Caspase

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Caspase

Caspase (/ˈkæspeɪz/), short for cysteine-aspartic acid protease, is a family of protease enzymes playing essential roles in programmed cell death (including apoptosis, pyroptosis, and necroptosis) and inflammation.

Etymology

The term "caspase" was coined from the merging of "cysteine protease" and "aspartate-specific". The name highlights the unique characteristic of these enzymes, which is the ability to cleave after an aspartic acid residue, and the presence of a critical cysteine residue in the active site.

Function

Caspases are essential in cells for apoptosis, or programmed cell death, in development and most other stages of adult life. They are also necessary in the immune system's response to infected or transformed, i.e., cancerous, cells.

Types

There are two types of caspases: initiator (apical) caspases and effector (executioner) caspases. Initiator caspases, which include caspase-2, -8, -9, and -10, cleave inactive pro-forms of effector caspases, thereby activating them. Effector caspases, which include caspase-3, -6, and -7, in turn, cleave other protein substrates within the cell, to trigger the apoptotic process.

Related Terms

  • Apoptosis: A form of programmed cell death that occurs in multicellular organisms.
  • Pyroptosis: A highly inflammatory form of programmed cell death.
  • Necroptosis: A form of programmed cell death which is associated with pathogen infection.

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