Caspase 6

Caspase 6

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

PBB_Summary
section_title =
summary_text = 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. [cite web | title = Entrez Gene: CASP6 caspase 6, apoptosis-related cysteine peptidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=839| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Cohen GM |title=Caspases: the executioners of apoptosis. |journal=Biochem. J. |volume=326 ( Pt 1) |issue= |pages= 1–16 |year= 1997 |pmid= 9337844 |doi=
*cite journal | author=Fernandes-Alnemri T, Litwack G, Alnemri ES |title=Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family. |journal=Cancer Res. |volume=55 |issue= 13 |pages= 2737–42 |year= 1995 |pmid= 7796396 |doi=
*cite journal | author=Fernandes-Alnemri T, Litwack G, Alnemri ES |title=CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. |journal=J. Biol. Chem. |volume=269 |issue= 49 |pages= 30761–4 |year= 1995 |pmid= 7983002 |doi=
*cite journal | author=Takahashi A, Alnemri ES, Lazebnik YA, "et al." |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 16 |pages= 8395–400 |year= 1996 |pmid= 8710882 |doi=
*cite journal | author=Tiso N, Pallavicini A, Muraro T, "et al." |title=Chromosomal localization of the human genes, CPP32, Mch2, Mch3, and Ich-1, involved in cellular apoptosis. |journal=Biochem. Biophys. Res. Commun. |volume=225 |issue= 3 |pages= 983–9 |year= 1996 |pmid= 8780721 |doi= 10.1006/bbrc.1996.1282
*cite journal | author=Bullrich F, Fernandes-Alnemri T, Litwack G, "et al." |title=Chromosomal mapping of cell death proteases CPP32, MCH2, and MCH3. |journal=Genomics |volume=36 |issue= 2 |pages= 362–5 |year= 1997 |pmid= 8812467 |doi= 10.1006/geno.1996.0476
*cite journal | author=Srinivasula SM, Fernandes-Alnemri T, Zangrilli J, "et al." |title=The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32. |journal=J. Biol. Chem. |volume=271 |issue= 43 |pages= 27099–106 |year= 1996 |pmid= 8900201 |doi=
*cite journal | author=Srinivasula SM, Ahmad M, Fernandes-Alnemri T, "et al." |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 25 |pages= 14486–91 |year= 1997 |pmid= 8962078 |doi=
*cite journal | author=Rao L, Perez D, White E |title=Lamin proteolysis facilitates nuclear events during apoptosis. |journal=J. Cell Biol. |volume=135 |issue= 6 Pt 1 |pages= 1441–55 |year= 1997 |pmid= 8978814 |doi=
*cite journal | author=Kim TW, Pettingell WH, Jung YK, "et al." |title=Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. |journal=Science |volume=277 |issue= 5324 |pages= 373–6 |year= 1998 |pmid= 9219695 |doi=
*cite journal | author=Srinivasula SM, Ahmad M, Ottilie S, "et al." |title=FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis. |journal=J. Biol. Chem. |volume=272 |issue= 30 |pages= 18542–5 |year= 1997 |pmid= 9228018 |doi=
*cite journal | author=Caulín C, Salvesen GS, Oshima RG |title=Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis. |journal=J. Cell Biol. |volume=138 |issue= 6 |pages= 1379–94 |year= 1997 |pmid= 9298992 |doi=
*cite journal | author=Hirata H, Takahashi A, Kobayashi S, "et al." |title=Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis. |journal=J. Exp. Med. |volume=187 |issue= 4 |pages= 587–600 |year= 1998 |pmid= 9463409 |doi=
*cite journal | author=Harvey KF, Harvey NL, Michael JM, "et al." |title=Caspase-mediated cleavage of the ubiquitin-protein ligase Nedd4 during apoptosis. |journal=J. Biol. Chem. |volume=273 |issue= 22 |pages= 13524–30 |year= 1998 |pmid= 9593687 |doi=
*cite journal | author=Utz PJ, Hottelet M, Le TM, "et al." |title=The 72-kDa component of signal recognition particle is cleaved during apoptosis. |journal=J. Biol. Chem. |volume=273 |issue= 52 |pages= 35362–70 |year= 1999 |pmid= 9857079 |doi=
*cite journal | author=Samejima K, Svingen PA, Basi GS, "et al." |title=Caspase-mediated cleavage of DNA topoisomerase I at unconventional sites during apoptosis. |journal=J. Biol. Chem. |volume=274 |issue= 7 |pages= 4335–40 |year= 1999 |pmid= 9933635 |doi=
*cite journal | author=Walter J, Schindzielorz A, Grünberg J, Haass C |title=Phosphorylation of presenilin-2 regulates its cleavage by caspases and retards progression of apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 4 |pages= 1391–6 |year= 1999 |pmid= 9990034 |doi=
*cite journal | author=van de Craen M, de Jonghe C, van den Brande I, "et al." |title=Identification of caspases that cleave presenilin-1 and presenilin-2. Five presenilin-1 (PS1) mutations do not alter the sensitivity of PS1 to caspases. |journal=FEBS Lett. |volume=445 |issue= 1 |pages= 149–54 |year= 1999 |pmid= 10069390 |doi=
*cite journal | author=Xanthoudakis S, Roy S, Rasper D, "et al." |title=Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis. |journal=EMBO J. |volume=18 |issue= 8 |pages= 2049–56 |year= 1999 |pmid= 10205159 |doi= 10.1093/emboj/18.8.2049

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