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Bone research is limited by the methods available for detecting changes in bone metabolism. While dual X-ray absorptiometry is rather insensitive, biochemical markers are subject to significant intra-individual variation. In the study presented here, we evaluated the isotopic labeling of bone using 41Ca, a long-lived radiotracer, as an alternative approach. After successful labeling of the skeleton, changes in the systematics of urinary 41Ca excretion are expected to directly reflect changes in bone Ca metabolism. A minute amount of 41Ca (100nCi) was administered orally to 22 postmenopausal women. Kinetics of tracer excretion were assessed by monitoring changes in urinary 41Ca/40Ca isotope ratios up to 700days post-dosing using accelerator mass spectrometry and resonance ionization mass spectrometry. Isotopic labeling of the skeleton was evaluated by two different approaches: (i) urinary 41Ca data were fitted to an established function consisting of an exponential term and a power law term for each individual; (ii) 41Ca data were analyzed by population pharmacokinetic (NONMEM) analysis to identify a compartmental model that describes urinary 41Ca tracer kinetics. A linear three-compartment model with a central compartment and two sequential peripheral compartments was found to best fit the 41Ca data. Fits based on the use of the combined exponential/power law function describing urinary tracer excretion showed substantially higher deviations between predicted and measured values than fits based on the compartmental modeling approach. By establishing the urinary 41Ca excretion pattern using data points up to day 500 and extrapolating these curves up to day 700, it was found that the calculated 41Ca/40Ca isotope ratios in urine were significantly lower than the observed 41Ca/40Ca isotope ratios for both techniques. Compartmental analysis can overcome this limitation. By identifying relative changes in transfer rates between compartments in response to an intervention

1. The stability of tryptophan was evaluated in several different food model systems using a chemical method (high pressure liquid chromatography after alkaline-hydrolysis) and rat assays. Losses of tryptophan were compared with the losses of lysine and methionine. 2. Whey proteins stored in the presence of oxidizing lipids showed large losses of lysine and extensive methionine oxidation but only minor losses of tryptophan as measured chemically. The observed decrease in bioavailable tryptophan was explained by a lower protein digestibility. 3. Casein treated with hydrogen peroxide to oxidize all methionine to methionine sulphoxide showed a 9% loss in bioavailable tryptophan. 4. When casein was reacted with caffeic acid at pH 7 in the presence of monophenol monooxygenase (tyrosinase; EC 1.14.18.l), no chemical loss of tryptophan occurred, although fluorodinitrobenzene-reactive lysine fell by 23%. Tryptophan bioavailability fell IS%, partly due to an 8% reduction in protein digestibility. 5. Alkali-treated casein (0.15 M-sodium hydroxide, 80°,4 h) did not support rat growth. Chemically-determined tryptophan, available tryptophan and true nitrogen digestibility fell 10, 46 and 23% respectively. Racemization of tryptophan was found to be 10% (D/(D+L)). 6. In whole-milk powder, which had undergone ‘early' or ‘advanced' Maillard reactions, tryptophan, determined chemically or in rat assays, was virtually unchanged. Extensive lysine losses occurred. 7. It was concluded that losses of tryptophan during food processing and storage are small and of only minor nutritional importance, especially when compared with much larger losses of lysine and the more extensive oxidation of methionine

1. The reactions between protein-bound amino acids and oxidizing lipid were investigated in a whey protein-methyl linolenate (C18.3)-water model system. The extent of fat oxidation was followed by measuring oxygen uptake, hydroperoxide formation and hydrocarbon (ethane and pentane) formation. 2. Significant losses occurred with lysine (up to 71 %), tryptophan (up to 31 %) and histidine (up to 57%). Methionine was extensively oxidized to its sulphoxide but less than 2% was further oxidized to the sulphone. No other amino acids were affected. 3. Increasing storage temperature (20°, 37°, 55°) resulted in an enhancement of fat oxidation reactions and amino acid degradation. 4. Increasing water activity (0.28, 0.65, 0.90) increased losses of lysine and tryptophan but had no influence on the oxidation of methionine, the level of remaining hydroperoxides or 02 uptake. Hydrocarbons were decreased. 5. Limitation of 02 uptake to 1 mol/mol lipid instead of excess 02 (02 uptake about 2.5 mol/mol lipid in 4 weeks) significantly reduced the degradation of lysine and tryptophan but had less influence on the oxidation of methionine. The level of remaining hydroperoxides was increased but hydrocarbons were unaffected

