Complement Component 5a

Complement component 5a is the most potent of the anaphylatoxins, liberated from C5 by C5 convertases during terminal complement activation. The peptide binds two receptors, C5aR1 (CD88) and C5aR2, on neutrophils, macrophages, mast cells, and endothelium, driving chemotaxis, oxidative burst, degranulation, vascular leakage, and cytokine induction. Excessive C5a signaling contributes to sepsis, ischemia-reperfusion injury, autoimmune disease, and paroxysmal nocturnal hemoglobinuria pathology, which is why terminal complement blockade by drugs such as eculizumab suppresses C5a generation. Recombinant C5a is essential for receptor pharmacology, neutrophil-activation assays, and complement-targeted drug screening. Its actions overlap with, yet are pharmacologically distinct from, those of C3a.