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Caspase 1 is an enzyme that cleaves inflammatory cytokines and Gasdermin D, and initiates inflammatory response and pyroptosis. It is activated by forming a ring complex called inflammasome with sensor and adaptor proteins, and can be inhibited by CARD-only proteins.
Caspase-1 itself is activated in different inflammasome complexes, which assemble in response to a variety of exogenous and endogenous stressors. More recently, pyroptosis, a caspase-1-dependent type of programmed cell death, has been identified that is able to support secreted IL-1 and IL-18 in triggering an inflammatory response.
Caspase-1, Caspase-4, Caspase-5 and Caspase-11 are considered 'Inflammatory Caspases'. [7] Caspase-1 is key in activating pro-inflammatory cytokines; these act as signals to immune cells and make the environment favourable for immune cell recruitment to the site of damage. Caspase-1 therefore plays a fundamental role in the innate immune system ...
Caspase-1 is the well-studied inflammatory mediated caspase, which is important for pro-inflammatory cytokines (proIL-1β and IL-18) maturation into IL-1β and IL-18. 5 Inflammatory mediated caspases are those caspases that take part in the process of inflammation and cell death to overcome the stimulatory materials. 26 The pro-caspase-1, is ...
Caspase-1 was cloned nearly three decades ago as the Interleukin-1β Converting Enzyme (ICE) in a hunt for the enzyme that is responsible for the proteolytic maturation of the pro-inflammatory cytokine IL-1β in human monocytes (Lamkanfi and Dixit, 2014, 2017). The subsequent generation of caspase-1-deficient mice confirmed the essential role ...
Caspase-1 is one of the main mediators of inflammatory caspases and has become a correspondent with inflammation, cell death, and several inflammatory diseases. In this review, we systematically summarize both original and recent advances in caspase-1 to provide references for a better understanding …
Caspase-1 was initially discovered as the cysteine proteinase in 1989 that was responsible for the processing of pro-interleukin-1β (IL-1β) to a biologically active form in human monocytes [11, 12]. Caspase-1 was found unrelated to any identified proteins when it was initially isolated, cloned, and sequenced in 1992 [13, 14].
Caspase-1 is a unique cysteine protease playing central roles in innate immunity. Pathogens, stress, and damage signals induce activation of caspase-1, typically mediated by proximity-induced autoproteolysis in multimeric protein complexes called the inflammasome. Active caspase-1 induces secretion …
Abstract. Caspase-1, formerly known as interleukin (IL)-1-converting enzyme is best established as the protease responsible for the processing of the key pro-inflammatory cytokine IL-1β from an inactive precursor to an active, secreted molecule. Thus, caspase-1 is regarded as a key mediator of inflammatory processes, and has become synonymous with inflammation.
Caspase-1, also known as interleukin-1β (IL-1β)-converting enzyme (ICE), regulates antimicrobial host defense, tissue repair, tumorigenesis, metabolism and membrane biogenesis. On activation ...