1. Storage of milk powder under unfavourable conditions accelerates the normally slow deterioration in nutritional quality. The effects of such storage on the water-soluble vitamin composition were examined. 2. (a) Spray-dried whole milk containing 25 g water/kg was stored at 60° and 70° and sampled weekly to 9 weeks. (b) Spray-dried whole milk and skimmed milk were adjusted to contain 40 and 100 g water/kg and stored at 37° in nitrogenand in oxygen. Samples were taken for analysis at intervals during storage. 3. The samples were analysed for eight B-complex vitamins and ascorbic acid, and also for total lysine, ‘reactive lysine' and ‘lysine as lactulosyl-lysine'. 4. Storage at 60° caused rapid destruction of folic acid (53% loss at 4 weeks) and slower loss of thiamin, vitamin B6 and pantothenic acid (18% at 8 weeks). There was no change in the content of riboflavin, biotin, nicotinic acid and vitamin B12. At 70° the rate of destruction of the four labile vitamins was much increased; 18% or less survived at 4 weeks. 5. At 37° and 40 g water/kg there was little change in total and ‘reactive' lysine during storage for 57 d. Lactulosyl-lysine was demonstrably present butatlow concentration. There was considerable loss of folate (72%) and ascorbate (91%) during storage for 30 d in O2, but no significant loss in N2. Thiamin fell by approximately 12% in 57 d, equally in O2 and N2. The content of the remaining vitamins was unchanged. At 100 g water/kg there were progressive Maillard changes. During 27 d in N2 the colour changed from cream to palebrown, but in O2 there was no perceptible colour change. Total lysine fell by 20% in 27 d, and ‘reactive lysine' by 30%. Folate was stable during 16 d in N2, but largely (94%) destroyed in O2. Ascorbic acid was also destroyed in N2 as in O2. Thiamin fell by 41% in 27 d, equally in O2 and N2. Vitamin B6 was more labile, especially in N2, falling by 71% in 16d. 6. With skimmed-milk powder containing 100 g water/kg, storage at 37° in

1. Whole-milk powders containing 25 g water/kg were stored for up to 9 weeks in sealed aluminium containers at elevated temperatures. Lysine and other essential amino acids were measured by chemical and microbiological methods. 2. Storage at 60° resulted in the progressive formation of lactulosyl-lysine. After 9 weeks, 30% of the lysine groups were present in this form. The powders still retained their natural colour and the levels of tryptophan, methionine, cyst(e)ine and leucine remained unchanged. 3. Storage at 70° resulted in the formation of lactulosyl-lysine followed by its complete degradation with the development of browning. Available tryptophan, methione, leucine and isoleucine decreased progressively during storage. 4. The different methods for lysine determination gave widely dissimilar results. The direct fluorodinitrobenzene (FDNB) technique and reactive lysine from furosine were considered to be the most reliable methods. The FDNB-difference, dye-binding lysine, Tetrahymena and Pediococcus methods all seriously underestimated reactive or available lysine in heat-damaged milk powders. Tetrahymena and Pediococcus appeared to utilize lactulosyl-lysine as a source of lysine. 5. The results are discussed in relation to storage and distribution of milk powders in hot climates

1. Tryptophan losses in stored milk powders and in different model systems representing the major reactions of food proteins during processing and storage were determined using four different chemical methods and in a rat assay. 2. Similar tryptophan values were obtained by the three chemical methods which included high pressure liquid chromatography (HPLC) after sodium hydroxide hydrolysis. colorimetric reaction with p-dimethylamino- benzaldehyde (p-DAB) after barium hydroxide hydrolysis, and fluorescence of the Norharman derivative after NaOH hydrolysis. 3. Tryptophan losses in the treated proteins as measured by the alkaline-hydrolysis methods were generally smaller than those determined by the rat assay. Good agreement however was obtained when the chemical value was multiplied by the true nitrogen digestibility. 4. Determination of tryptophan by reaction with p-DAB after papain (EC 3.4.22.2) digestion gave lower values in the processed proteins than the other chemical methods or the rat assay. 5. A method using alkaline-hydrolysis is recommended, preferably combined with HPLC-measurement of the liberated tryptophan

Paramount among the challenges to our ability to address the role of food and nutrition in health promotion and disease prevention is how to design and implement context-specific interventions and guidance. The Integration to Effective Implementation (I-to-I) concept is intended to address the complexities of the global health context through engagement of the continuum of stakeholders involved in the food and nutrition enterprise. The 2014 Micronutrient Forum (MNF) Global Conference held in Addis Ababa, Ethiopia, in June 2014 offered the opportunity to apply the I-to-I approach with the use of current concerns about the safety and effectiveness of interventions to prevent and treat iron deficiency (ID) as a case study. ID is associated with a range of adverse outcomes, especially in pregnant and nonpregnant women, infants, and primary school-age children. Strategies to combat ID include iron supplementation, multiple micronutrient powders, and food-based interventions to enhance dietary iron intake. Recent reports indicate potential increased adverse risks when iron is provided in areas with high infection burdens (e.g., malaria). This paradox has weakened iron intervention programs. Furthermore, the selection and interpretation of available biomarkers for assessing iron nutrition have been found to be compromised by the inflammatory process. These issues highlight the need for a comprehensive approach that considers basic biology, assessment, interventions, and how these can be translated into appropriate programs and policies. The application of the I-to-I with the use of the MNF offered an opportunity to explore how that might be achieved.

