Members of the ICE/CED-3 protease family play key biologic roles in inflammation and mammalian apoptosis. Alnemri et
al. (1996) indicated that 10 homologs of human origin had been published. They proposed a nomenclature for the human
members of this protease family. They recommended use of the trivial name 'caspase' as a root for serial names for all family
members. The selection of caspase was based on 2 catalytic properties of these enzymes. The 'c' was intended to reflect a
cysteine protease mechanism, and 'aspase' referred to their ability to cleave after aspartic acid, the most distinctive catalytic
feature of this protease family. To designate individual family members, caspase was to be followed by an arabic number,
assigned on the date of publication.
Fernandes-Alnemri et al. (1995) isolated MCH2, a member of the ced-3 subfamily of apoptotic proteases, by performing
PCR on human Jurkat T lymphocytes using degenerate oligonucleotides corresponding to conserved peptides in known
apoptotic cysteine proteases. The gene, also symbolized CASP6, encodes a 34-kD protein that is highly homologous to
human CPP32 , C. elegans ced-3, mammalian Ich1/Nedd2, and mammalian interleukin-1-beta converting
enzyme.
NCBI Summary:
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 2 subunits, large and small, that dimerize to form the active enzyme. This protein could be 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 which encode different isoforms.
Review: lamin a/c, caspase-6, and chromatin configuration during meiosis resumption in the mouse oocyte. Arnault E et al. After in vitro maturation (IVM), isolation of the healthiest oocytes is essential for successful in vitro fertilization. As germinal vesicle (GV) oocytes resume meiosis through healthy or apoptotic pathways without discernable morphological criteria, we checked for an apoptotic element acting at the nucleus level. We hypothesized that caspase-6 with its corresponding substrate, lamin A/C, could be a potential target candidate, because caspase-6 is the only functional caspase for lamin A/C. We used immunohistochemistry methods, Western blots, and a specific caspase-6 inhibitor to determine the presence of lamin A/C and caspase-6 during oogenesis and in isolated oocytes. Our results demonstrated that these proteins were always present and that their distributions were related to oocyte maturity, determined by chromatin configuration and oocyte diameter. Caspase-6 inhibition slowed meiosis resumption suggesting the involvement of caspase-6 in the oocyte apoptotic pathway. Lamin A/C and caspase-6 could be valuable tools in the knowledge of oocyte in vitro destiny.
Genes whose expression is detected by cDNA array hybridization: GDP/GTP exchangers, GTPase stimulators and inhibitors, apoptosis Rozenn Dalbi?Tran and Pascal Mermilloda
Expression regulated by
Comment
Ovarian localization
Cumulus
Comment
Mapping and transcription profiling of CASP1, 3, 6, 7 and 8 in relation to caspase activity in the bovine cumulus-oocyte complex 9 Yuan YQ, et al .
Follicle stages
Primordial
Comment
Arraztoa JA, et al 2005 reported the identification of genes expressed in primate primordial oocytes.