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

Dobó, József and Schroeder, Verena and Jenny, Lorenz and Cervenak, László and Závodszky, Péter and 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. ISSN 0161-5890

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Abstract

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. © 2014 Elsevier Ltd. All rights reserved.

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