Virtual Water as a Metric for Institutional Sustainability

Carbon and nitrogen footprints are increasingly common metrics used to consider the environmental impacts of activities and consumption by institutions; an institutional water footprint complements these assessments by providing a third metric: water use. This study calculated the water footprint of the University of Virginia (UVA) as a summation of direct water use and virtual water use. The latter was estimated using purchasing records for utilities, food, transportation, paper, research animals, and hospital purchases for calendar year 2014. The direct water use portion of the footprint was 1.7 million m3 water. The virtual water footprint was 15.2 million m3. The utilities sector is responsible for 46 percent of UVA's total water footprint, and food production 23 percent. The UVA Health System contributed 17 percent, and paper, transportation, and research animals each constituted less than 3 percent of the total footprint. The most water-intensive inputs were biofuels, hydroelectricity, and animal products. This water footprint assessment supports carbon and nitrogen footprint-reduction strategies, such as replacing coal with natural gas and reducing beef consumption. Water footprints also require explicitly considering the impacts of renewable energy sources, such as biofuels or hydropower. The water footprint of the University of Virginia provides an additional measure to address the environmental implications of the institution's resource demands and this approach is broadly applicable to other institutions

Relaxed specificity of matrix metalloproteinases (MMPS) and TIMP insensitivity of tumor necrosis factor-alpha (TNF-alpha) production suggest the major TNF-alpha converting enzyme is not an MMP.

Tumor necrosis factor-alpha is released from cells by a proteolytic cleavage. Previous work suggested that a specific, non-matrix metalloproteinase carries out this cleavage, but matrix metalloproteinases have also been implicated. In this paper, we report that none of the matrix metalloproteinases tested cleaved peptide substrates as specifically as the non-matrix metalloproteinase. A matrix metalloproteinase did process tumor necrosis factor-alpha extracted from COS cells, but neither tissue inhibitor of metalloproteinases-1 nor -2 blocked tumor necrosis factor-alpha processing by human monocytes. Moreover, tissue inhibitor of metalloproteinases-1 had at most a partial effect on the in vivo release of the cytokine in mice. We conclude that a non-matrix metalloproteinase is the major physiological tumor necrosis factor-alpha convertase