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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...
Apoptosis01:30

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 and crRNAs02:53

CRISPR and crRNAs

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...
Overview of Cell Death01:30

Overview of Cell Death

Cell death is an essential process where the body gets rid of old or damaged cells. Cell proliferation and death need to be balanced, as an imbalance between the two may lead to cancer or autoimmune diseases.
Cell death was observed in the early 19th century, but there was no experimental evidence to prove it. In 1842, Carl Vogt first discovered cell death in a metamorphic toad; however, it was not termed ‘cell death.’ Scientists discovered different cell death pathways only in the 20th century...

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Updated: Jul 5, 2026

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

Caspase mechanisms.

Guy S Salvesen1, Stefan J Riedl

  • 1Program on Apoptosis and Cell Death, Burnham Institute for Medical Research, 10901 N. Torrey Pines Road, La Jolla, CA 92037, USA. gsalvesen@burnham.org

Advances in Experimental Medicine and Biology
|April 29, 2008
PubMed
Summary
This summary is machine-generated.

Apoptosis, programmed cell death, is executed by caspase proteases. Initiator caspases activate effector caspases through a two-step signaling pathway, amplifying the cell death signal.

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Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
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Evaluation of Caspase Activation to Assess Innate Immune Cell Death
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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Apoptosis, or programmed cell death, is a fundamental biological process crucial for development and tissue homeostasis.
  • Caspases, a family of proteases, are the primary mediators of apoptosis, existing as inactive precursors in cells.

Purpose of the Study:

  • To elucidate the signaling pathway and activation mechanisms of caspases in apoptosis.
  • To understand how apoptotic stimuli are converted into proteolytic activity for efficient cell death.

Main Methods:

  • The study focuses on the molecular mechanisms of caspase activation and function.
  • Analysis of the two-step signaling cascade involving initiator and effector caspases.

Main Results:

  • Apoptotic stimuli trigger the formation of oligomeric signaling complexes, leading to initiator caspase activation via proximity-induced clustering.
  • Activated initiator caspases proteolytically cleave and activate executioner caspases, amplifying the apoptotic signal.
  • This cascade results in the cleavage of numerous protein substrates, driving efficient apoptosis.

Conclusions:

  • The caspase-mediated apoptotic pathway involves a precise two-step activation mechanism.
  • Proximity-induced clustering of initiator caspases is key to their activation.
  • The amplification of proteolytic activity ensures the efficient execution of apoptosis.