| First Author | Hayashi M | Year | 2019 |
| Journal | J Immunol | Volume | 203 |
| Issue | 6 | Pages | 1411-1416 |
| PubMed ID | 31399515 | Mgi Jnum | J:279043 |
| Mgi Id | MGI:6360371 | Doi | 10.4049/jimmunol.1900605 |
| Citation | Hayashi M, et al. (2019) Cutting Edge: Role of MASP-3 in the Physiological Activation of Factor D of the Alternative Complement Pathway. J Immunol 203(6):1411-1416 |
| abstractText | The complement system, a part of the innate immune system, can be activated via three different pathways. In the alternative pathway, a factor D (FD) plays essential roles in both the initiation and the amplification loop and circulates as an active form. Mannose-binding lectin-associated serine proteases (MASPs) are key enzymes of the lectin pathway, and MASP-1 and/or MASP-3 are reported to be involved in the activation of FD. In the current study, we generated mice monospecifically deficient for MASP-1 or MASP-3 and found that the sera of the MASP-1-deficient mice lacked lectin pathway activity, but those of the MASP-3-deficient mice lacked alternative pathway activity with a zymogen FD. Furthermore, the results indicate that MASP-3 but not MASP-1 activates the zymogen FD under physiological conditions and MASP-3 circulates predominantly as an active form. Therefore, our study illustrates that, in mice, MASP-3 orchestrates the overall complement reaction through the activation of FD. |
