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Caspases01:24

Caspases

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Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
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Formation of Lipopolysaccharides01:19

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Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...
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The Extrinsic Apoptotic Pathway01:17

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The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...
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Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
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Cells undergoing apoptosis form apoptotic bodies that must be removed immediately to prevent inflammation, autoimmune diseases, and necrosis. Phagocytosis is carried out by professional phagocytes such as macrophages or  immature dendritic cells. Non-professional phagocytes such as  epithelial cells and fibroblasts also take part in this process; however, they are not as effective as professional phagocytes. 
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Complement System01:27

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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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Caspases come together over LPS.

Christina Smith1, Xiaohui Wang2, Hang Yin3

  • 1Department of Chemistry & Biochemistry and the BioFrontiers Institute, University of Colorado Boulder, 596 UCB, Boulder, CO 80309-0596, USA.

Trends in Immunology
|January 10, 2015
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Caspases 4/5/11 act as cytosolic lipopolysaccharide (LPS) receptors, triggering cell death pathways. Their activation via oligomerization upon LPS binding reveals new insights into pyroptosis and sepsis treatment strategies.

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Area of Science:

  • Cellular Biology
  • Immunology
  • Biochemistry

Background:

  • Caspases are key regulators of programmed cell death.
  • Pyroptosis is an inflammatory form of cell death with implications in various diseases.
  • The precise mechanisms of cytosolic pattern recognition receptor activation remain an active area of research.

Purpose of the Study:

  • To elucidate the role of caspases 4/5/11 in sensing cytosolic lipopolysaccharide (LPS).
  • To investigate the activation mechanism of caspases 4/5/11 in response to LPS.
  • To explore the implications of these findings for understanding pyroptosis and sepsis.

Main Methods:

  • Biochemical assays to study protein-ligand interactions.
  • Cell-based assays to monitor caspase activation and cell death.
  • Oligomerization studies to analyze protein complex formation.

Main Results:

  • Caspases 4/5/11 function as direct cytosolic receptors for LPS.
  • LPS binding induces oligomerization and subsequent activation of caspases 4/5/11.
  • This activation initiates pyroptotic cell death.

Conclusions:

  • Caspases 4/5/11 are critical sensors of cytosolic LPS.
  • The oligomerization-driven activation mechanism provides a new understanding of pyroptosis.
  • Targeting this pathway may offer novel therapeutic strategies for sepsis.