II tended to be lower than in group I. In conclusion, we consider that the Japanese traditional food, ‘tsumire,’ may be effective as a functional food for human health management worldwide.

Branched-chain amino acids (BCAA) are considered markers of insulin resistance (IR) in subjects with obesity. In this study, we evaluated whether the presence of the SNP of the branched-chain aminotransferase 2 (BCAT2) gene can modify the effect of a dietary intervention (DI) on the plasma concentration of BCAA in subjects with obesity and IR. A prospective cohort study of adult subjects with obesity, BMI ≥ 30 kg/m2, homeostatic model assessment-insulin resistance (HOMA-IR ≥ 2·5) no diagnosed chronic disease, underwent a DI with an energy restriction of 3140 kJ/d and nutritional education for 1 month. Anthropometric measurements, body composition, blood pressure, resting energy expenditure, oral glucose tolerance test results, serum biochemical parameters and the plasma amino acid profile were evaluated before and after the DI. SNP were assessed by the TaqMan SNP genotyping assay. A total of eighty-two subjects were included, and fifteen subjects with a BCAT2 SNP had a greater reduction in leucine, isoleucine, valine and the sum of BCAA. Those subjects also had a greater reduction in skeletal muscle mass, fat-free mass, total body water, blood pressure, muscle strength and biochemical parameters after 1 month of the DI and adjusting for age and sex. This study demonstrated that the presence of the BCAT2 SNP promotes a greater reduction in plasma BCAA concentration after adjusting for age and sex, in subjects with obesity and IR after a 1-month energy-restricted DI.

Alcohol abuse causes severe metabolic abnormalities inducing hepatic damage and malnutrition. Since higher Fischer ratio proteins have therapeutic value in liver diseases, an investigation was undertaken to study the ameliorative effect of the enhanced Fischer ratio flaxseed protein hydrolysate (EFR-FPH) alone and in combination with antioxidant micronutrients on ethanol-induced hepatotoxicity in a rat model. The EFR-FPH was prepared by dual enzymatic hydrolysis and charcoal treatment of flaxseed protein. The ratio of the branched-chain:aromatic amino acids (Fischer ratio) was found to be 7·08. The EFR-FPH, characterised using LC-MS/MS, showed the abundance of free leucine and isoleucine compared with phenylalanine and tyrosine. The matrix-assisted laser desorption/ionisation-time of flight MS analysis revealed the larger peptides present in EFR-FPH with mass 2·3 kDa. The EFR-FPH improved the nutritional status, liver function and antioxidant defense in the ethanol hepatotoxicity-induced rat model. The hepatoprotective effect of EFR-FPH was significantly enhanced when combined with selenium or vitamin E. Ethanol-induced changes in the liver tissue were effectively suppressed in the groups receiving EFR-FPH. Flaxseed-based hepatoprotective dietary supplement was formulated incorporating an optimum level of EFR-FPH (10 %) based on sensory acceptability and was fortified with selenium and vitamin E. The hepatoprotective formulation significantly lowered aspartate transaminase, alanine transaminase, alkaline phosphatase and bilirubin by 47, 61, 55 and 78 %, respectively, and improved the antioxidant defense in the ethanol hepatotoxicity-induced rat model. The current investigation suggests that EFR-FPH in synergy with antioxidant micronutrients is potent in ameliorating ethanol-induced hepatotoxicity and has a potential to form a hepatoprotective dietary supplement.

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.

An adequate intake of branched-chain amino acids (BCAA) is required for protein synthesis and metabolic functions, including insulin metabolism. Emerging studies found positive associations between BCAA and the risk of various diseases sharing aetiological aspects with colorectal cancer (CRC), including type 2 diabetes, obesity and pancreatic cancer. We investigated the relation between dietary BCAA and CRC using data from a multicentric Italian case–control study, including 1953 cases of CRC (of these, 442 of sigmoid colon) and 4154 hospital controls with acute, non-neoplastic diseases. A validated FFQ was used to estimate the participants’ usual diet and to assess dietary intakes of various nutrients, including energy, BCAA and Ca. OR and corresponding CI were computed by multiple logistic regression models adjusted for age, sex and other confounding factors, including total energy intake. BCAA intake was inversely related to CRC risk (OR for the highest v. the lowest quintile 0·73; 95 % CI 0·55, 0·97), but the association was attenuated after adjustment for Ca intake (OR 0·90; 95 % CI 0·65, 1·25). An inverse association with sigmoid colon cancer risk also remained after adjustment for other dietary factors, including Ca intake (OR 0·49; 95 % CI 0·27, 0·87). This study provides supporting evidence that higher levels of dietary BCAA intake are not associated with an increase of CRC risk, but confirms that they may be related to a reduced risk of sigmoid colon cancer.

