Impact of Raspberry (Rubus idaeus L.) Primocane Tipping on Fruit Yield and Quality

High temperature stress, which has been occurring more often in recent years, usually coincides with the flowering of primocane raspberries and causes a negative effect on fruit quality parameters. One of the methods of delaying raspberry flowering and fruit development to avoid high summer temperatures is tipping the young primocanes. The aim of the study was to investigate how this practice affects the fruit characteristics and primary and secondary metabolites of two primocane raspberry cultivars (‘Amira’ and ‘Polka’). For this purpose, we performed primocane tipping on two different dates in late spring and analyzed the berries from three subsequent sampling dates. High performance liquid chromatography-mass spectrometry (HPLC-MS) analyses were used for the identification and quantification of individual phenolic compounds and HPLC analyses for individual sugars and organic acids. Primocane tipping had great influence on the beginning of the harvest season of both cultivars. The impact on fruit yield was insignificant. Sampling date had a greater influence on fruit metabolite contents than did different treatments, with cultivar ‘Polka’ showing a greater response to primocane tipping than cultivar 'Amira'. Based on primary and secondary metabolites, it is difficult to say which treatment provided the best results, since dissimilar patterns were shown at different sampling dates and between cultivars. With negligible differences in fruit quality, primocane tipping was shown to be a good cultivation practice for delaying the production season of raspberries

Hot-water immersion does not increase postprandial muscle protein synthesis rates during recovery from resistance-type exercise in healthy, young males

The purpose of this study was to assess the impact of postexercise hot-water immersion on postprandial myofibrillar protein synthesis rates during recovery from a single bout of resistance-type exercise in healthy, young men. Twelve healthy, adult men (age: 23 ± 1 y) performed a single bout of resistance-type exercise followed by 20 min of water immersion of both legs. One leg was immersed in hot water [46°C: hot-water immersion (HWI)], while the other leg was immersed in thermoneutral water (30°C: CON). After water immersion, a beverage was ingested containing 20 g intrinsically L-[1-13C]-phenylalanine and L-[1-13C]-leucine labeled milk protein with 45 g of carbohydrates. In addition, primed continuous L-[ring-2H5]-phenylalanine and L-[1-13C]-leucine infusions were applied, with frequent collection of blood and muscle samples to assess myofibrillar protein synthesis rates in vivo over a 5-h recovery period. Muscle temperature immediately after water immersion was higher in the HWI compared with the CON leg (37.5 ± 0.1 vs. 35.2 ± 0.2°C; P < 0.001). Incorporation of dietary protein-derived L-[1-13C]-phenylalanine into myofibrillar protein did not differ between the HWI and CON leg during the 5-h recovery period (0.025 ± 0.003 vs. 0.024 ± 0.002 MPE; P = 0.953). Postexercise myofibrillar protein synthesis rates did not differ between the HWI and CON leg based upon L-[1-13C]-leucine (0.050 ± 0.005 vs. 0.049 ± 0.002%/h; P = 0.815) and L-[ring-2H5]-phenylalanine (0.048 ± 0.002 vs. 0.047 ± 0.003%/h; P = 0.877), respectively. Hot-water immersion during recovery from resistance-type exercise does not increase the postprandial rise in myofibrillar protein synthesis rates. In addition, postexercise hot-water immersion does not increase the capacity of the muscle to incorporate dietary protein-derived amino acids in muscle tissue protein during subsequent recovery

Ingestion of an ample amount of meat substitute based on a lysine-enriched,plant-based protein blend stimulates postprandial muscle proteinsynthesis to a similar extent as an isonitrogenous amount of chickenin healthy, young men

Plant-based proteins are considered to be less effective in their capacity to stimulate muscle protein synthesis when compared with animal-based protein sources, likely due to differences in amino acid contents. We compared the postprandial muscle protein synthetic response following the ingestion of a lysine-enriched plant-based protein product with an isonitrogenous amount of chicken. Twenty-four men (age 24 ± 5 years; BMI 22·9 ± 2·6 kg·m−2) participated in this parallel, double-blind, randomised controlled trial and consumed 40 g of protein as a lysine-enriched wheat and chickpea protein product (Plant, n 12) or chicken breast fillet (Chicken, n 12). Primed, continuous intravenous L-(ring-13C6)-phenylalanine infusions were applied while repeated blood and muscle samples were collected over a 5-h postprandial period to assess plasma amino acid responses, muscle protein synthesis rates and muscle anabolic signalling responses. Postprandial plasma leucine and essential amino acid concentrations were higher following Chicken (P < 0·001), while plasma lysine concentrations were higher throughout in Plant (P < 0·001). Total plasma amino acid concentrations did not differ between interventions (P = 0·181). Ingestion of both Plant and Chicken increased muscle protein synthesis rates from post-absorptive: 0·031 ± 0·011 and 0·031 ± 0·013 to postprandial: 0·046 ± 0·010 and 0·055 ± 0·015 % h−1, respectively (P-time < 0·001), with no differences between Plant and Chicken (time x treatment P = 0·068). Ingestion of 40 g of protein in the form of a lysine-enriched plant-based protein product increases muscle protein synthesis rates to a similar extent as an isonitrogenous amount of chicken in healthy, young men. Plant-based protein products sold as meat replacers may be as effective as animal-based protein sources to stimulate postprandial muscle protein synthesis rates in healthy, young individuals

