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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.

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Caspase-1 and IL-1β processing in a teleost fish.

Marta I R Reis1, Ana do Vale, Pedro J B Pereira

  • 1Fish Immunology and Vaccinology, Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal.

Plos One
|December 11, 2012
PubMed
Summary

Interleukin-1β (IL-1β) processing differs between mammals and fish. This study reveals sea bass caspase-1 activity and identifies distinct cleavage sites in fish and avian IL-1β, impacting inflammatory response research.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Comparative Genomics

Background:

  • Interleukin-1β (IL-1β) is a key pro-inflammatory cytokine central to immune responses.
  • Mammalian IL-1β is processed by caspase-1, but this cleavage site is absent in non-mammalian vertebrates.
  • Fish caspase-1 orthologues exist, yet their processing and activity remain largely uncharacterized.

Purpose of the Study:

  • To investigate the auto-processing and activity of sea bass caspase-1.
  • To identify alternatively spliced variants of caspase-1 in sea bass.
  • To determine the cleavage sites of sea bass and avian IL-1β by caspase-1.

Main Methods:

  • Biochemical assays to study sea bass caspase-1 auto-processing and activity.
  • Molecular cloning and sequencing to identify caspase-1 variants.
  • In vitro cleavage assays to map IL-1β processing sites.

Main Results:

  • Sea bass caspase-1 auto-processing mirrors human enzyme activity, forming active heterodimers.
  • Alternatively spliced variants of sea bass caspase-1 were identified.
  • Sea bass and avian IL-1β are cleaved by caspase-1 at distinct, conserved aspartate residues, differing from mammalian sites.

Conclusions:

  • Fish caspase-1 exhibits functional similarities to its mammalian counterpart.
  • The evolution of caspase-1 isoforms suggests a conserved regulatory role in inflammation.
  • Differential IL-1β cleavage sites in fish and birds highlight evolutionary divergence in inflammatory pathways.