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Related Concept Videos

Necrosis01:16

Necrosis

Necrosis is considered as an “accidental” or unexpected form of cell death that ends in cell lysis. The first noticeable mention of “necrosis” was in 1859 when Rudolf Virchow used this term to describe advanced tissue breakdown in his compilation titled “Cell Pathology”.
Morphological Manifestations of Necrosis
Necrotic cells show different types of morphological appearance depending on the type of tissue and infection. In coagulative necrosis, cells become anucleated and die, but their...
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...
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...
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...
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.

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Related Experiment Video

Updated: Jul 4, 2026

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

A non-classical necroptosis pathway mediated by caspases.

Qingyue Wang1,2, Hang Xu3, Xin Ding1,2

  • 1State Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture and Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, 266071, China.

Cell Communication and Signaling : CCS
|July 3, 2026
PubMed
Summary

This study reveals that caspases regulate necroptosis in teleosts by cleaving key pathway proteins. This caspase-mediated necroptosis regulation is likely conserved across vertebrates, offering new insights into cell death mechanisms.

Keywords:
Larimichthys croceaCaspaseMLKLNecroptosisRIPK

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

Published on: March 24, 2023

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Last Updated: Jul 4, 2026

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

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

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Immunology

Background:

  • Necroptosis is a regulated cell death pathway involving RIPK1, RIPK3, and MLKL.
  • In humans, caspase-8 inhibits necroptosis by inactivating RIPK1 and RIPK3.
  • The role of caspases in necroptosis regulation in teleosts is largely unexplored.

Purpose of the Study:

  • Investigate caspase-mediated regulation of necroptosis in teleosts using the large yellow croaker (Larimichthys crocea).
  • Identify and characterize the core necroptosis components in L. crocea.
  • Determine how caspases interact with and modulate the RIPK1/RIPK3-MLKL pathway in teleosts.

Main Methods:

  • Microscopy and biochemical assays to study necroptosis.
  • Immunoblotting to analyze caspase cleavages.
  • Co-immunoprecipitation to examine protein-protein interactions.
  • Sequence alignment and WebLogo analysis for evolutionary conservation.

Main Results:

  • Identified and characterized LcRIPK1, LcRIPK3, and LcMLKL in L. crocea.
  • Demonstrated that LcRIPK3 complexes with LcRIPK1 and recruits/activates LcMLKL.
  • Showed that L. crocea caspases (LcCASP) 3, 6, and 7 differentially regulate LcRIPK1, LcRIPK3, and LcMLKL.
  • LcCASP3/6 inactivate LcRIPK1 and LcRIPK3, while LcCASP1/3/7 activate LcMLKL.
  • Found conserved caspase cleavage sites in RIPK1/3 and MLKL across vertebrates, suggesting a common regulatory mechanism.

Conclusions:

  • Revealed a teleost necroptosis pathway with integrated caspase regulation networks.
  • Proposed a conserved CASPs-MLKL pathway across vertebrate lineages.
  • Provided new insights into the complex regulation of necroptosis in Vertebrata.