N-Acetyl-beta -D-Glucosaminidase Release Induced by Complement Component C5a and Neutralization by Human Complement Component C5a Antibody. |
Recombinant Human Complement Component C5a (Catalog # 2037-C5) induces N‑acetyl‑ beta ‑D‑glucosaminidase release in the the dibutyryl cyclic-AMP differentiated U937 human histiocytic lymphoma cell line in a dose-dependent manner (orange line). N-Acetyl-beta -D-Glucosaminidase Release elicited by Recombinant Human Complement Component C5a (10 ng/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Human Complement Component C5a Monoclonal Antibody (Catalog # MAB2037). The ND50 is typically 0.04‑0.12 µg/mL in the presence of cytochalasin‑B.
Human complement component C5a (C5a) is an enzymatically generated glycoprotein that belongs to a family of structurally and functionally related proteins known as anaphylatoxins. C5a is a 74 amino acid (aa) peptide that is created by the activity of C5a convertase on the C5 alpha -chain (1, 2). Human C5a has four alpha -helices plus three intrachain disulfide bonds that create a triple loop structure (3). In serum, proteolytic processing removes the C-terminal arginine, creating a low activity C5a desArg74 molecule (1). Human C5a is 60% and 54% aa identical to mouse and rat C5a, respectively. C5a binds to a signaling G-protein coupled receptor (C5aR/CD88) and a non-signaling GPCR termed C5L2 (4). Activation of Cd88 results in neutrophil chemotaxis and endothelial cell activation (1, 5). It also triggers an oxidative burst in macrophages and neutrophils, and induces release of histamine in basophils and mast cells.
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