caspase
Sign in to saveAlso known as caspases
Caspases (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death. They are named caspases due to their specific cysteine protease activity – a cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. As of 2009, there are 12 confirmed caspases in humans and 10 in mice, carrying out a variety of cellular functions.
Key facts
- Protein family.Symbol
- Peptidase_C14
- Protein family.Name
- Caspase domain
- Protein family.image
- Caspase 1.png
- Protein family.caption
- Structure of caspase-1 (CASP1), originally called interleukin-1 beta-converting enzyme (ICE), the first human caspase to be identified.
- Protein family.Pfam
- PF00656
- Protein family.Pfam_clan
- CL0093
- Protein family.InterPro
- IPR002398
- Protein family.MEROPS
- C14
- Protein family.PROSITE
- PS50208
- Protein family.SCOP
- 1ice
via Wikipedia infobox
Research
156,506 papers- Caspase-9.The international journal of biochemistry & cell biology · 2000
- Non-canonical inflammasome activation targets caspase-11.Nature · 2011
- Caspase-5: Structure, Pro-Inflammatory Activity and Evolution.Biomolecules · 2024
- Caspase Activation and Inhibition.Cold Spring Harbor perspectives in biology · 2022
- Inflammatory caspase substrate specificities.mBio · 2024
via PubMed
~18 min read
Article
16 sectionsContents
- Functional classification of caspases
- Activation of caspases
- Dimerisation
- Cleavage
- Some roles of caspases
- Apoptosis
- Pyroptosis
- Pyroptosis by caspase-1
- Role in inflammation
- Discovery of caspases
- Evolution
- Detection
- See also
- Notes
- References
- External links
Caspases (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death. They are named caspases due to their specific cysteine protease activity – a cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. As of 2009, there are 12 confirmed caspases in humans and 10 in mice, carrying out a variety of cellular functions.
The role of these enzymes in programmed cell death was first identified in 1993, with their functions in apoptosis well characterised. This is a form of programmed cell death, occurring widely during development, and throughout life to maintain cell homeostasis. Activation of caspases ensures that the cellular components are degraded in a controlled manner, carrying out cell death with minimal effect on surrounding tissues.