This gene encodes a protein that is a member of the cysteine-aspartic acidprotease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis.[8] Caspases exist as inactive proenzymes that 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. Caspase 6 can also undergo self-processing without other members of the caspase family.[12]Alternative splicing of this gene results in two transcript variants that encode different isoforms.[13]
Caspase-6 plays a role in the early immune response via de-repression. It reduces the expression of the immunosuppressant cytokine interleukin-10[9] and cleaves the macrophage suppressing IRAK-M.[10]
↑"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑Tiso N, Pallavicini A, Muraro T, Zimbello R, Apolloni E, Valle G, etal. (Oct 1996). "Chromosomal localization of the human genes, CPP32, Mch2, Mch3, and Ich-1, involved in cellular apoptosis". Biochemical and Biophysical Research Communications. 225 (3): 983–989. doi:10.1006/bbrc.1996.1282. hdl:11577/2461073. PMID8780721.
↑Fernandes-Alnemri T, Litwack G, Alnemri ES (Aug 1995). "Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family". Cancer Research. 55 (13): 2737–2742. PMID7796396.
Kim TW, Pettingell WH, Jung YK, Kovacs DM, Tanzi RE (1998). "Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease". Science. 277 (5324): 373–376. CiteSeerX10.1.1.1025.8052. doi:10.1126/science.277.5324.373. PMID9219695.
van de Craen M, de Jonghe C, van den Brande I, Declercq W, van Gassen G, van Criekinge W, etal. (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 Letters. 445 (1): 149–154. doi:10.1016/S0014-5793(99)00108-8. hdl:10067/238040151162165141. PMID10069390. S2CID31218178.