EC Number   |
General Information |
Reference |
|---|
   3.4.21.104 | metabolism |
MASP-2 is the initiating protease of the lectin pathway |
718122 |
| 3.4.21.104 | physiological function |
effect of MASP-2 deficiency in an isogenic mouse model of renal transplantation. Wild-type kidneys grafted into wild-type recipients develop acute renal failure. Wild-type grafts transplanted into MASP-2-deficient recipients show significantly better kidney function, less C3 deposition, and less ischemia reperfusion injury. In the absence of donor or recipient complement C4, the wild-type to wild-type phenotype is preserved, indicating that the MASP-2-mediated damage is independent of C4 activation. In mice deficient for both MASP-2 and C4, the protection from postoperative acute renal failure is no greater than in mice with MASP-2 deficiency alone. Injury occurs through MASP-2-dependent activation events independent of C4 |
731780 |
| 3.4.21.104 | physiological function |
lectin pathway activation by Trypanosoma cruzi requires the MASP2 activity resulting in C2 complement factor cleavage |
709985 |
| 3.4.21.104 | physiological function |
mannan-binding lectin-associated serine proteases MASP-1 and MASP-2 can readily form heterodimers after dissociation and re-association, however, in thepresence of Ca2+ exchange of subunits is slow between the homodimers. Modeling of isoforms MASP-1:MASP-3 heterodimer formation indicates that subunits of these proteins are readily exchanged even in the presence of Ca2+ |
732518 |
| 3.4.21.104 | physiological function |
MASP-2 acts as acute-phase reactant, but it is neither marker for severity, multiorgan failure, nor for mortality in acute pancreatitis. MASP-2 plays only a minor role in the inflammatory response in acute pancreatitis |
718181 |
| 3.4.21.104 | physiological function |
MASP-2 is not an activator of complement factor D |
754326 |
| 3.4.21.104 | physiological function |
MASP-2 is the main initiator of the lectin complement pathway by cleaving C4 and C2 to form the C4b2a complex leading to further downstream complement activation |
709160 |
| 3.4.21.104 | physiological function |
the addition of mannan-binding lectin or ficolins allows the formation of serine proteases MASP-1-MASP-2 co-complexes. Such co-complexes have a functional role in activating complement and are present in serum at varying levels, impacting on the degree of complement activation. MASP-2 can be found in complex with each of the other MASPs and mannan-binding lectin-associated proteins in serum, and coexpression of MASP-2 with MASP-1, MASP-3, or mannan-binding lectin-associated protein 4 leads to detectable levels of heterodimers |
732265 |
| 3.4.21.104 | physiological function |
the MBL-MASP pathway of complement activation is of importance to innate immunity and to response to pathogens |
708201 |
| 3.4.21.104 | physiological function |
two areas outside of the active site of MASP-2 (so-called exosites) are crucial for efficient cleavage of substrate C4 complement component. Both exosites are required for high affinity binding and efficient cleavage of the substrate protein. Within the SP domain exosite, two arginine residues are most important for high affinity binding and efficient cleavage of C4. The CCP domain exosite appears to play the major role in the initial interaction with C4, whilst the SP domain exosite plays the major role in a secondary conformational change between the two proteins required to form a high affinity complex |
754748 |
