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, Lanfranchi G, Danieli GA (Oct 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.
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 Res. 55 (13): 2737–42.
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): 373–6.
CiteSeerX10.1.1.1025.8052.
doi:
10.1126/science.277.5324.373.
PMID9219695.
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, Lanfranchi G, Danieli GA (Oct 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.
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 Res. 55 (13): 2737–42.
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): 373–6.
CiteSeerX10.1.1.1025.8052.
doi:
10.1126/science.277.5324.373.
PMID9219695.