Complement system
The proteins and glycoproteins that constitute the complement system are synthesized by the liver hepatocytes.
C3-convertase cleaves and activates component C3, creating C3a and C3b and causing a cascade of further cleavage and activation events. C3b binds to the surface of pathogens leading to greater internalization by phagocytic cells by opsonization. C5a is an important chemotactic protein, helping recruit inflammatory cells. Both C3a and C5a have anaphylatoxin activity, directly triggering degranulation of mast cells as well as increasing vascular permeability and smooth muscle contraction. C5b initiates the membrane attack pathway, which results in the membrane attack complex (MAC), consisting of C5b, C6, C7, C8, and polymeric C9. MAC is the cytolytic endproduct of the complement cascade; it forms a transmembrane channel, which causes osmotic lysis of the target cell. Kupffer cells and other macrophage cell types help clear complement-coated pathogens. As part of the innate immune system, elements of the complement cascade can be found in species earlier than vertebrates; most recently in the protostome horseshoe crab species, putting the origins of the system back further than was previously thought.
Complement factor H (CFH) is the major fluid-phase regulator of the alternative pathway of complement. It plays a key role in controlling complement activation in vivo.
 |
The complement
system plays an
important role in both innate and adaptive immunity.
The complement
activation pathways, the classical, the lectin and the
alternative pathway merge through at common intersection C3 that plays
a central role in the complement system. C3 activation leads to
activation of C5 that initiates lytic pathway involving the formation
of the membrane attack complex. The activation pathway leads to the
formation of the anaphylatoxins C3a and C5a...
|