PPARgamma activity in subcutaneous abdominal fat tissue and fat mass gain during short-term overfeeding

Objective: As the peroxisome proliferator-activated receptor (PPAR) plays a central role in fat mass regulation, we investigated whether initial subcutaneous PPAR activity is related to fat mass generation during overfeeding. Subjects: Fourteen healthy female subjects (age 254 years, BMI 22.12.3 kg/m2). Design and measurements: Subjects were overfed with a diet supplying 50% more energy than baseline energy requirements for 14 days. Fasting blood samples were analyzed for leptin, insulin and glucose. Fasting subcutaneous abdominal fat biopsies were obtained for analysis of PPAR1, PPAR2, aP2 and UCP2 mRNAs. Results: Initial PPAR1 and 2, aP2 and UCP2 mRNAs were not related to fat gain (P>0.12). However, PPAR1, PPAR2 and aP2 mRNA changes were positively related to changes in plasma leptin (

A single session of resistance exercise enhances insulin sensitivity for at least 24 h in healthy men.

The aim of the present study was to determine whether a single session of resistance exercise improves whole-body insulin sensitivity in healthy men for up to 24 h. Twelve male subjects (23 +/- 1 years) were studied over a period of 4 days during which they consumed a standardized diet, providing 0.16 +/- 0.01 MJ.kg(-1).day(-1) containing 15 +/- 0.1 energy% (En%) protein, 29 +/ -0.1 En% fat and 55 +/- 0.3 En% carbohydrate. Insulin sensitivity was determined 24 h before and 24 h after a single resistance exercise session (8 sets of 10 repetitions at 75% of 1 repetition maximum for two leg exercise tasks) using an intravenous insulin tolerance test. Insulin sensitivity index was calculated by the decline in arterial blood glucose concentration following intravenous administration of a single bolus of human insulin (0.075 IU.kg(-1) fat free mass). Basal glucose and insulin concentrations were not changed up to 24 h after the resistance exercise. However, a substantial 13+/-5% improvement in whole-body insulin sensitivity was observed, 24 h after the resistance exercise (P < 0.05). This study shows that even a single session of resistance exercise improves whole-body insulin sensitivity for up to 24 h in healthy men, which is consistent with earlier observations following endurance exercise tasks

Protein co-ingestion strongly increases postprandial insulin secretion in type 2 diabetes patients

The capacity of nutritional protein to induce endogenous insulin secretion has been well established. However, it is not known whether such a response is applicable in a diverse population of type 2 diabetes patients. The aim of the present study was to assess the impact of co-ingesting either intact or hydrolyzed protein with carbohydrate on postprandial plasma insulin and glucose responses in type 2 diabetes patients. Sixty longstanding, male, type 2 diabetes patients participated in a study in which we determined postprandial plasma insulin and glucose responses after ingesting a single bolus of carbohydrate (0.7 g/kg: CHO) with or without an intact protein (0.3 g/kg: PRO) or its hydrolysate (0.3 g/kg: PROh). Results showed that protein co-ingestion strongly increased postprandial insulin release, with the insulin response +99 ± 41 and +110 ± 10% greater in the CHO+PRO and CHO+PROh experiments when compared with the CHO experiment. The insulinotropic properties of protein co-ingestion were evident in nearly all patients, with 58 out of 60 patients responding >10% when compared with the insulin response following carbohydrate ingestion only (CHO). The concomitant plasma glucose responses were 22 ± 32 and 23 ± 36% lower in the CHO+PRO and CHO+PROh experiments, respectively. We conclude that protein co-ingestion represents an effective dietary strategy to strongly augment postprandial insulin release and attenuate the postprandial rise in glucose concentration in type 2 diabetes patients