Ad
related to: caspase 1 cell death rate
Search results
Results From The WOW.Com Content Network
Recent studies implicated caspase-1 in promoting CD4 T-cell death and inflammation by HIV, two signature events that fuel HIV disease progression to AIDS. [29] [30] [31] Caspase-1 activity has also been implicated in lysosome acidification following phagocytosis of bacteria [32] and immune complexes. [33]
The integral role caspases play in cell death and disease has led to research on using caspases as a drug target. For example, inflammatory caspase-1 has been implicated in causing autoimmune diseases; drugs blocking the activation of Caspase-1 have been used to improve the health of patients. Additionally, scientists have used caspases as ...
The inflammasome was discovered by the team of Jürg Tschopp, at the University of Lausanne, in 2002. [17] [18] In 2002, it was first reported by Martinon et al. [17] that NLRP1 (NLR family PYD-containing 1) could assemble and oligomerize into a structure in vitro, which activated the caspase-1 cascade, thereby leading to the production of pro-inflammatory cytokines, including IL-1β and IL-18.
[2] [16] Dark, just as Apaf-1, has an N-terminal CARD domain that interacts with caspase Dronc, which is incorporated into this protein complex that will induce cell death. [ 12 ] Recruitment of Dronc by Dark seems to facilitate Dronc autocleavage at residue E352.
The apoptotic DNA fragmentation is being used as a marker of apoptosis and for identification of apoptotic cells either via the DNA laddering assay, [2] the TUNEL assay, [3] [4] or the by detection of cells with fractional DNA content ("sub G 1 cells") on DNA content frequency histograms e.g. as in the Nicoletti assay. [5] [6]
In a healthy cell, caspase-1 activation helps to fight infection caused by Salmonella and Shigella by introducing cell death to restrict pathogen growth. [6] When the "danger" signal is sensed, the quiescent cells will be activated to undergo pyroptosis and produce inflammatory cytokines IL-1β and IL-18.
Upon activation of Ipaf-1 by the intracellular bacterium S. typhimurium or other stress signals, Ipaf-1 recruits a CARD-containing adapter termed ASC and caspase-1 in unknown stoichiometry via CARD-CARD association. This complex in turn leads to autoproteolytic activation of caspase-1 and subsequent IL-1β and IL-18 maturation. [citation needed]
The death-effector domain (DED) is a protein interaction domain found only in eukaryotes that regulates a variety of cellular signalling pathways. [2] The DED domain is found in inactive procaspases (cysteine proteases) and proteins that regulate caspase activation in the apoptosis cascade such as FAS-associating death domain-containing protein ().