Reducing the size of low-solubility iron (Fe)-containing compounds to nanoscale has the potential to improve their bioavailability. Because Fe and zinc (Zn) deficiencies often coexist in populations, combined Fe/Zn-containing nanostructured compounds may be useful for nutritional applications. Such compounds are developed here and their solubility in dilute acid, a reliable indicator of iron bioavailability in humans, and sensory qualities in sensitive food matrices are investigated. Phosphates and oxides of Fe and atomically mixed Fe/Zn-containing (primarily ZnFe(2)O(4))nanostructured powders were produced by flame spray pyrolysis (FSP). Chemical composition and surface area were systematically controlled by varying precursor concentration and feed rate during powder synthesis to increase solubility to the level of ferrous sulfate at maximum Fe and Zn content. Solubility of the nanostructured compounds was dependent on their particle size and crystallinity. The new nanostructured powders produced minimal color changes when added to dairy products containing chocolate or fruit compared to the changes produced when ferrous sulfate or ferrous fumarate were added to these foods. Flame-made Fe- and Fe/Zn-containing nanostructured powders have solubilities comparable to ferrous and Zn sulfate but may produce fewer color changes when added to difficult-to-fortify foods. Thus, these powders are promising for food fortification and other nutritional applications.

BACKGROUND: Obesity increases the risk for iron deficiency, but the underlying mechanism is unclear. It is possible that overweight individuals may have lower dietary iron intake and/or bioavailability. Alternatively, obesity-related inflammation may increase hepcidin concentrations and reduce iron availability. Circulating hepcidin levels have not been compared in normal weight vs overweight individuals. OBJECTIVE: The objective of this study was to compare iron status, dietary iron intake and bioavailability, as well as circulating levels of hepcidin, leptin and interleukin-6 (IL-6), in overweight vs normal weight children. DESIGN: In 6-14-year-old normal and overweight children (n=121), we measured dietary iron intake, estimated iron bioavailability and determined body mass index s.d. scores (BMI-SDS). In all children (n=121), we measured fasting serum ferritin, soluble transferrin receptor (sTfR), C-reactive protein (CRP) and leptin; in a subsample, we measured IL-6 (n=68) and serum hepcidin (n=30). RESULTS: There were no significant differences in dietary iron intake or bioavailability comparing normal and overweight children. The prevalence of iron-deficient erythropoiesis (an increased sTfR concentration) was significantly higher in the overweight than in the normal weight children (20 vs 6%, P=0.022, with sTfR concentrations of 4.40+/-0.77 and 3.94+/-0.88 mg l(-1), respectively, P=0.010). Serum hepcidin levels were significantly higher in the overweight children (P=0.001). BMI-SDS significantly correlated with sTfR (P=0.009), serum hepcidin (P=0.005) and the three measures of subclinical inflammation, namely CRP (P<0.001), IL-6 (P<0.001) and leptin (P<0.001). In a multiple regression model, serum hepcidin was correlated with BMI-SDS (P=0.020) and body iron (P=0.029), but not with the inflammatory markers. CONCLUSION: Our findings indicate that there is reduced iron availability for erythropoiesis in overweight children and that this is unlikely due to low di

OBJECTIVE: Deficiencies of vitamin A and iodine are common in many developing countries. Vitamin A deficiency (VAD) may adversely affect thyroid metabolism. The study aim was to investigate the effects of concurrent vitamin A and iodine deficiencies on the thyroid-pituitary axis in rats. DESIGN: Weanling rats (n = 56) were fed diets deficient in vitamin A (VAD group), iodine (ID group), vitamin A and iodine (VAD + ID group), or sufficient in both vitamin A and iodine (control) for 30 days in a pair-fed design. Serum retinol (SR), thyroid hormones (FT(4), TT(4), FT(3), and TT(3)), serum thyrotropin (TSH), pituitary TSHbeta mRNA expression levels, and thyroid weights were determined at the end of the depletion period. MAIN OUTCOME: Compared to the control and ID groups, SR concentrations were about 35% lower in the VAD and VAD + ID groups (p < 0.001), indicating moderate VA deficiency. Comparing the VAD and control groups, there were no significant differences in TSH, TSHbeta mRNA, thyroid weight, or thyroid hormone levels. Compared to the control group, serum TSH, TSHbeta mRNA, and thyroid weight were higher (p < 0.05), and FT4 and TT4 were lower (p < 0.001), in the VAD + ID and ID groups. Compared to the ID group, TSH, TSHbeta mRNA, and thyroid weight were higher (p < 0.01) and FT(4) and TT(4) were lower (p < 0.001) in the VAD + ID group. There were no significant differences in TT3 or FT3 concentrations among groups. CONCLUSION: Moderate VAD alone has no measurable effect on the pituitary-thyroid axis. Concurrent ID and VAD produce more severe primary hypothyroidism than ID alone.