Exploring the long-term sustainability of school-based nutrition and food programs: What works, where and why?

ISSUE ADDRESSED: Most food and nutrition programs cease within 2 years. Understanding the determinants of program sustainability is crucial to maximise output from funding, whilst allowing sufficient time for program benefits to be achieved. This study applied the Consolidated Framework for Implementation Research (CFIR) to map the barriers and enablers of successful long-term implementation of school-based nutrition and food programs. METHODS: Qualitative methods with purposive and snowball sampling were used to recruit experts who were identified as being influential in implementing and sustaining long-term (>2 years) school-based food and nutrition programs. Semi-structured interviews with global experts were conducted, transcribed verbatim and coded deductively (by applying the CFIR constructs) and inductively when required. Thematic analysis informed the development of themes. RESULTS: Interviews were conducted with 11 experts including researchers, government employees, and a consultant of an international agency, from seven countries. Forty-eight deductive codes and eight inductive codes identified six main themes: (1) funding and integrity of its source; (2) political landscape; (3) nutrition policies and their monitoring; (4) involvement of community actors; (5) adaptability of the program and (6) effective program evaluation. Themes related mainly to the 'outer setting' domain of the CFIR. CONCLUSIONS: The CFIR highlighted pertinent factors that influence the successful long-term implementation of school-based food and nutrition programs. SO WHAT?: The findings suggest that to sustain program implementation beyond its initial funding, relationships across government departments, local organisations and communities, need to be nurtured and prioritised from the outset.

Inverted U-shaped associations between serum uric acid and fasting - plasma glucose level in non-diabetic, pre-diabetic, and diabetic adults: A population-based study in China.

OBJECTIVE: This study was designed to examine the correlation between serum uric acid (SUA) and fasting plasma glucose (FPG) levels across non-diabetic, pre-diabetic, and diabetic adults from Northwest China. MATERIALS AND METHODS: This study utilized data from a cross-sectional survey conducted in Ningxia Hui Autonomous Region, which investigated the prevalence and risk factors of cardiovascular disease. All subjects underwent tests for SUA and FPG levels. Generalized additive models and two-piecewise linear regression models were applied to explore the relationships between SUA and FPG level. The triglyceride-glucose (TyG) index was examined as a measure of insulin resistance, with an analysis of its mediating effects on the association between SUA and FPG level. RESULTS: A total of 10,217 individuals aged 18 and over were included. Generalized additive models verified the inverted U-shaped association between SUA and FPG levels, and the inflection points of FPG levels in the curves were 6.5 mmol/L in males and 8.8 mmol/L in females. The TyG index is an intermediate variable in the relationship between SUA levels and elevated FPG levels, with mediating effects of 12.82% (P < 0.001) for males and 34.02% (P < 0.001) for females. CONCLUSIONS: An inverted U-shaped association between FPG and SUA levels was observed in both genders. The threshold of FPG level was lower in males than in females. The relationship between these variables seems to be partially mediated by serum insulin levels.

Reversible domain closure modulates GlnBP ligand binding affinity.

Glutamine binding protein (GlnBP) is an Escherichia Coli periplasmic binding protein, which binds and carries glutamine to the inner membrane ATP-binding cassette (ABC) transporter. GlnBP binds the ligand with affinity around 0.1µM measured by isothermal titration calorimetry (ITC) and ligand binding stabilizes protein structure shown by its increase in thermodynamic stability. However, the molecular determinant of GlnBP ligand binding is not known. Electrostatic and hydrophobic interaction between GlnBP and glutamine are critical factors. We propose that the freedome of closure movement is also vital for ligand binding. In order to approve this hypothesis, we generate a series of mutants with different linker length that has different magnitude of domain closure. Mutants show different ligand binding affinity, which indicates that the propensity of domain closure determines the ligand binding affinity. Ligand binding triggers gradual ensemble conformational change. Structural changes upon ligand binding are monitored by combination of small angle x-ray scattering (SAXS) and NMR spectroscopy. Detailed structure characterization of GlnBP contributes to a better understanding of ligand binding and provides the structural basis for biosensor design.