Related Experiment Video
Updated: Aug 6, 2026

Strategies for Tracking Anastasis, A Cell Survival Phenomenon that Reverses Apoptosis
Published on: February 16, 2015
Endonuclease activation and chromosomal DNA fragmentation during apoptosis in leukemia cells
Akira Yoshida1, Yves Pommier, Takanori Ueda
1First Department of Internal Medicine, Faculty of Medical Sciences, University of Fukui, Matsuoka, Fukui, Japan. ayoshi@fmsrsa.fukui-med.ac.jp
Abstract:
Apoptotic endonuclease is a key enzyme that mediates regulated DNA fragmentation and chromatin condensation in response to apoptotic signals such as the Fas ligand, ionizing radiation, and anticancer agents. An endonuclease that is activated specifically by caspase-3 has been identified in humans and mice. The human gene for this protein has been termed DFF40 (DNA fragmentation factor, 40-kd subunit) or caspase-activated nuclease (CPAN), whereas the mouse homologue has been named caspase-activated deoxyribonuclease (CAD). Although CAD/DFF40 is known as a major apoptotic nuclease, mice lacking inhibitor of CAD (ICAD) (also known as DFF45) are viable and still show DNA fragmentation, suggesting that alternative endonucleases play an important role during apoptosis. Endonuclease G has been reported to possibly be responsible for DNA fragmentation in various cells during apoptosis. Furthermore, we also have found that apurinic/apyrimidinic endonuclease 1 (Ape1) and its N-terminal-truncated form (AN34) are involved in DNA fragmentation during apoptosis in leukemia cells. In this review, we describe the features of several endonucleases that are involved in the apoptosis of human leukemia cells. Apoptotic endonuclease may vary among different leukemia cell types.
Insights
Apoptotic endonucleases, including caspase-activated DNase (CAD) and Endonuclease G, are crucial for DNA fragmentation during apoptosis. Different leukemia cell types may utilize distinct apoptotic endonucleases.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Apoptotic endonuclease is vital for DNA fragmentation and chromatin condensation during programmed cell death.
- Caspase-3-activated endonucleases, such as DFF40 (human) and CAD (mouse), are key players in apoptosis.
- Despite CAD/DFF40's role, alternative endonucleases contribute to DNA fragmentation, as evidenced by viable mice lacking ICAD/DFF45.
Purpose of the Study:
- To review the features of various endonucleases involved in human leukemia cell apoptosis.
- To highlight the potential diversity of apoptotic endonucleases across different leukemia subtypes.
Main Methods:
- Literature review of studies on apoptotic endonucleases.
- Analysis of known endonuclease functions in apoptosis.
- Examination of findings related to Endonuclease G, Ape1, and AN34 in leukemia cells.
Main Results:
- Several endonucleases, including CAD/DFF40, Endonuclease G, apurinic/apyrimidinic endonuclease 1 (Ape1), and its truncated form (AN34), are implicated in DNA fragmentation during apoptosis.
- Ape1 and AN34 have been specifically identified in DNA fragmentation during apoptosis in leukemia cells.
- The specific apoptotic endonuclease involved may differ depending on the type of leukemia cell.
Conclusions:
- Apoptotic endonuclease activity is essential for DNA fragmentation in programmed cell death.
- While CAD/DFF40 is a major nuclease, other enzymes like Endonuclease G, Ape1, and AN34 also contribute to DNA fragmentation.
- The landscape of apoptotic endonucleases in human leukemia cells is diverse and cell-type specific.
Related Concept Videos
The Intrinsic Apoptotic Pathway
Apoptosis
The Extrinsic Apoptotic Pathway
DNA Damage can Stall the Cell Cycle
Nucleotide Excision Repair
Caspases
