Effect of Intensive Training on Mood With No Effect on Brain-Derived Neurotrophic Factor

Purpose Monitoring mood state is a useful tool for avoiding non-functional overreaching (NFOR). Brain derived neurotrophic factor (BDNF) is implicated in stress-related mood disorders. The purpose of the present study was to investigate the impact of intensified training-induced mood disturbance on plasma BDNF concentrations at rest and in response to exercise.  Methods Eight cyclists performed 1 week of normal (NT), 1 week of intensified (INT) and 1 week of recovery (REC) training. Fasted blood samples were collected before and after exercise, on day 7 of each training week and were analyzed for plasma BDNF and cortisol concentrations. A 24-item Profile Of Mood State questionnaire was administered on day 7 of each training week and global mood score (GMS) was calculated. Results Time trial performance was impaired during INT (p=0.01) and REC (p=0.02) compared with NT. Basal plasma cortisol (NT=153±16 ng/ml, INT=130±11 ng/ml, REC=150±14 ng/ml) and BDNF (NT=484±122 pg/ml, INT=488±122 pg/ml, REC=383±56 pg/ml) concentrations were similar between training conditions. Likewise, similar exercise-induced increases in cortisol and BDNF concentrations were observed between training conditions. GMS was 32% greater during INTvs.NT (P<0.001). Conclusion Consistent with a state of functional overreaching (FOR), impairments in performance and mood state with INT were restored after one week of REC. These results support evidence that mood changes before plasma BDNF concentrations as a biochemical marker of FOR and that cortisol is not a useful marker for predicting FOR

Enhanced Lacto-Tri-Peptide Bio-Availability by Co-Ingestion of Macronutrients

Some food-derived peptides possess bioactive properties, and may affect health positively. For example, the C-terminal lacto-tri-peptides Ile-Pro-Pro (IPP), Leu-Pro-Pro (LPP) and Val-Pro-Pro (VPP) (together named here XPP) are described to lower blood pressure. The bioactivity depends on their availability at the site of action. Quantitative trans-organ availability/kinetic measurements will provide more insight in C-terminal tri-peptides behavior in the body. We hypothesize that the composition of the meal will modify their systemic availability. We studied trans-organ XPP fluxes in catheterized pigs (25 kg; n=10) to determine systemic and portal availability, as well as renal and hepatic uptake of a water-based single dose of synthetic XPP and a XPP containing protein matrix (casein hydrolyte, CasH). In a second experiment (n=10), we compared the CasH-containing protein matrix with a CasH-containing meal matrix and the modifying effects of macronutrients in a meal on the availability (high carbohydrates, low quality protein, high fat, and fiber). Portal availability of synthetic XPP was 0.08 ± 0.01% of intake and increased when a protein matrix was present (respectively 3.1, 1.8 and 83 times for IPP, LPP and VPP). Difference between individual XPP was probably due to release from longer peptides. CasH prolonged portal bioavailability with 18 min (absorption half-life, synthetic XPP: 15 ± 2 min, CasH: 33 ± 3 min, p<0.0001) and increased systemic elimination with 20 min (synthetic XPP: 12 ± 2 min; CasH: 32 ± 3 min, p<0.0001). Subsequent renal and hepatic uptake is about 75% of the portal release. A meal containing CasH, increased portal 1.8 and systemic bioavailability 1.2 times. Low protein quality and fiber increased XPP systemic bioavailability further (respectively 1.5 and 1.4 times). We conclude that the amount and quality of the protein, and the presence of fiber in a meal, are the main factors that increase the systemic bioavailability of food-derived XPP

Over-toasting dehulled rapeseed meal and soybean meal, but not sunflower seed meal, increases prececal nitrogen and amino acid digesta flows in broilers

