Caspase-7, apoptosis-related cysteine peptidase, also known as CASP7, is a human protein encoded by the CASP7gene.
CASP7orthologs[5] 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.[6]
^Tamm I, Wang Y, Sausville E, Scudiero DA, Vigna N, Oltersdorf T, Reed JC (Dec 1998). "IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs". Cancer Res. 58 (23): 5315–20.
PMID9850056.
^Shin S, Sung BJ, Cho YS, Kim HJ, Ha NC, Hwang JI, Chung CW, Jung YK, Oh BH (Jan 2001). "An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7". Biochemistry. 40 (4): 1117–23.
doi:
10.1021/bi001603q.
PMID11170436.
Caspase-7, apoptosis-related cysteine peptidase, also known as CASP7, is a human protein encoded by the CASP7gene.
CASP7orthologs[5] 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.[6]
^Tamm I, Wang Y, Sausville E, Scudiero DA, Vigna N, Oltersdorf T, Reed JC (Dec 1998). "IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs". Cancer Res. 58 (23): 5315–20.
PMID9850056.
^Shin S, Sung BJ, Cho YS, Kim HJ, Ha NC, Hwang JI, Chung CW, Jung YK, Oh BH (Jan 2001). "An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7". Biochemistry. 40 (4): 1117–23.
doi:
10.1021/bi001603q.
PMID11170436.