How does caspase 7 cause apoptosis?
Caspases, an evolutionary conserved family of aspartate-specific cystein proteases, are at the heart of the apoptotic machinery (Lamkanfi et al., 2002). Activated initiator caspases directly activate the executioner caspases-3 and/or -7, which lead to apoptosis or inflammation by cleaving specific sets of substrates.
What is a caspase inhibitor?
Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the initiation and execution of apoptosis. They are expressed as latent zymogens and are activated by an autoproteolytic mechanism or by processing by other proteases (frequently other caspases).
What is the role of caspase 1?
Caspase-1 is a cysteine protease that converts the inactive proform of IL-1β to the active inflammatory cytokine and hence represents an attractive target for the modulation of the effects of IL-1β (12,13).
How are caspases inhibited?
Caspases exist as inactive zymogens in cells and undergo a cascade of catalytic activation at the onset of apoptosis. The activated caspases are subject to inhibition by the inhibitor-of-apoptosis (IAP) family of proteins.
What are effector caspases?
Effector caspases cause cell-wide specific proteolysis and dysfunction, including the labeling of the cell with “eat me” signals, thus allowing the apoptotic cell to be recognized and engulfed by phagocytic cells.
How does Z-VAD-FMK work?
Z-VAD-FMK (carbobenzoxy-valyl-alanyl-aspartyl-[O-methyl]- fluoromethylketone) is a cell-permeant pan caspase inhibitor that irreversibly binds to the catalytic site of caspase proteases and can inhibit induction of apoptosis.
What happens when caspase-1 is activated?
Pyroptosis response 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.
What are the executioner caspases?
Executioner caspases can cleave an array of target proteins leading to characteristic apoptotic breakdown of a cell. DNA fragmentation is a caspase-mediated hallmark of apoptosis, which helps facilitate the clearance of apoptotic bodies.
What is the role of caspase 7 in apoptosis?
Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis.
Which is a member of the caspase family?
Caspase-7 is a member of the caspase (c ysteine asp artate prote ase) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis.
Which is the precursor of the active enzyme Caspase 9?
Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream caspases (caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this caspase is cleaved by caspase 3, caspase 10, and caspase 9.
What kind of animals have CASP7 orthologs?
CASP7 orthologs have been identified in nearly all mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts . Caspase-7 is a member of the caspase ( c ysteine asp artate prote ase) family of proteins, and has been shown to be an executioner protein of apoptosis.