The increased prevalence of lifestyle diseases, such as the metabolic syndrome and type 2 diabetes mellitus (T2DM), calls for more knowledge on dietary treatments targeting the specific metabolic pathways involved in these conditions. Several studies have shown a protein preload before a meal to be effective in lowering the postprandial glycaemic response in healthy individuals and patients with T2DM. The aim of the present study was to assess the effect of a marine protein hydrolysate (MPH) from Atlantic cod (Gadus morhua) on postprandial glucose metabolism in healthy, middle-aged to elderly subjects. This double-blind cross-over trial (n 41) included two study days with 4–7 d wash-out in between. The intervention consisted of 20 mg of MPH (or casein as control) per kg body weight given before a breakfast meal. The primary outcome was postprandial response in glucose metabolism, measured by samples of serum glucose, insulin and plasma glucagon-like peptide 1 (GLP-1) in 20 min intervals for 180 min. In a mixed-model regression analysis, no differences were observed between MPH and control for postprandial glucose concentration (mean difference: −0·04 (95 % CI –0·17, 0·09) mmol/l; P = 0·573) or GLP-1 concentration (mean difference between geometric means: 1·02 (95 % CI 0·99, 1·06) pmol/l; P = 0·250). The postprandial insulin concentration was significantly lower after MPH compared with control (mean difference between geometric means: 1·067 (95 % CI 1·01, 1·13) mIU/l; P = 0·032). Our findings demonstrate that a single dose of MPH before a breakfast meal reduces postprandial insulin secretion, without affecting blood glucose response or GLP-1 levels, in healthy individuals. Further studies with repeated dosing and in target groups with abnormal glucose control are warranted.

Lowering protein level in diets for piglets urge to have knowledge on the piglet’s requirements for essential amino acids (AA) and their interactions. The present studies aimed to determine the interaction between the dietary level of valine (Val) and tryptophan (Trp) and the effect of AA imbalance at two levels of dietary Val on the growth performance of post-weaning piglets. In Experiment 1 (duration 4 weeks), the effects of supplementation of free l-Val (1.0 g/kg) and/or l-Trp (0.5 g/kg) in a low-CP diet (CP 17.7%), marginal in Trp and Val, was studied in a 2×2 factorial design and using an additional reference treatment (CP 19.5%). In Experiment 2 (duration 5 weeks), the influence of a stepwise increase in excess supply of isoleucine (Ile), histidine (His) and leucine (Leu), up to 10, 10% and 30% relative to their requirement values respectively, was evaluated at 60% or 70% standardized ileal digestible (SID) Val relative to SID lysine, using a 3×2 factorial design. In Experiment 1, over the whole experimental period, feed intake (FI) was affected by dietary Trp level (P<0.05) and feed conversion ratio (FCR) by both the level of Trp and Val in the diet (both P<0.05). Increasing Trp level increased FI and decreased FCR while increasing dietary Val level reduced FI and increased FCR. For BW gain (BWG), there was an interaction between dietary level of Trp and Val (P<0.05). Valine supplementation decreased BWG using a diet marginal in Trp, whereas it increased BWG when using a Trp sufficient diet. Piglets fed the low-CP diet with adequate levels of Val and Trp showed at least same performance compared to piglets fed the high CP reference diet. In Experiment 2, increasing dietary Val improved FI and BWG (P<0.001) and tended to improve FCR. Dietary AA excess for Ile, His and Leu reduced FI and BWG (P<0.05) and only affected FCR (P<0.01) in the 1st week of the study. Dietary level of Val and AA excess did not show interactive effects, except for FCR over the final 2 weeks of the study (P<0.05). In conclusion, an interaction exists between dietary supply of Val and Trp on the zootechnical performance of post-weaning piglets and dietary AA excess for Ile, Leu and His, reduces growth performance of piglets in low-protein diets, independent of the dietary level of Val.

