Abstract
Mannose-binding lectin-associated serine proteases (MASPs) are important elements of innate immunity. MASP-1 and MASP-2 are responsible for the activation of the lectin pathway of the complement system, while MASP-3 is indispensable for alternative pathway activation. Beside its action in complement activation, MASP-1 also cleaves other substrates in the blood boosting the innate immune response. MASP-1 can stimulate endothelial cells by cleaving the protease activated receptors (PARs) bridging the humoral and cellular immunity. MASP-1 also has a pivotal role in the cross-talk between the complement and the coagulation system. MASP-1 and MASP-2 are regulated by serpins (C1-inhibitor and antithrombin) whereas MASP-3 has no known natural inhibitor in the circulation. In this chapter we summarize our current knowledge about the physiological role of MASPs and also discuss the open questions and future directions of research in this field.
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Gál, P., Dobó, J. (2021). Activities of MASPs, The Complement Proteases Associated with Collectins and Ficolins. In: Kishore, U., Madan, T., Sim, R.B. (eds) The Collectin Protein Family and Its Multiple Biological Activities. Springer, Cham. https://doi.org/10.1007/978-3-030-67048-1_3
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