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Related Concept Videos

Caspases01:24

Caspases

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 cells.
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

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...
The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

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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Related Experiment Video

Updated: Jul 6, 2026

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry
05:29

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry

Published on: March 24, 2023

Brain cathepsin B cleaves a caspase substrate.

A A Yakovlev1, A Yu Gorokhovatsky, M V Onufriev

  • 1Institute of Higher Nervous Activity and Neurophysiology, Russian Academy of Sciences, Moscow, Russia.

Biochemistry. Biokhimiia
|April 9, 2008
PubMed
Summary

Researchers found an enzyme in rat brains that cleaves caspase-3 substrates at low pH. This enzyme, identified as cathepsin B, is primarily in lysosomes and may play a role in brain cells during conditions like hypoxia.

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Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry
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Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
08:47

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

Published on: March 5, 2018

Area of Science:

  • Biochemistry
  • Neuroscience
  • Cell Biology

Background:

  • Caspase-3 is a key enzyme in apoptosis.
  • The activity of caspase-3 and its substrates can be influenced by cellular conditions.
  • Understanding enzymes that interact with caspase-3 substrates is crucial for studying cell death pathways.

Purpose of the Study:

  • To identify enzymes in rat brain that cleave caspase-3 specific peptide substrates at acidic pH.
  • To characterize the properties and localization of this enzyme.
  • To investigate the potential role of this enzyme in vivo, particularly under stress conditions.

Main Methods:

  • Enzyme activity assays using the specific substrate Ac-DEVD-AMC at low pH.
  • Enzyme purification from rat brain homogenates.
  • Enzyme identification using MALDI-TOF Mass Spectrometry.
  • Subcellular localization studies.

Main Results:

  • An enzyme capable of cleaving Ac-DEVD-AMC at low pH was detected in rat brain.
  • The enzyme exhibits characteristics of a cysteine protease and is predominantly localized in lysosomes.
  • Purification and mass spectrometry identified the enzyme as cathepsin B.
  • The in vivo role of cathepsin B in cleaving caspase-3 substrates remains unclear, but a role under conditions like hypoxia is proposed.

Conclusions:

  • Cathepsin B possesses "acidic" DEVDase activity in rat brain.
  • While its in vivo function in caspase-3 substrate cleavage is not fully established, cathepsin B may contribute to this process in brain cells during specific conditions such as hypoxia.
  • Further research is needed to elucidate the precise physiological and pathological roles of cathepsin B in relation to caspase-3 activity.