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Related Experiment Videos

Programmed cell death induced by ceramide

L M Obeid1, C M Linardic, L A Karolak

  • 1Department of Medicine, Duke University Medical Center, Durham, NC 27710.

Science (New York, N.Y.)
|March 19, 1993
PubMed
Summary

Synthetic C2-ceramide triggers DNA fragmentation and apoptosis in leukemic cells, a process influenced by sphingolipid structure and protein kinase C signaling.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Sphingomyelin hydrolysis and ceramide generation are key in cell signaling pathways affecting cell growth and differentiation.
  • Tumor necrosis factor-alpha (TNF-alpha) induces DNA fragmentation and apoptosis in leukemic cells.

Purpose of the Study:

  • To investigate the role of C2-ceramide, a synthetic analog, in inducing apoptosis in leukemic cells.
  • To explore the structural requirements for ceramide-induced apoptosis and its regulation by intracellular pathways.

Main Methods:

  • Treatment of leukemic cells with C2-ceramide and related lipids.
  • Assessment of DNA fragmentation and apoptosis induction.
  • Investigation of the effects of zinc ions and protein kinase C activators.

Main Results:

  • C2-ceramide (0.6-5 microM) induced internucleosomal DNA fragmentation, a hallmark of apoptosis.
  • Zinc ions inhibited C2-ceramide-induced DNA fragmentation.
  • C2-dihydroceramide and other amphiphilic lipids did not induce apoptosis, highlighting the importance of the sphingolipid double bond.
  • Phorbol 12-myristate 13-acetate, a protein kinase C activator, prevented C2-ceramide's apoptotic effects.

Conclusions:

  • C2-ceramide effectively induces apoptosis in leukemic cells via DNA fragmentation.
  • Apoptosis induction by C2-ceramide is dependent on the sphingolipid double bond and is modulated by opposing intracellular signaling pathways involving protein kinase C.

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