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Péter Gál, József Dobó, Gábor Pál, Comment on “Cutting Edge: Role of MASP-3 in the Physiological Activation of Factor D of the Alternative Complement Pathway”, The Journal of Immunology, Volume 203, Issue 12, December 2019, Page 3091, https://doi.org/10.4049/jimmunol.1901055
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We read with great interest the article by Hayashi et al. (1), in which the authors report the generation of two new mouse strains, specifically deficient in MASP-1 or MASP-3. In their study, the authors demonstrated in mice that MASP-1 is indispensable for lectin pathway activation, and MASP-3 is responsible for proteolytic processing of zymogen FD (pro-FD) to FD, the initiating protease of the alternative pathway.
The authors’ findings in these mouse models are in perfect agreement with our previous results obtained with human whole blood, plasma, and serum samples using specific human MASP-1, MASP-2, and MASP-3 inhibitors developed by directed evolution (2, 3). In our prior studies, we showed that a monospecific MASP-1 inhibitor completely prevented lectin pathway activation (2). Using a specific MASP-3 inhibitor, we also demonstrated that MASP-3 is the exclusive activator of pro-FD in resting human blood (3). A publication by another research group also highlighted the important role of MASP-3 in pro-FD activation (4).