Poorly digestible proteins may lead to increased protein fermentation in the ceca of broilers and hence, the production of potentially harmful metabolites. To evaluate effects of protein fermentation on gut health, an experimental contrast in ileal nitrogen (N) and amino acid (AA) flow is required. Therefore, our objective was to develop a model that creates a contrast in protein fermentation by increasing the prececal flow of protein within ingredients. To this end, we used additional toasting of protein sources and evaluated the effect on prececal N and AA flows. One-day-old Ross 308 male broilers (n = 480) were divided over 6 dietary treatments, with 8 replicate pens with 10 broilers each. Diets contained 20% of a regular soybean meal (SBM), high protein sunflower seed meal (SFM) or a dehulled rapeseed meal (dRSM) as is, or heat damaged by secondary toasting at 136°C for 20 min (tSBM, tSFM, or tdRSM). Ileal and total tract digesta flows of N and AA were determined with 5 birds per pen in their third week of life using an inert marker (TiO2) in the feed. Additional toasting increased the feed conversion ratio (FCR) only in birds fed dRSM (1.39 vs. 1.31), but not SBM and SFM (interaction P = 0.047). In SBM, additional toasting increased the flow of histidine, lysine, and aspartate through the distal ileum and excreted, while in SFM it had no effect on flows of N and AA. Toasting dRSM increased the prececal flows and excretion of N (862 vs 665 and 999 vs 761 mg/d, respectively) and of the AA. Of the ingredients tested, toasting dRSM is a suitable model to increase protein flows into the hind-gut, permitting the assessment of effects of protein fermentation

Protein fermentation in the gut; implications for intestinal dysfunction in humans, pigs, and poultry

The amount of dietary protein is associated with intestinal disease in different vertebrate species. In humans, this is exemplified by the association between high-protein intake and fermentation metabolite concentrations in patients with inflammatory bowel disease. In production animals, dietary protein intake is associated with postweaning diarrhea in piglets and with the occurrence of wet litter in poultry. The underlying mechanisms by which dietary protein contributes to intestinal problems remain largely unknown. Fermentation of undigested protein in the hindgut results in formation of fermentation products including short-chain fatty acids, branchedchain fatty acids, ammonia, phenolic and indolic compounds, biogenic amines, hydrogen sulfide, and nitric oxide. Here, we review the mechanisms by which these metabolites may cause intestinal disease. Studies addressing how different metabolites induce epithelial damage rely mainly on cell culture studies and occasionally on mice or rat models. Often, contrasting results were reported. The direct relevance of such studies for human, pig, and poultry gut health is therefore questionable and does not suffice for the development of interventions to improve gut health. We discuss a roadmap to improve our understanding of gut metabolites and microbial species associated with intestinal health in humans and production animals and to determine whether these metabolite/bacterial networks cause epithelial damage. The outcomes of these studies will dictate proof-of-principle studies to eliminate specific metabolites and or bacterial strains and will provide the basis for interventions aiming to improve gut health.</p

High-Intensity Training Reduces CD8+ T-cell Redistribution in Response to Exercise

