Complement component 5a des-arginine (C5a des-Arg)

Complement component 5a des-arginine (C5a des-Arg) is the primary metabolite of the potent anaphylatoxin C5a, formed by the rapid removal of the C-terminal arginine residue by serum carboxypeptidases such as carboxypeptidase N. While historically considered a significantly less potent form of C5a, recent research has established its role as a high-affinity ligand for the C5aR2 (C5L2) receptor and a partial agonist for the C5aR1 (CD88) receptor, contributing to the propagation of inflammatory responses. C5a des-Arg is a key mediator in the pathogenesis of severe inflammatory conditions, including sepsis, acute respiratory distress syndrome (ARDS), and rheumatoid arthritis, where it promotes leukocyte recruitment, cytokine release, and vascular permeability. Therapeutic strategies targeting C5a des-Arg, such as the monoclonal antibody vilobelimab, aim to neutralize its pro-inflammatory effects while sparing the terminal complement pathway's ability to form the membrane attack complex (MAC). This targeted approach potentially offers a superior safety profile compared to broad C5 inhibitors by maintaining the host's essential lytic defense mechanisms against bacterial pathogens.

Other names

C5a-desArgDesarginated C5aC5a(desArg)Complement component C5a des-Arg

Neutralization of the anaphylatoxin to prevent its interaction with C5a receptors (C5aR1 and C5aR2), thereby inhibiting downstream inflammatory signaling and leukocyte activation.