Quantitative pathways for Northeast Atlantic fisheries based on climate, ecological–economic and governance modelling scenarios

Here we present quantitative projections of potential futures for ecosystems in the North Atlantic basin generated from coupling a climate change-driven biophysical model (representing ecosystem and fish populations under climate change) and a scenario-driven ecological–economic model (representing fleets and industries under economic globalization). Four contrasting scenarios (Baseline, Fortress, Global Commons, Free Trade) were defined from the perspective of alternative regional management and governance of the oceanic basin, providing pathways for the future of ecosystems in the Northeast Atlantic basin by 2040. Results indicate that in the time frame considered: (1) the effects of governance and trade decisions are more significant in determining outcomes than the effects of climate change alone, (2) climate change is likely to result in a poleward latitudinal shift of species ranges and thus resources, with implications for exploitation patterns, (3) the level of fisheries regulation is the most important factor in determining the long term evolution of the fisheries system, (4) coupling climate change and governance impacts demonstrates the complex interaction between different components of this social–ecological system, (5) an important driver of change for the future of the North Atlantic and the European fishing fleets appears to be the interplay between wild fisheries and aquaculture development, and finally (6) scenarios demonstrate that the viability and profit of fisheries industries is highly volatile. This study highlights the need to explore basin-scale policy that combines medium to long-term environmental and socio-economic considerations, and the importance of defining alternative sustainable pathways.

A Quantitative Investigation of Selected Reactions in the Fibrinolytic Cascade

Previous work has shown that thrombin activatable fibrinolysis inhibitor (TAFI) was unable to prolong lysis of purified clots in the presence of Lys-plasminogen (Lys-Pg), indicating a possible mechanism for fibrinolysis to circumvent prolongation mediated by activated TAFI (TAFIa). Therefore, the effects of TAFIa on Lys-Pg activation and Lys-plasmin (Lys-Pn) inhibition by antiplasmin (AP) were quantitatively investigated using a fluorescently labeled recombinant Pg mutant which does not produce active Pn. High molecular weight fibrin degradation products (HMW-FDPs), a soluble fibrin surrogate that models Pn modified fibrin, treated with TAFIa decreased the catalytic efficiency (kcat/Km) of 5IAF-Glu-Pg cleavage by 417-fold and of 5IAF-Lys-Pg cleavage by 55-fold. A previously devised intact clot system was used to measure the apparent second order rate constant (k2) for Pn inhibition by AP over time. While TAFIa was able to abolish the protection associated with Pn modified fibrin in clots formed with Glu-Pg, it was not able to abolish the protection in clots formed with Lys-Pg. However, TAFIa was still able to prolong the lysis of clots formed with Lys-Pg. TAFIa prolongs clot lysis by removing the positive feedback loop for Pn generation. The effect of TAFIa modification of the HMW-FDPs on the rate of tissue type plasminogen activator (tPA) inhibition by plasminogen activator inhibitor type 1 (PAI-1) was investigated using a previously devised end point assay. HMW-FDPs decreased the k2 for tPA inhibition rate by 3-fold. Thus, HMW-FDPs protect tPA from PAI-1. TAFIa treatment of the HMW-FDPs resulted in no change in protection. Vitronectin also did not appreciably affect tPA inhibition by PAI-1. Pg, in conjunction with HMW-FDPs, decreased the k2 for tPA inhibition by 30-fold. Hence, Pg, when bound to HMW-FDPs, protects tPA by an additional 10-fold. TAFIa treatment of the HMW-FDPs completely removed this additional protection provided by Pg. In conclusion, an additional mechanism was identified whereby TAFIa can prolong clot lysis by increasing the rate of tPA inhibition by PAI-1 by eliminating the protective effects of Pn-modified fibrin and Pg. Because TAFIa can suppress Lys-Pg activation but cannot attenuate Lys-Pn inhibition by AP, the Glu- to Lys-Pg/Pn conversion is able to act as a fibrinolytic switch to ultimately lyse the clot.