Mechanism The polymerization of perforin and pore formation requires calcium ions. These ions involve in the conformational transition of inactive globular perforin to an active form and get incorporated into the cell membrane. Perforin is capable to get attached to the cells by membrane phospholipids. Phosphatidylcholine attaches calcium ions and upregulates the perforin affinity to the cell membrane. Pores generated by perforin alters cell membrane permeability and allows the transport of ions and water. Due to this mineral homeostasis get altered and tonic shock develops inside the cell. This change leads to the activation of the pro-apoptotic pathway and DNA degradation resulting in cell death.
Perforin involves in the cytotoxic activity of natural killer cell and cytotoxic CD8 T cells. Both these cell eliminates the infected cell by a similar mechanism. Natural killer cells show a quick cytotoxicity activity against the infected cells, which is mainly based on the release of perforin and granzyme B. In an infected cell, the antigen is fragmented partially by the lysosome in the cell and these fragmented antigens are processed and expressed on the cell surface through major histocompatibility complex II. CD8 T lymphocytes recognize these antigens and acts against this cell. Once the MHC II is detected, the effector cell binds with the target cell through T cell receptor forming a lytic synapse. There is a change in the cell ultrastructure and cytolytic granules, microtubules and Golgi apparatus move towards the lytic synapse. The cytolytic granules consist of the proteins namely perforin and granzyme B and it mediates the cytotoxic activity. The pore formation occurs in the target cell with the help of perforin and infusion of ions, water, and molecules into the cell cause cell lysis.
Mechanism of Action of Cytotoxic Effector Cell (Cytolytic Granules)
Perforin/granzyme signaling is carried out by cytotoxic T lymphocytes that exhibits the cytotoxic effects on cancer cells and virus or bacteria-infected cells.
It mediates the release of the pore-forming molecule, perforin, with a consequent release of cytoplasmic granules through the pore targeting the infected cell.
The granules consist of two serine proteases; granzyme B and granzyme A that can stimulate different proteins
Granzyme B stimulates caspase activation indirectly, by activating the pro-apoptotic BH3-interacting domain death agonist (Bid).
Bid along with BCL-2 family Bax and/or Bak proteins cause in the leakage of mitochondrial components, such as cytochrome
Cytochrome c activates pro caspase-9, and reacts with the apoptotic protease activating factor 1(Apaf-1), pro-caspase-9 to form the apoptosome and activates caspase-3 resulting in apoptosis of the infected cell.
Granzyme B directly stimulates inactive caspase-3 to an active form. This activation mediates apoptosis.
Granzyme A mediates the cytotoxic T cell-induced apoptosis and activates caspase-independent pathways.
Granzyme A affects the membrane potential mitochondrial inner region and leakage of reactive oxygen species (ROS). It generates single-stranded DNA breaks.
Granzyme A protease breaks the SET complex that stops the synthesis of the DNAse enzyme.
The inactivation of the SET complex by stimulates apoptosis by affecting the integrity of chromatin structure.
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