activation of cysteine-type endopeptidase activity involved in apoptotic process

Definition

Target type: biologicalprocess

Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process. [GOC:al, GOC:dph, GOC:jl, GOC:mtg_apoptosis, GOC:tb, PMID:14744432, PMID:18328827, Wikipedia:Caspase]

Activation of cysteine-type endopeptidase activity involved in the apoptotic process is a complex and tightly regulated cascade that ultimately leads to the dismantling of the cell. This process is triggered by a variety of stimuli, including DNA damage, growth factor deprivation, and cytotoxic stress. The core of the apoptotic cascade is the activation of a family of cysteine proteases known as caspases. Caspases are synthesized as inactive pro-enzymes (pro-caspases) and must undergo proteolytic processing to become active. This activation typically occurs through a series of sequential proteolytic cleavages.

One major pathway leading to caspase activation is the extrinsic pathway, which is initiated by the binding of death ligands, such as tumor necrosis factor (TNF) or Fas ligand, to their respective death receptors on the cell surface. These receptors contain cytoplasmic death domains that recruit adaptor proteins, leading to the formation of the death-inducing signaling complex (DISC). The DISC serves as a platform for the activation of caspase-8 and caspase-10, which then activate downstream effector caspases.

The intrinsic or mitochondrial pathway is triggered by internal cellular stress, such as DNA damage or growth factor deprivation. This pathway involves the release of cytochrome c from the mitochondria into the cytosol. Cytochrome c binds to Apaf-1, which then recruits pro-caspase-9 to form the apoptosome complex. The apoptosome activates caspase-9, which subsequently activates downstream effector caspases.

Once activated, effector caspases (such as caspase-3, caspase-6, and caspase-7) cleave a variety of cellular substrates, leading to the dismantling of the cell. These substrates include proteins involved in DNA repair, cell cycle regulation, and cytoskeletal integrity. The cleavage of these substrates ultimately results in the characteristic morphological changes associated with apoptosis, including chromatin condensation, nuclear fragmentation, and cell shrinkage.

Activation of cysteine-type endopeptidase activity involved in the apoptotic process is a critical mechanism for eliminating damaged or unwanted cells and maintaining tissue homeostasis. Dysregulation of this process can contribute to the development of diseases, such as cancer and autoimmune disorders.'
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Proteins (33)

Compounds (1,467)