Poor nutritional status of schoolchildren in urban and peri-urban areas of Ouagadougou (Burkina Faso)

<p>Abstract</p> <p>Background</p> <p>Malnutrition is still highly prevalent in developing countries. Schoolchildren may also be at high nutritional risk, not only under-five children. However, their nutritional status is poorly documented, particularly in urban areas. The paucity of information hinders the development of relevant nutrition programs for schoolchildren. The aim of this study carried out in Ouagadougou was to assess the nutritional status of schoolchildren attending public and private schools.</p> <p>Methods</p> <p>The study was carried out to provide baseline data for the implementation and evaluation of the Nutrition Friendly School Initiative of WHO. Six intervention schools and six matched control schools were selected and a sample of 649 schoolchildren (48% boys) aged 7-14 years old from 8 public and 4 private schools were studied. Anthropometric and haemoglobin measurements, along with thyroid palpation, were performed. Serum retinol was measured in a random sub-sample of children (N = 173). WHO criteria were used to assess nutritional status. Chi square and independent t-test were used for proportions and mean comparisons between groups.</p> <p>Results</p> <p>Mean age of the children (48% boys) was 11.5 ± 1.2 years. Micronutrient malnutrition was highly prevalent, with 38.7% low serum retinol and 40.4% anaemia. The prevalence of stunting was 8.8% and that of thinness, 13.7%. The prevalence of anaemia (p = 0.001) and vitamin A deficiency (p < 0.001) was significantly higher in public than private schools. Goitre was not detected. Overweight/obesity was low (2.3%) and affected significantly more children in private schools (p = 0.009) and younger children (7-9 y) (p < 0.05). Thinness and stunting were significantly higher in peri-urban compared to urban schools (p < 0.05 and p = 0.004 respectively). Almost 15% of the children presented at least two nutritional deficiencies.</p> <p>Conclusion</p> <p>This study shows that malnutrition and micronutrient deficiencies are also widely prevalent in schoolchildren in cities, and it underlines the need for nutrition interventions to target them.</p

Divergent Modulation of Proteostasis in Prostate Cancer

Ballar, Petek/0000-0002-6189-1818WOS: 000530838600006PubMed: 32274755Proteostasis regulates key cellular processes such as cell proliferation, differentiation, transcription, and apoptosis. the mechanisms by which proteostasis is regulated are crucial and the deterioration of cellular proteostasis has been significantly associated with tumorigenesis since it specifically targets key oncoproteins and tumor suppressors. Prostate cancer (PCa) is the second most common cause of cancer death in men worldwide. Androgens mediate one of the most central signaling pathways in all stages of PCa via the androgen receptor (AR). in addition to their regulation by hormones, PCa cells are also known to be highly secretory and are particularly prone to ER stress as proper ER function is essential. Alterations in various complex signaling pathways and cellular processes including cell cycle control, transcription, DNA repair, apoptosis, cell adhesion, epithelial-mesenchymal transition (EMT), and angiogenesis are critical factors influencing PCa development through key molecular changes mainly by posttranslational modifications in PCa-related proteins, including AR, NKX3.1, PTEN, p53, cyclin D1, and p27. Several ubiquitin ligases like MDM2, Siah2, RNF6, CHIP, and substrate-binding adaptor SPOP; deubiquitinases such as USP7, USP10, USP26, and USP12 are just some of the modifiers involved in the regulation of these key proteins via ubiquitin-proteasome system (UPS). Some ubiquitin-like modifiers, especially SUMOs, have been also closely associated with PCa. on the other hand, the proteotoxicity resulting from misfolded proteins and failure of ER adaptive capacity induce unfolded protein response (UPR) that is an indispensable signaling mechanism for PCa development. Lastly, ER-associated degradation (ERAD) also plays a crucial role in prostate tumorigenesis. in this section, the relationship between prostate cancer and proteostasis will be discussed in terms of UPS, UPR, SUMOylation, ERAD, and autophagy.Scientific and Technological Research Council of Turkey (TUBITAK)Turkiye Bilimsel ve Teknolojik Arastirma Kurumu (TUBITAK) [SBAG-108S056/114S062]; Ege University internal funds; BAGEP Award of the Science Academy; Pfizer-TurkeyPfizer; COST Action (PROTEOSTASIS)European Cooperation in Science and Technology (COST) [BM1307]; COST (European Cooperation in Science and Technology)European Cooperation in Science and Technology (COST)Work by PBK is supported by the Scientific and Technological Research Council of Turkey (TUBITAK, SBAG-108S056/114S062), Ege University internal funds, BAGEP Award of the Science Academy with funding supplied by Pfizer-Turkey, COST Action (PROTEOSTASIS BM1307), and by COST (European Cooperation in Science and Technology)

B meson decays to η(′)K*, η(′)ρ, η(′)π0, ωπ0, and φπ0

We present measurements of the branching fractions and charge asymmetries (where appropriate) of two-body B decays to η(′)K*, η(′)ρ, η(′)π0, ωπ0, and φπ0. The data were recorded with the BABAR detector at PEP-II and correspond to 89×106 BB̅ pairs produced in e+e- annihilation through the Υ(4S) resonance. We find significant signals for two decay modes and measure the branching fractions B(B+→ηK*+)=(25.6±4.0±2.4)×10-6 and B(B0→ηK*0)=(18.6±2.3±1.2)×10-6, where the first error is statistical and the second systematic. We also find evidence with significance 3.5σ for a third decay mode and measure B(B+→ηρ+)=(9.2±3.4±1.0)×10-6. For other channels, we set 90% C.L. upper limits of B(B0→ηρ0)<1.5×10-6, B(B+→η′K*+)<14×10-6, B(B0→η′K*0)<7.6×10-6, B(B+→η′ρ+)<22×10-6, B(B0→η′ρ0)<4.3×10-6, B(B0→ηπ0)<2.5×10-6, B(B0→η′π0)<3.7×10-6, B(B0→ωπ0)<1.2×10-6, and B(B0→φπ0)<1.0×10-6. For self-flavor-tagging modes with significant signals, the time-integrated charge asymmetries are Ach(ηK*+)=+0.13±0.14±0.02 and Ach(ηK*0)=+0.02±0.11±0.02