The membrane attack complex is initiated when the complement protein C5 convertase cleaves C5 into C5a and C5b. These fluid phase complexes do not bind to cell membranes and are ultimately scavenged by clusterin and vitronectin, two regulators of complement. If the pre-MAC complexes of C5b-7, C5b-8 or C5b-9 do not insert into a membrane, they can form inactive complexes with Protein S (sC5b-7, sC5b-8 and sC5b-9). If enough pores form, the cell is no longer able to survive. The ring structure formed by C9 is a pore in the membrane that allows free diffusion of molecules in and out of the cell. This region is homologous to cholesterol-dependent cytolysins from Gram-positive bacteria. MAC is composed of a complex of four complement proteins (C5b, C6, C7, and C8) that bind to the outer surface of the plasma membrane, and many copies of a fifth protein (C9) that hook up to one another, forming a ring in the membrane. C5b-6-7-8 subsequently binds to C9 and acts as a catalyst in the polymerization of C9. The C5b-6-7 complex binds to C8, which is composed of three chains (alpha, beta, and gamma), thus forming the C5b-6-7-8 complex. Freshly activated C5b binds to C6 to form a C5b-6 complex, then to C7 forming the C5b-6-7 complex. The MAC is composed of the complement components C5b, C6, C7, C8 and several C9 molecules.Ī number of proteins participate in the assembly of the MAC. Assembly of the MAC leads to pores that disrupt the cell membrane of target cells, leading to cell lysis and death. Antibody-mediated complement activation leads to MAC deposition on the surface of infected cells. ![]() ![]() The membrane attack complex ( MAC) or terminal complement complex ( TCC) is a complex of proteins typically formed on the surface of pathogen cell membranes as a result of the activation of the host's complement system, and as such is an effector of the immune system. A membrane attack complex attached to a pathogenic cell
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