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LPS and ATP-induced Death of PMA-differentiated THP-1 Macrophages and its Validation
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Ripped to death.

Ricardo Weinlich1, Christopher P Dillon, Douglas R Green

  • 1Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.

Trends in Cell Biology
|October 8, 2011
PubMed
Summary
This summary is machine-generated.

Caspase-8 and FADD proteins prevent embryonic lethality by blocking RIPK-mediated necrosis, a newly discovered pro-survival role essential for yolk sac vasculature development.

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Area of Science:

  • Cell biology
  • Developmental biology
  • Molecular mechanisms of cell death

Background:

  • The roles of caspase-8 and Fas-associated death domain (FADD) in apoptosis are well-established.
  • Embryonic lethality in caspase-8 or FADD-deficient animals was previously unexplained.
  • Receptor interacting serine-threonine kinases (RIPKs) are known mediators of cell death.

Purpose of the Study:

  • To elucidate the cause of embryonic lethality in caspase-8/FADD-deficient animals.
  • To investigate the pro-survival function of caspase-8 and FADD.
  • To understand the interplay between apoptosis and necrosis pathways.

Main Methods:

  • Analysis of embryonic lethality in genetically modified animal models.
  • Investigating the role of RIPKs in development.
  • Studying the interaction between caspase-8, FADD, and FLIP(Long).

Main Results:

  • Embryonic lethality is due to defective yolk sac vasculature development, not failed apoptosis.
  • Caspase-8 and FADD, with FLIP(Long), inhibit RIPK-mediated necrosis.
  • Ablation of RIPKs rescues the embryonic lethality phenotype.

Conclusions:

  • Caspase-8 and FADD possess a critical pro-survival function by suppressing RIPK-mediated necrosis.
  • This pro-survival role is crucial for embryonic development, specifically yolk sac vasculature formation.
  • The findings reveal a novel mechanism regulating cell death and survival pathways.