| First Author | Ruseva MM | Year | 2014 |
| Journal | Clin Exp Immunol | Volume | 176 |
| Issue | 1 | Pages | 84-92 |
| PubMed ID | 24279761 | Mgi Jnum | J:209080 |
| Mgi Id | MGI:5565642 | Doi | 10.1111/cei.12244 |
| Citation | Ruseva MM, et al. (2014) C3 dysregulation due to factor H deficiency is mannan-binding lectin-associated serine proteases (MASP)-1 and MASP-3 independent in vivo. Clin Exp Immunol 176(1):84-92 |
| abstractText | Uncontrolled activation of the complement alternative pathway is associated with complement-mediated renal disease. Factor B and factor D are essential components of this pathway, while factor H (FH) is its major regulator. In complete FH deficiency, uncontrolled C3 activation through the alternative pathway results in plasma C3 depletion and complement-mediated renal disease. These are dependent on factor B. Mannan-binding lectin-associated serine proteases 1 and 3 (MASP-1, MASP-3) have been shown recently to contribute to alternative pathway activation by cleaving pro-factor D to its active form, factor D. We studied the contribution of MASP-1 and MASP-3 to uncontrolled alternative pathway activation in experimental complete FH deficiency. Co-deficiency of FH and MASP-1/MASP-3 did not ameliorate either the plasma C3 activation or glomerular C3 accumulation in FH-deficient mice. Our data indicate that MASP-1 and MASP-3 are not essential for alternative pathway activation in complete FH deficiency. |
