Description
Activation of the classical, alternate, or lectin complement pathways can result in the production of the C3a anaphylatoxin. C3a has been shown to be a multifunctional proinflammatory mediator. Thus, C3a has been shown to increase vascular permeability, to be spasmogenic and chemotactic, and to induce the release of pharmacologically active mediators from a number of cell types. C3a production in vivo may also initiate, contribute to, or exacerbate the inflammatory reactions seen in gram-negative bacterial sepsis, trauma, ARDS, ischemic heart disease, post-dialysis syndrome, and several autoimmune diseases including rheumatoid arthritis, lupus erythematosus, and acute glomerulonephritis.
In blood plasma or serum, once formed, the nascent C3a anaphylatoxin is rapidly cleaved to the C3a-desArg form by the endogenous serum carboxypeptidase N enzyme. Thus, the quantitation of C3a-desArg in plasma or experimental samples should yield a reliable measurement of the level of complement activation that has occurred in the test samples under investigation