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Related Concept Videos

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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The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

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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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The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

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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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CRISPR and crRNAs02:53

CRISPR and crRNAs

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Bacteria and archaea are susceptible to viral infections just like eukaryotes; therefore, they have developed a unique adaptive immune system to protect themselves. Clustered regularly interspaced short palindromic repeats and CRISPR-associated proteins (CRISPR-Cas) are present in more than 45% of known bacteria and 90% of known archaea.
The CRISPR-Cas system stores a copy of foreign DNA in the host genome and uses it to identify the foreign DNA upon reinfection. CRISPR-Cas has three different...
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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
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Updated: Jun 24, 2025

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry
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Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry

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Inflammatory caspase substrate specificities.

Patrick M Exconde1, Christopher M Bourne1, Madhura Kulkarni1

  • 1Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania, USA.

Mbio
|June 5, 2024
PubMed
Summary
This summary is machine-generated.

Inflammatory caspases, crucial for pyroptosis, use two binding sites—the active site and an exosite—to recognize protein substrates. This expands our understanding beyond peptide studies.

Keywords:
IL-18IL-1βcaspase substratescaspase-1caspase-11caspase-4caspase-5cytokinesinflammasomesinflammatory caspasespyroptosis

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Caspases are cysteine proteases regulating cell death and inflammation.
  • Apoptosis substrates are well-characterized, but inflammatory caspase substrates (pyroptosis) are less understood.
  • Current knowledge often relies on peptide substrates, not native proteins.

Purpose of the Study:

  • To review recent advances in understanding caspase substrate specificity.
  • To focus on inflammatory caspases and their substrate recognition mechanisms.
  • To highlight newly discovered inflammatory caspase substrates.

Main Methods:

  • Literature review of recent research on caspase substrate specificity.
  • Analysis of studies identifying novel caspase substrates.
  • Examination of experimental evidence for substrate recognition interfaces.

Main Results:

  • Inflammatory caspases recognize substrates via two interfaces: the active site and a conserved exosite.
  • New protein substrates for inflammatory caspases have been identified.
  • Specificity determinants for inflammatory caspase substrates are increasingly understood.

Conclusions:

  • Inflammatory caspases employ dual binding sites for substrate recognition, improving specificity.
  • Recent discoveries are significantly advancing the field of pyroptosis and inflammatory caspase biology.
  • Future research should focus on native protein substrates and these dual recognition mechanisms.