This study examined the effects of post-resistance exercise protein ingestion timing on the rate of gastric emptying (GE) and blood glucose (BG) and plasma branched-chain amino acid (BCAA) responses. In all, eleven healthy participants randomly ingested 400 ml of a nutrient-rich drink containing 12 g carbohydrates and 20 g protein at rest (Con), at 5 min (post-exercise (PE)-5) or at 30 min (PE-30) after a single bout of strenuous resistance exercises. The first and second sets comprised ten repetitions at 50 % of each participant’s one-repetition maximum (1RM). The third, fourth and fifth sets comprised ten repetitions at 75 % of 1RM, and the sixth set involved repeated repetitions until exhaustion. Following ingestion of the nutrient-rich drink, we assessed the GE rate using 13C-sodium acetate breath test and evaluated two parameters according to the Tmax-calc (time when the recovery per hour is maximised), which is a standard analytical method, and T1/2 (time when the total cumulative dose of [13CO2] reaches one-half). Tmax-calc and T1/2 were slower for the PE-5 condition than for either the PE-30 or Con condition (Tmax-calc; Con: 53 (sd 7) min, PE-5: 83 (sd 16) min, PE-30: 62 (sd 9) min, T1/2; Con: 91 (sd 7) min, PE-5: 113 (sd 21) min, PE-30: 91 (sd 11) min, P<0·05). BG and BCAA responses were also slower for the PE-5 condition than for either the PE-30 or Con condition. Ingesting nutrients immediately after strenuous resistance exercise acutely delayed GE, which affected BG and plasma BCAA levels in blood circulation.

Branched-chain amino acids (BCAA) are essential amino acids that are necessary for muscle mass maintenance. Little is known about the plasma concentrations of BCAA and the protein intake in relation to sarcopenia. We aimed to compare the non-fasting plasma concentrations of the BCAA and the dietary protein intake between sarcopenic and non-sarcopenic older adults. Norwegian older home-dwelling adults (≥70 years) were invited to a cross-sectional study with no other exclusion criteria than age. Sarcopenic subjects were defined by the diagnostic criteria by the European Working Group on Sarcopenia in Older People. Non-fasting plasma concentrations of eight amino acids were quantified using NMR spectroscopy. Protein intake was assessed using 2×24-h dietary recalls. In this study, ninety out of 417 subjects (22 %) were sarcopenic, and more women (32 %) than men (11 %) were sarcopenic (P<0·0001). Sex-adjusted non-fasting plasma concentrations of leucine and isoleucine, and the absolute intake of protein (g/d), were significantly lower among the sarcopenic subjects, when compared with non-sarcopenic subjects (P=0·003, P=0·026 and P=0·003, respectively). A similar protein intake was observed in the two groups when adjusted for body weight (BW) and sex (1·1 g protein/kg BW per d; P=0·50). We show that sarcopenia is associated with reduced non-fasting plasma concentration of the BCAA leucine and isoleucine, and lower absolute intake of protein. More studies are needed to clarify the clinical relevance of these findings, related to maintenance of muscle mass and prevention of sarcopenia.

Epidemiological studies demonstrate that poor glycaemic control is an independent risk factor for CVD. Postprandial glycaemia has been demonstrated as a better predictor of glycated Hb, the gold standard of glycaemic control, when compared with fasting blood glucose. There is a need for more refined strategies to tightly control postprandial glycaemia, particularly in those with type 2 diabetes, and nutritional strategies around meal consumption may be effective in enhancing subsequent glycaemic control. Whey protein administration around meal times has been demonstrated to reduce postprandial glycaemia, mediated through various mechanisms including an enhancement of insulin secretion. Whey protein ingestion has also been shown to elicit an incretin effect, enhancing the secretion of glucose-dependent insulinotropic peptide and glucagon-like peptide-1, which may also influence appetite regulation. Acute intervention studies have shown some promising results however many have used large dosages (50–55 g) of whey protein alongside high-glycaemic index test meals, such as instant powdered potato mixed with glucose, which does not reflect realistic dietary strategies. Long-term intervention studies using realistic strategies around timing, format and amount of whey protein in relevant population groups are required.