CASP1

(redirected from Caspase-1)

CASP1

A gene on chromosome 11q23 that encodes a protein belonging to the cysteine-aspartic acid protease (caspase) family which, once activated by proteolytic processing, plays a central role in the execution-phase of cell apoptosis, as well as various stages of embryological development.

Molecular pathology
CASP1 mutations may play a role in Huntington’s disease.
References in periodicals archive ?
Inflammasomes are multiprotein complexes that mediate activation of caspase-1 and promote secretion of proinflammatory cytokines.
gingivalis 381, the cells were harvested, and the caspase-1, caspase-3, caspase-8, caspase-9, and caspase-12 activities were measured using a caspase fluorometric protease assay kit (MBL).
Western blot analysis for active caspase-1 and cleaved caspase-3, evaluation of lung injury and a cytokine release analysis were performed.
NLRP3 inflammasome activates caspase-1 which can promote the maturation and secretion of inflammatory cytokine interleukin 1[beta] (IL-1[beta]) and trigger a powerful and endogenous inflammatory cascade reaction, which would cause the occurrence and development of DN [6, 7].
Pyroptosis, a supramolecular assembly of ASC dimers, is a recently identified kind of cell death and dependent on caspase-1 [10-12].
To the Editor: The inflammasome, a multiprotein oligomer which regulates the innate immune functions by activating caspase-1 and catalyzing the hydrolysis and secretion of interleukin (IL)-1[sz] and IL-18, is an important mediator of ventilator-induced lung injury (VILI).[1] The NACHT, LRR, and PYD domains-containing protein 3 (NLRP3) initiates the inflammatory response by assembling with the ASC and caspase-1 to form the inflammasome and then activating pro-caspase-1 and the release of IL-1[sz] and IL-18.[2] That study also showed the involvement of NLRP3 inflammasome in VILI.
Mucus-secreting cells have been associated with inflammatory reactions and parasitic infection in salmonids (Reite & Evensen, 2006), and pro-inflammatory caspase-1 activation as a proxy for immunological activation due to the fundamental role this molecule plays in vertebrate innate immunity (Lopez-Castejon et al., 2008).
Johnson, et al., concluded that activation of caspase recruitment domain-containing protein 8 acts as an inflammasome sensor to activate caspase-1 and mediates DPP8/9 inhibitor-induced cell death in myeloid cells.
Its main function is to identify the risk signals of exogenous infection and internal injury of various pathogenic microorganisms and mediate the activation of caspase-1 and process pro-IL-[beta] into a mature active form to secrete extracellularly, so as to activate a natural immune response, resulting in multicascade inflammatory response and cell apoptosis [4].
In general, IL-1[beta] is cleaved by caspase-1. However, some previous studies also indicated that IL-1[beta] can be processed by caspase-8 [19] or caspase-11 through a noncanonical inflammasome [20].
Inflammasomes lead to the activation of caspase-1 and the following cleavage of IL-1[beta] and IL-18, the two major proinflammatory cytokines.
Inflammasomes, such as NOD-like receptors (NLRP) and absent in melanoma 2(AIM 2-) like receptors, are innate immune system sensors of damage-associated molecular patterns (DAMPs) and pathogen-associated molecular patterns (PAMPs) that regulate the activation of caspase-1 and promote secretion of proinflammatory cytokines, such as IL-1[beta] and IL-18 [23-25].

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