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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...
Cellular Injury V: Apoptosis and Autophagy01:22

Cellular Injury V: Apoptosis and Autophagy

Cells respond to damage and stress through highly coordinated processes that decide whether they survive or undergo controlled self-destruction. Two major pathways involved in this regulation are apoptosis, a type of programmed cell death, and autophagy, a survival mechanism that helps cells adapt to adverse conditions.ApoptosisApoptosis removes aged or injured cells to maintain tissue balance. During this process, the cell shrinks, chromatin condenses and fragments, and membrane-bound...
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.
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

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Evaluation of Caspase Activation to Assess Innate Immune Cell Death
10:23

Evaluation of Caspase Activation to Assess Innate Immune Cell Death

Published on: January 20, 2023

Human caspases: activation, specificity, and regulation.

Cristina Pop1, Guy S Salvesen1

  • 1Program in Apoptosis and Cell Death Research, Burnham Institute for Medical Research, La Jolla, California 92037.

The Journal of Biological Chemistry
|May 29, 2009
PubMed
Summary

Caspases, crucial proteases regulating cell death and inflammation, are activated through a tightly controlled cellular mechanism. This review updates knowledge on caspase activation and regulation, highlighting areas needing further research.

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Evaluation of Caspase Activation to Assess Innate Immune Cell Death
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Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
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Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Caspases are intracellular proteases essential for programmed cell death, proliferation, and inflammation.
  • Their activation is a conserved cellular process governed by strict regulatory mechanisms.
  • Activated caspases cleave specific substrates, initiating signaling cascades for biological responses.

Purpose of the Study:

  • To provide an updated overview of caspase activation and regulation mechanisms.
  • To identify and discuss significant knowledge gaps in caspase function.
  • To suggest potential experimental approaches for future research.

Main Methods:

  • Literature review and synthesis of current research on caspases.
  • Analysis of conserved mechanisms in caspase activation.
  • Identification of areas requiring further investigation through emerging techniques.

Main Results:

  • Caspase activation follows a conserved pathway involving specific stimuli and regulated proteolysis.
  • Significant advancements have been made in understanding caspase activation and regulatory networks.
  • Substantial gaps remain in fully elucidating the diverse functions of caspases.

Conclusions:

  • Caspase activity is fundamental to cellular homeostasis and disease processes.
  • Continued research is vital to address current knowledge deficits in caspase biology.
  • Developing and applying novel experimental paradigms will be key to future discoveries.