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caspase 1 OKDB#: 865
 Symbols: CASP1 Species: human
 Synonyms: ICE, P45, IL1BC  Locus: 11q22.3 in Homo sapiens


For retrieval of Nucleotide and Amino Acid sequences please go to: OMIM Entrez Gene
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General Comment Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Unlike apoptosis, cell death by pyroptosis results in plasma-membrane rupture and the release of damage-associated molecular pattern (DAMP) molecules such as ATP, DNA and ASC oligomers (specks) into the extracellular milieu, including cytokines that recruit more immune cells and further perpetuate the inflammatory cascade in the tissue. Fink SL et al. (2005)////////////////// 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.

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 gene was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. This gene has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing results in transcript variants encoding distinct isoforms. [provided by RefSeq, Mar 2012]
General function Cell death/survival, Apoptosis, Enzyme, Hydrolase, Peptidase/Protease
Comment
Cellular localization Cytoplasmic
Comment
Ovarian function Follicle atresia, Ovulation, Oogenesis, Oocyte maturation
Comment Expression and Contribution of NLRP3 Inflammasome During the Follicular Development Induced by PMSG. Zhang Z et al. (2019) Follicular development and following ovulation induced by luteinizing hormone (LH) surge are critical for ovarian functions, but the molecular mechanism regulating ovarian ovulation attracts more attention and remains mainly unknown. Recent researches on the nucleotide leukin rich polypeptide 3 (NLRP3) inflammasome shred light on it. Given pregnant mare serum gonadotropin (PMSG) can not only trigger the follicular development, but also induce the following ovulation, the present study therefore examined that expression and localization of NLRP3 inflammasome through immunohistochemistry and Western blotting during the follicular development induced by PMSG. The results showed expressions of NLRP3 and the adaptor protein apoptosis-associated speck-like protein (ASC) significantly increased in the outside of intrafollicular fluid, further analysis found that caspase-1 was activated and IL-1β production was also upregulated after 52 h-treatment of PMSG. Furthermore, a significant increase of ovulation-related genes, hypoxia inducible factor (HIF)-1α and endothelin (ET)-1, was found after 52 h-treatment of PMSG. To our knowledge, it is the first time to clearly indicated the activation of NLRP3 inflammasome may contribute to the ovulation of PMSG-treated ovaries, which will help to further clarify the ovulatory mechanism in mammals.////////////////// Izawa M, et al. reported the expression of the apoptosis-related genes, caspase-1, caspase-3, DNA fragmentation factor, and apoptotic protease activating factor-1, in human granulosa cells. Johnson AL, et al. reported characterization of the chicken interleukin-1beta converting enzyme (caspase-1) cDNA and expression of caspase-1 mRNA in the hen.
Expression regulated by LH, Steroids
Comment Irahara M, et al. reported the expression and hormonal regulation of rat ovarian interleukin-1beta converting enzyme. They document a periovulatory increase in ovarian ICE gene expression, show the inhibitory effect of glucocorticoids in this regard, and establish TNF alpha as an upregulator.
Ovarian localization Granulosa, Theca
Comment
Follicle stages Secondary, Antral, Preovulatory
Comment
Phenotypes
Mutations 1 mutations

Species: mouse
Mutation name:
type: null mutation
fertility: fertile
Comment: Li et al. (1997) generated ICE-deficient mice through gene targeting technology. ICE-deficient mice developed normally, appeared healthy, and were fertile. Peritoneal macrophages from ICE-deficient mice underwent apoptosis normally upon ATP treatment.Peritoneal macrophages from ICE-deficient mice underwent apoptosis normally upon ATP treatment. Thymocytes from young ICE-deficient mice also underwent apoptosis when triggered by dexamethasone, gamma irradiation, or aging. ICE-deficient mice had a major defect in the production of mature IL-1 beta and had impaired IL-1 alpha production on LPS stimulation in vitro and in vivo. ICE-deficient mice were resistant to LPS-induced endotoxic shock.

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Links
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created: Feb. 19, 2000, midnight by: hsueh   email:
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last update: Sept. 30, 2020, 10:44 a.m. by: hsueh    email:



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