Multiple roles of complement MASP-1 at the interface of innate immune response and coagulation

Dobó, József; Schroeder, Verena; Jenny, Lorenz; Cervenak, László; Závodszky, Péter; Gál, Péter (2014). Multiple roles of complement MASP-1 at the interface of innate immune response and coagulation. Molecular immunology, 61(2), pp. 69-78. Elsevier 10.1016/j.molimm.2014.05.013

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MASP-1 is a versatile serine protease that cleaves a number of substrates in human blood. In recent years it became evident that besides playing a crucial role in complement activation MASP-1 also triggers other cascade systems and even cells to mount a more powerful innate immune response. In this review we summarize the latest discoveries about the diverse functions of this multi-faceted protease. Recent studies revealed that among MBL-associated serine proteases, MASP-1 is the one responsible for triggering the lectin pathway via its ability to rapidly autoactivate then cleave MASP-2, and possibly MASP-3. The crystal structure of MASP-1 explains its more relaxed substrate specificity compared to the related complement enzymes. Due to the relaxed specificity, MASP-1 interacts with the coagulation cascade and the kinin generating system, and it can also activate endothelial cells eliciting pro-inflammatory signaling.

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