Get The Long Form Of FLIP Is An Activator Of Caspase-8 At The Fas Death ... - Jbc

Caspase-8 is involved in inflammasome activity as well (reviewed in (107–109)) and can be activated by NLRP3, AIM2 and NLRC4 inflammasomes in macrophages (110, 111) and NLRP3 inflammasome in dendritic cells (97).

Caspase-8 and monocyte-macrophage differentiation The extrinsic pathway to caspase activation is initiated through ligation of membrane death receptors, which recruits the cytosolic adapter protein, FADD, and caspase-8, which form the death-inducing signaling complex (DISC).

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.

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.

Caspase-8 is an apical caspase involved in the programmed form of cell death called apoptosis that is critically important for mammalian development and immunity. Apoptosis was historically described as immunologically silent in contrast to other types of programmed cell death such as necroptosis or pyroptosis.

Like all caspases, caspase-8 is synthesized as an inactive single polypeptide chain zymogen procaspase and is activated by proteolytic cleavage, through either autoactivation after recruitment into a multimeric complex or trans-cleavage by other caspases.

Caspase-8 plays an important role in the CD95 (APO-1/Fas) signalling pathway. It is activated at the CD95 DISC. The mechanism of caspase-8 activation at the DISC is in the focus of intensive studies.

Cellular FLICE (FADD-like IL-1β-converting enzyme)-inhibitory protein (c-FLIP) is a major antiapoptotic protein and an important cytokine and chemotherapy resistance factor that suppresses cytokine- and chemotherapy-induced apoptosis.