Caspase 1

From Wikipedia, the free encyclopedia
Caspase 1, apoptosis-related cysteine peptidase

PDB rendering based on 1bmq.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsCASP1; ICE; IL1BC; P45
External IDsOMIM: 147678 MGI: 96544 HomoloGene: 133272 ChEMBL: 4801 GeneCards: CASP1 Gene
EC number3.4.22.36
Orthologs
SpeciesHumanMouse
Entrez83412362
EnsemblENSG00000137752ENSMUSG00000025888
UniProtP29466P29452
RefSeq (mRNA)NM_001223NM_009807
RefSeq (protein)NP_001214NP_033937
Location (UCSC)Chr 11:
104.9 – 104.97 Mb		Chr 9:
5.3 – 5.31 Mb
PubMed search
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Caspase 1/Interleukin-1 converting enzyme is an enzyme that proteolytically cleaves other proteins, such as the precursor forms of the inflammatory cytokines interleukin 1β and interleukin 18, into active mature peptides.[1][2] It belongs to a family of cysteine proteases known as caspases that always cleave proteins following an aspartic acid residue.[3] Caspase 1 is produced as a zymogen that is cleaved into 20 kDa (p20) and 10 kDa (p10) subunits that become part of the active enzyme. Active caspase 1 contains two heterodimers of p20 and p10. It interacts with another CARD domain containing protein called PYCARD (or ASC) and is involved in inflammasome formation and activation of inflammatory processes.[4]

Caspase 1 has been shown to induce cell necrosis or pyroptosis and may function in various developmental stages. Studies of a similar protein in mouse suggest a role in the pathogenesis of Huntington's disease. Alternative splicing of the gene results in five transcript variants encoding distinct isoforms.[5] Recent studies implicated caspase 1 in promoting CD4 T-cell death and inflammation by HIV, two signature events that fuel HIV disease progression to AIDS[6][7]

Interactions

Caspase 1 has been shown to interact with NLRC4.[8][9]

Caspase-1 has been shown to interact with RIPK2 via CARD-CARD domain interactions.

See also

References

  1. ↑ Thornberry N, Bull H, Calaycay J, et al. (1992). "A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes". Nature 356 (6372): 768–74. doi:10.1038/356768a0. PMID 1574116. 
  2. ↑ Cerretti DP, Kozlosky CJ, Mosley B, et al. (1992). "Molecular cloning of the interleukin-1 beta converting enzyme". Science 256 (5053): 97–100. doi:10.1126/science.1373520. PMID 1373520. 
  3. ↑ Black RA, Kronheim SR, Merriam JE, March CJ, Hopp TP (1989). "A pre-aspartate-specific protease from human leukocytes that cleaves pro-interleukin-1 beta". J Biol Chem 264 (10): 5323–5326. PMID 2784432. 
  4. ↑ Mariathasan S, Newton K, Monack D, Vucic D, French D, Lee W, Roose-Girma M, Erickson S, Dixit V (2004). "Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf". Nature 430 (6996): 213–8. doi:10.1038/nature02664. PMID 15190255. 
  5. ↑ "Entrez Gene: CASP1 caspase 1, apoptosis-related cysteine peptidase (interleukin 1, beta, convertase)". 
  6. ↑ Doitsh, G. et al Nature (2013) "Cell death by pyroptosis drives CD4 T-cell depletion in HIV-1 infection"
  7. ↑ Monroe KM et al Science (2013) "IFI16 DNA Sensor Is Required for Death of Lymphoid CD4 T Cells Abortively Infected with HIV"
  8. ↑ Damiano, Jason S; Oliveira Vasco, Welsh Kate, Reed John C (Jul 2004). "Heterotypic interactions among NACHT domains: implications for regulation of innate immune responses". Biochem. J. (England) 381 (Pt 1): 213–9. doi:10.1042/BJ20031506. PMC 1133779. PMID 15107016. 
  9. ↑ Damiano, J S; Stehlik C, Pio F, Godzik A, Reed J C (Jul 2001). "CLAN, a novel human CED-4-like gene". Genomics (United States) 75 (1–3): 77–83. doi:10.1006/geno.2001.6579. ISSN 0888-7543. PMID 11472070. 

External links

  • The MEROPS online database for peptidases and their inhibitors: C14.001
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Fruit-derived
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Cathepsin
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