Caspase 6

Caspase 6, apoptosis-related cysteine peptidase
Identifiers
Symbols	CASP6 ; MCH2
External IDs	Template:OMIM5 Template:MGI HomoloGene: 37455
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Caspase 6, apoptosis-related cysteine peptidase, also known as CASP6, is a human gene.

This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Alternative splicing of this gene results in two transcript variants that encode different isoforms.

Further reading

• Cohen GM (1997). "Caspases: the executioners of apoptosis". Biochem. J. 326 ( Pt 1): 1–16. PMID 9337844.
• Fernandes-Alnemri T, Litwack G, Alnemri ES (1995). "Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family". Cancer Res. 55 (13): 2737–42. PMID 7796396.CS1 maint: Multiple names: authors list (link)
• Fernandes-Alnemri T, Litwack G, Alnemri ES (1995). "CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme". J. Biol. Chem. 269 (49): 30761–4. PMID 7983002.CS1 maint: Multiple names: authors list (link)
• Takahashi A, Alnemri ES, Lazebnik YA; et al. (1996). "Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis". Proc. Natl. Acad. Sci. U.S.A. 93 (16): 8395–400. PMID 8710882.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tiso N, Pallavicini A, Muraro T; et al. (1996). "Chromosomal localization of the human genes, CPP32, Mch2, Mch3, and Ich-1, involved in cellular apoptosis". Biochem. Biophys. Res. Commun. 225 (3): 983–9. doi:10.1006/bbrc.1996.1282. PMID 8780721.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bullrich F, Fernandes-Alnemri T, Litwack G; et al. (1997). "Chromosomal mapping of cell death proteases CPP32, MCH2, and MCH3". Genomics. 36 (2): 362–5. doi:10.1006/geno.1996.0476. PMID 8812467.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Srinivasula SM, Fernandes-Alnemri T, Zangrilli J; et al. (1996). "The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32". J. Biol. Chem. 271 (43): 27099–106. PMID 8900201.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Srinivasula SM, Ahmad M, Fernandes-Alnemri T; et al. (1997). "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. PMID 8962078.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rao L, Perez D, White E (1997). "Lamin proteolysis facilitates nuclear events during apoptosis". J. Cell Biol. 135 (6 Pt 1): 1441–55. PMID 8978814.CS1 maint: Multiple names: authors list (link)
• Kim TW, Pettingell WH, Jung YK; et al. (1998). "Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease". Science. 277 (5324): 373–6. PMID 9219695.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Srinivasula SM, Ahmad M, Ottilie S; et al. (1997). "FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis". J. Biol. Chem. 272 (30): 18542–5. PMID 9228018.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Caulín C, Salvesen GS, Oshima RG (1997). "Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis". J. Cell Biol. 138 (6): 1379–94. PMID 9298992.CS1 maint: Multiple names: authors list (link)
• Hirata H, Takahashi A, Kobayashi S; et al. (1998). "Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis". J. Exp. Med. 187 (4): 587–600. PMID 9463409.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Harvey KF, Harvey NL, Michael JM; et al. (1998). "Caspase-mediated cleavage of the ubiquitin-protein ligase Nedd4 during apoptosis". J. Biol. Chem. 273 (22): 13524–30. PMID 9593687.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Utz PJ, Hottelet M, Le TM; et al. (1999). "The 72-kDa component of signal recognition particle is cleaved during apoptosis". J. Biol. Chem. 273 (52): 35362–70. PMID 9857079.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Samejima K, Svingen PA, Basi GS; et al. (1999). "Caspase-mediated cleavage of DNA topoisomerase I at unconventional sites during apoptosis". J. Biol. Chem. 274 (7): 4335–40. PMID 9933635.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Walter J, Schindzielorz A, Grünberg J, Haass C (1999). "Phosphorylation of presenilin-2 regulates its cleavage by caspases and retards progression of apoptosis". Proc. Natl. Acad. Sci. U.S.A. 96 (4): 1391–6. PMID 9990034.CS1 maint: Multiple names: authors list (link)
• van de Craen M, de Jonghe C, van den Brande I; et al. (1999). "Identification of caspases that cleave presenilin-1 and presenilin-2. Five presenilin-1 (PS1) mutations do not alter the sensitivity of PS1 to caspases". FEBS Lett. 445 (1): 149–54. PMID 10069390.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Xanthoudakis S, Roy S, Rasper D; et al. (1999). "Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis". EMBO J. 18 (8): 2049–56. doi:10.1093/emboj/18.8.2049. PMID 10205159.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)