Biology:Caspase 7

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Caspase-7, apoptosis-related cysteine peptidase, also known as CASP7, is a human protein encoded by the CASP7 gene. CASP7 orthologs[1] have been identified in nearly all mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.

Function

Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream caspases (caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this caspase is cleaved by caspase 3, caspase 10, and caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms.[2]

Interactions

Caspase 7 has been shown to interact with:

See also

References

  1. "OrthoMaM phylogenetic marker: CASP7 coding sequence". http://www.orthomam.univ-montp2.fr/orthomam/data/cds/detailMarkers/ENSG00000165806_CASP7.xml. 
  2. "Entrez Gene: CASP7 caspase 7, apoptosis-related cysteine peptidase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=840. 
  3. "Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria". J. Biol. Chem. 277 (16): 13430–7. Apr 2002. doi:10.1074/jbc.M108029200. PMID 11832478. 
  4. "Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. Natl. Acad. Sci. U.S.A. 93 (25): 14486–91. Dec 1996. doi:10.1073/pnas.93.25.14486. PMID 8962078. Bibcode1996PNAS...9314486S. 
  5. "IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs". Cancer Res. 58 (23): 5315–20. Dec 1998. PMID 9850056. 
  6. "An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7". Biochemistry 40 (4): 1117–23. Jan 2001. doi:10.1021/bi001603q. PMID 11170436. 
  7. "Structural basis for the inhibition of caspase-3 by XIAP". Cell 104 (5): 791–800. Mar 2001. doi:10.1016/S0092-8674(01)00274-4. PMID 11257232. 
  8. "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases". EMBO J. 16 (23): 6914–25. Dec 1997. doi:10.1093/emboj/16.23.6914. PMID 9384571. 
  9. "X-linked IAP is a direct inhibitor of cell-death proteases". Nature 388 (6639): 300–4. Jul 1997. doi:10.1038/40901. PMID 9230442. Bibcode1997Natur.388..300D. 
  10. "X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes". J. Biol. Chem. 276 (29): 27058–63. Jul 2001. doi:10.1074/jbc.M102415200. PMID 11359776. 

Further reading

External links

  • The MEROPS online database for peptidases and their inhibitors: C14.004
  • Overview of all the structural information available in the PDB for UniProt: P55210 (Human Caspase-7) at the PDBe-KB.