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Identification of p32 as a novel substrate for ATM in heart

Hisakazu Kato1, Seiji Takashima, Yoshihiro Asano

  • 1Department of Cardiovascular Medicine, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

Biochemical and Biophysical Research Communications
|December 12, 2007
PubMed

Insights

Researchers identified p32 as a novel ATM substrate in the heart, revealing a new pathway for DNA damage response that may impact cardiotoxicity from chemotherapy.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cardiology

Background:

  • Chemotherapy-induced DNA damage can cause cardiotoxicity, limiting treatment efficacy.
  • ATM (Ataxia-telangiectasia mutated) is crucial for DNA damage response but its role in cardiac cells is unclear.
  • Understanding ATM's cardiac function is vital for mitigating chemotherapy side effects.

Purpose of the Study:

  • To identify ATM substrates in mouse heart homogenate.
  • To elucidate the role of ATM-mediated DNA damage response in cardiac cells.
  • To investigate potential new pathways for cardiac protection during chemotherapy.

Main Methods:

  • In vitro ATM kinase assays using purified recombinant proteins.
  • Anion-exchange chromatography and reverse-phase HPLC for protein purification.
  • Identification of ATM substrates through phosphorylation analysis.

Main Results:

  • p32, an ASF/SF2-associated protein, was identified as a novel substrate of ATM in mouse heart.
  • ATM directly phosphorylates p32 in vitro.
  • Serine 148 (Ser 148) was identified as the specific ATM phosphorylation site on p32.

Conclusions:

  • ATM directly phosphorylates p32 at Ser 148 in cardiac cells.
  • This phosphorylation may represent a novel regulatory pathway for DNA damage response in the heart.
  • Further research into this pathway could lead to strategies for reducing chemotherapy-induced cardiotoxicity.

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