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Caspases

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 Pathway

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 Pathway

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...

Apoptosis

Apoptosis

Apoptosis is a combination of two Greek words, 'apo' and 'ptosis,' meaning separation and falling off, respectively. Hippocrates used this word to describe gangrene, which was caused due to bandaging of fractured bones. Apoptosis was distinguished from necrosis in 1970 when John Kerr reported observations of morphological changes occurring during apoptosis. During one experiment, he observed that the disruption of blood supply to the liver tissue resulted in a size reduction of the tissue.

CRISPR/Cas9 Genome Editing

CRISPR/Cas9 Genome Editing

The CRISPR-Cas system serves as a bacterial defense mechanism against invading genetic elements such as viruses and plasmids, forming the foundation for its adaptation as a powerful genome-editing tool. Originally discovered in prokaryotes, this system has been repurposed to revolutionize genetic engineering across a wide range of organisms, including plants, animals, and humans. The core component, Cas9, is an endonuclease derived from Streptococcus pyogenes, capable of introducing...

CRISPR

CRISPR

Genome editing technologies allow scientists to modify an organism’s DNA via the addition, removal, or rearrangement of genetic material at specific genomic locations. These types of techniques could potentially be used to cure genetic disorders such as hemophilia and sickle cell anemia. One popular and widely used DNA-editing research tool that could lead to safe and effective cures for genetic disorders is the CRISPR-Cas9 system. CRISPR-Cas9 stands for Clustered Regularly Interspaced Short...

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Related Experiment Video

Updated: Jun 1, 2026

In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila

In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila

Published on: November 27, 2016

A designed redox-controlled caspase.

Witold A Witkowski¹, Jeanne A Hardy

¹Department of Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, USA.

Protein Science : a Publication of the Protein Society

|June 16, 2011

Summary

This summary is machine-generated.

Researchers engineered a redox-controlled caspase-7 enzyme. This apoptosis-inducing protein can be inactivated in oxidizing environments and reactivated in reducing conditions, enabling targeted cell death strategies.

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Last Updated: Jun 1, 2026

In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila

In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila

Published on: November 27, 2016

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

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Published on: March 5, 2018

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry

Published on: March 24, 2023

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Caspases are critical cysteine proteases that induce apoptosis.
Controlled activation of caspases is essential for targeted cell death therapies.

Purpose of the Study:

To design and characterize a redox-switchable caspase-7 enzyme.
To enable targeted apoptosis induction via external triggers.

Main Methods:

Engineered a disulfide bond to allosterically inactivate caspase-7.
Utilized oxidizing extracellular and reducing intracellular conditions for inactivation and reactivation.
Characterized enzyme activity and structure using immunoblotting, mass spectrometry, and crystallography.

Main Results:

Developed a caspase-7 variant controllable by redox conditions.
Demonstrated reversible inactivation and reactivation of caspase-7 activity.
Obtained the first crystal structure of an ordered, active caspase-7 in its substrate-free state.

Conclusions:

The engineered redox-controlled caspase-7 offers precise temporal and spatial control over apoptosis.
This enzyme is suitable for targeted cell death applications, especially with redox-triggered delivery systems.