Mapping Southampton's food system: Towards a healthier and more sustainable future

This policy brief is the result of a collaboration between the University of Southampton School of Biological Sciences and Southampton City Council. This work intends to shine a light on food inequalities at a local level, mapping the food system and listening to the voices of the community to inform policy. Locally, almost 1 in 3 businesses in Southampton are part of the food system. These provide over 6,700 jobs and contribute up to £487.3 million to Southampton’s economy per year. However, over 40% of local people have reported experiencing food insecurity and rates of childhood obesity are significantly higher in Southampton than the average for England. The food system is also linked to a third of all human-caused greenhouse gas emissions. Therefore, we must act now to influence and improve the sustainability and health of our food system and deliver numerous economic, environmental and social co-benefits. The term ‘food system’ refers to the inter-connections between how we: produce, process, transport, buy, consume, and dispose of the food we eat and the way this affects us as individuals and communities. A food system is considered sustainable when it delivers food security and nutrition for all in such a way that the economic, social, and environmental bases to generate food security and nutrition for future generations are not compromised

Molecular investigation of the unfolded protein response in select human tauopathies

Background: Tauopathies are a group of neurodegenerative diseases associated with the accumulation of misfolded tau protein. The mechanisms underpinning tau-dependent proteinopathy remain to be elucidated. A protein quality control pathway within the endoplasmic reticulum, the unfolded protein response (UPR), has been suggested as a possible pathway modulating cellular responses in a range of neurodegenerative diseases, including those associated with misfolded cytosolic tau.Objective: In this study we investigated three different clinically defined tauopathies to establish whether these diseases are accompanied by the activation of UPR.Methods: We used PCR and western blotting to probe for the modulation of several reliable UPR markers in mRNA and proteins extracted from three distinct tauopathies: 20 brain samples from Alzheimer's disease patients, 11 from Pick's disease, and 10 from progressive supranuclear palsy. In each disease samples from these patients were compared with equal numbers of age-matched non-demented controls.Results: Our investigation showed that different markers of UPR are not changed at the late stage of any of the human tauopathies investigated. Interestingly, UPR signatures were often observed in non-demented controls.Conclusion: These data from late-stage human cortical tissue report an activation of UPR markers within the aged brain across all cohorts investigated and further support the emerging evidence that the accumulation of misfolded cytosolic tau does not drive a disease-associated activation of UPR.</p