Complement system (via mannose-binding lectin-associated serine proteases activation) (null)

The complement system is a critical component of the innate immune response, with three major activation pathways: classical, lectin, and alternative. The mannan-binding lectin–associated serine proteases (MASPs)—especially MASP-1, MASP-2, and MASP-3—are serine protease enzymes that mediate the lectin pathway, serving as key activators upon recognition of pathogen-associated ligands. Specifically, MASP-2 cleaves C4 and C2 to generate C3 convertase, driving formation of downstream effector complexes, while MASP-1 and MASP-3 regulate this pathway and can also activate the alternative pathway indirectly by activating complement factor D[1][3][4][5]. Dysregulation of MASPs or aberrant lectin pathway activity is implicated in a range of inflammatory and autoimmune diseases, and they are emerging as potential therapeutic targets for complement-driven pathology. For structured data systems, it is preferable to list the individual MASPs (MASP-1, MASP-2, MASP-3) as explicit targets rather than the vague “complement system via MASPs activation.”

Other names

Lectin pathway of complement activationMannan-binding lectin–associated serine proteases (MASPs) pathwayMASP-1, MASP-2, MASP-3

Inhibition of MASP-2: Blocks cleavage of C4 and C2, preventing lectin pathway activation and downstream complement cascade. Inhibition of MASP-3: Prevents activation of complement factor D, reducing alternative pathway activity.