Purpose: We examined whether exercise-induced lymphocytosis and lymphocytopenia are impaired with high-intensity training. Methods: Eight trained cyclists (V˙O2max = 64.2 &plusmn; 6.5 mL&middot;kg-1&middot;min-1) undertook 1 wk of normal-intensity training and a second week of high-intensity training. On day 7 of each week, participants performed a cycling task, consisting of 120 min of submaximal exercise followed by a 45-min time trial. Blood was collected before, during, and after exercise. CD8+ T lymphocytes (CD8+TLs) were identified, as well as CD8+TL subpopulations on the basis of CD45RA and CD27 expression. Results: High-intensity training (18,577 &plusmn; 10,984 cells per microliter &times; &sim;165 min) was associated with a smaller exercise-induced mobilization of CD8+TLs compared with normal-intensity training (28,473 &plusmn; 16,163 cells per microliter &times; &sim;165 min, P = 0.09). The response of highly cytotoxic CD8+TLs (CD45RA+CD27-) to exercise was smaller after 1 wk of high-intensity training (3144 &plusmn; 924 cells per microliter &times; &sim;165 min) compared with normal-intensity training (6417 &plusmn; 2143 cells per microliter &times; &sim;165 min, P &lt; 0.05). High-intensity training reduced postexercise CD8+TL lymphocytopenia (-436 &plusmn; 234 cells per microliter) compared with normal-intensity training (-630 &plusmn; 320 cells per microliter, P&nbsp;less than&nbsp;0.05). This was driven by a reduced egress of naive CD8+TLs (CD27+CD45RA+). High-intensity training was associated with reduced plasma epinephrine (-37%) and cortisol (-15%) responses (P&nbsp;less than&nbsp;0.05). Conclusions: High-intensity training impaired CD8+TL mobilization and egress in response to exercise. Highly cytotoxic CD8+TLs were primarily responsible for the reduced mobilization of CD8+TLs, which occurred in parallel with smaller neuroendocrine responses. The reduced capacity for CD8+TLs to leave blood after exercise with high-intensity training was accounted for primarily by naive, and also, highly cytotoxic CD8+TLs. This impaired CD8+TL redistribution in athletes undertaking intensified training may imply reduced immune surveillance

Seasonal variation in vitamin D status in elite athletes: a longitudinal study

Studies monitoring vitamin D status in athletes are seldom conducted for a period of 12 months or longer, thereby lacking insight into seasonal fluctuations. The objective of the cur-rent study was to identify seasonal changes in total 25-hydroxyvitamin D (25(OH)D) concen-tration throughout the year. Fifty-two, mainly Caucasian athletes with a sufficient 25(OH)D concentration (>75 nmol/L) in June were included in this study. Serum 25(OH)D concentra-tion was measured every three months (June, September, December, March, June). Addition-ally, vitamin D intake and sun exposure were assessed by questionnaires at the same time points. Highest total 25(OH)D concentrations were found at the end of summer (113±26 nmol/L), whereas lowest concentrations were observed at the end of winter (78±30 nmol/L). Although all athletes had a sufficient 25(OH)D concentration at the start of the study, nearly 20% of the athletes were deficient (<50 nmol/L) in late winter

Portal Drained Viscera fluxes of XPP—Effect of a protein matrix.

<p>Post-prandial portal drained viscera (PDV) fluxes after <i>intra-gastric</i> administration of tri-peptide (XPP) mixtures: control salt solution (Control), synthetic XPP’s (XPP), casein hydrolyte rich in XPP (CasH) or spiked CasH (CasH + XPP). A: Isoleucine-proline-proline (IPP). B: Leucine-proline-proline (LPP). C: Valine-proline-proline (VPP). Respective number of observations for Control, XPP, CasH and CasH +XPP are for graph A: n = 6, 9, 8 and 9; graph B: n = 6, 10, 9 and 9; graph C: n = 5, 9, 9 and 9. Values are mean ± SEM. Positive values is net release, negative values is net uptake. Statistics: repeated measures two-way ANOVA, mixed model, planned comparisons. All curves are significantly different from the XPP mixture: effect test mixture p<0.01; effect time p<0.01; interaction p<0.01</p

Composition of test mixtures—Study 1.

<p>¹⁾ Chemical purities of the IPP, LPP, and VPP synthetic products were 93.4, 95.0 and 98.7%, respectively (Bachem, Weil am Rhein, Switzerland).</p><p>²⁾ The given amounts of tri-peptides isoleucine-proline-proline (IPP), leucine-proline-proline (LPP), valine-proline-proline (VPP) in the casein hydrolysate (CasH, Casimax, DSM Food Specialties, Delft, The Netherlands). The casein hydrolysate contained 57% protein with 5.4, 16.5 and 0.3 mg/g protein of LPP, LPP and VPP, respectively.</p><p>³⁾ Total XPP = total amount of IPP, LPP and VPP.</p><p>Composition of test mixtures—Study 1.</p