membrane attack complex , MAC (skrót)

C5b forms the first part of the complement membrane attack complex.

SP-40, 40 is associated with the assembly of the membrane attack complex of human complement.

Secondly, some complement system components form a membrane attack complex to assist antibodies to kill the bacterium directly.

In lieu of the membrane attack complex, complement proteins (particularly C3b and C4b) are deposited on red blood cells.

It is part of the membrane attack complex which can insert into the cell membrane and cause cell to lyse.

If the complement response is sufficient, red blood cells are damaged by the membrane attack complex, an effector of the complement cascade.

The subsequent complement cascade catalyzed by C3-convertase results in creating a membrane attack complex, which causes lysis of the pathogen.

A cluster of proteins called the membrane attack complex, which normally attack only foreign particles, suddenly attacks cells that line the inside of vessels.

C8 alpha-gamma induces the polymerization of 10-16 molecules of C9 into a pore-forming structure known as the membrane attack complex.

That is, mediators of acute inflammation are generated at the site and membrane attack complexes cause cell lysis and death.

One example is CD59, also known as protectin, which inhibits C9 polymerisation during the formation of the membrane attack complex.

Activation of complements occurs far from the cell membrane, and insertion of the membrane attack complex does not occur.

Terminal complement pathway deficiency is a genetic condition affecting the complement membrane attack complex (MAC).

The membrane attack complex is initiated when the complement protein C5 convertase cleaves C5 into C5a and C5b.

The proteolytic cleavage of C5 is the only known enzymatic event in assembly of the cytolytic membrane attack complex of complement.

It is a member of the Membrane Attack Complex (MAC) and induces pores on membranes.

If the complement response is insufficient to form membrane attack complexes, then extravascular lysis will be favored over intravascular red blood cell lysis.

The worms have many tools that help in this evasion, including the tegument, antioxidant proteins, and defenses against host membrane attack complex (MAC).

The C5b then recruits and assembles C6, C7, C8 and multiple C9 molecules to assemble the membrane attack complex.

The end-result of this activation cascade is massive amplification of the response and activation of the cell-killing membrane attack complex.

A C5,6,7,8,9 (the MAC, membrane attack complex, or terminal complement proteins) deficiency lead to unopposed Neisserial infections.

The complement proteins C6-C9 all contain a MACPF domain and assemble into the membrane attack complex.

When complement activation leads to deposition of C5b678 on host cells, CD59 can prevent C9 from polymerizing and forming the complement membrane attack complex.

Quinidine (IgM mediated activation of classical complement pathway and Membrane attack complex, MAC)

CFHR1 blocks C5 convertase activity and interferes with C5b surface deposition and membrane attack complex (MAC) formation.