positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis

Definition

Target type: biologicalprocess

Any process that activates or increases the frequency, rate or extent of cysteine-type endopeptidase activity involved in execution phase of apoptosis. [GOC:mtg_apoptosis]

Positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis is a complex and tightly regulated process that plays a critical role in the dismantling of cells during programmed cell death. It involves the activation and regulation of a specific subset of cysteine-type endopeptidases, primarily caspases, which execute the dismantling of the cell by cleaving specific proteins. This process is initiated by various apoptotic stimuli, such as DNA damage, growth factor deprivation, or cytotoxic stress, and is typically characterized by a series of events leading to the activation of a cascade of caspases.

- **Initiator Caspases:** Apoptotic stimuli trigger the activation of initiator caspases (Caspase-8, -9, -10, and -12), which are responsible for initiating the apoptotic cascade. These caspases are typically activated through the formation of DISC (Death-Inducing Signaling Complex) or apoptosome, multiprotein complexes that bring together the initiator caspases with their respective adaptor proteins.

- **Executioner Caspases:** Once activated, initiator caspases cleave and activate executioner caspases (Caspase-3, -6, and -7). These caspases are the main effectors of apoptosis and are responsible for the dismantling of the cell. They cleave a wide range of substrates, including:

- **Cytoskeletal proteins:** Disrupting the cell's structural integrity.
- **DNA repair proteins:** Compromising the cell's ability to repair DNA damage.
- **Nuclear lamins:** Fragmenting the nuclear envelope.
- **Inhibitors of apoptosis:** Eliminating the cell's protective mechanisms.

- **Activation of the Executioner Caspases:** The activation of executioner caspases involves a complex process that involves the proteolytic cleavage of their pro-enzymes. This cleavage releases the active catalytic domain of the caspase, allowing it to cleave its substrate. This process can be regulated by:

- **Inhibitors of apoptosis:** Proteins that can block the activation of caspases, such as XIAP, cIAP, and survivin.
- **Apoptotic signals:** Signals that can enhance or suppress the activation of caspases, such as the presence of pro- or anti-apoptotic proteins.

- **Regulation of Apoptotic Pathway:** The activation of executioner caspases is tightly regulated to ensure that apoptosis occurs only when necessary. This regulation involves a complex interplay of pro-apoptotic and anti-apoptotic proteins.

The positive regulation of cysteine-type endopeptidase activity involved in the execution phase of apoptosis ensures that the apoptotic cascade is initiated and completed in a timely and efficient manner. This process is essential for maintaining cellular homeostasis and preventing the accumulation of damaged or unwanted cells. Disruptions in this process can contribute to various diseases, including cancer, autoimmune diseases, and neurodegenerative disorders. '"

Proteins (1)

Compounds (2)