What is the function of caspase-1?
Caspase-1 is an enzyme involved in the processing of pro-IL-1β to active secreted IL-1β, a key inflammatory mediator driving the host response to infection, injury, and disease. During disease, IL-1β-driven inflammation has often disastrous consequences, and thus represents a therapeutic target.
What is pro caspase?
Caspases (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death. Caspases also have a role in inflammation, whereby it directly processes pro-inflammatory cytokines such as pro-IL1β.
What happens when caspase-1 is activated?
Following the inflammatory response, an activated Caspase-1 can induce pyroptosis, a lytic form of cell death, depending on the signal received as well as the specific inflammasome sensor domain protein that received it.
Is caspase-1 secreted?
Inflammatory protease, caspase-1, is secreted from monocytes in a stably active form in response to inflammasome activation (INM3P.
Where is caspase-1 produced?
Caspase-1 Activation by Inflammasomes. Caspase-1 is produced as an inactive zymogen that is recruited and activated by cytosolic multi-protein complexes known as inflammasomes (Lamkanfi and Dixit, 2009).
How are pro caspases activated?
All caspases are synthesized in cells as catalytically inactive zymogens, and must undergo an activation process. The activation of an effector caspase, such as caspase-3 or -7, is performed by an initiator caspase, such as caspase-9, through an internal cleavage to separate the large and small subunits.
How are caspases activated?
What is the role of caspase-1 in activation of IL 1β?
Caspase-1 cleaves the prodomain from inactive pro-IL-1β at YVHD ( 119 )-A, producing bioactive IL-1β ( 31,32 ). Characterization of caspase-1 -deficient mice confirmed that caspase-1 plays a major role in vivo in activation of IL-1β ( 33,34 ).
What was the original name of caspase 1?
Caspase-1 was first described in 1989 as the cysteine proteinase responsible for the production of interleukin 1-beta (IL-1-beta) in monocytes [1,2], hence its original name, interleukin 1-beta-converting enzyme ( ICE ). When it was first purified, cloned and sequenced in 1992, it was found to be unrelated to any known protein [3,4].
What is the specificity of the caspase 1 antibody?
Specificity / Sensitivity. Caspase-1 Antibody detects endogenous levels of pro-caspase-1 and the caspase-1 p20 subunit. The antibody is expected to detect alpha, beta, gamma and delta isoforms.
What happens to caspase 1 after an infection?
Following infection, the inflammatory response increases expression of Caspase-1, by a positive feedback mechanism that amplifies the response. Caspase-1 is produced as a zymogen that can then be cleaved into 20 kDa (p20) and 10 kDa (p10) subunits that become part of the active enzyme. Active Caspase 1 contains two heterodimers of p20 and p10.
