Heat shock induces phosphorylation of histone H2AX in mammalian cells.
Heat shock induces a variety of biological events including gene activation, cell cycle arrest, and apoptosis. Heat shock has recently been shown to be potentially useful when combined with radiation in cancer therapy, probably because, in mammalian cells, heat inhibits the repair of double-strand breaks (DSBs) induced by ionizing radiation. It remains unclear, however, whether heat shock by itself induces DSBs. In this communication, we present the first evidence that heat shock induces the phosphorylated form of histone H2AX, which is thought to be generated at the chromatin proximal to DSB sites. These results suggest that heat shock induces DSBs in mammalian cells and may provide direct evidence to explain previous reports on DSB-related events occurring after heat shock treatment.
Kaneko
Haruna
H
Molecular Diagnosis and Therapeutics, Department of Oral Restitution, Graduate School, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8549, Japan.
Igarashi
Kaori
K
Kataoka
Keiko
K
Miura
Masahiko
M
D000818:Animals; D002417:Cattle; D002478:Cells, Cultured / Q000528:radiation effects; D004249:DNA Damage / Q000528:radiation effects*; D004260:DNA Repair / Q000528:radiation effects*; D004307:Dose-Response Relationship, Radiation; D005786:Gene Expression Regulation / Q000502:physiology / Q000528:radiation effects; D018869:Heat-Shock Response / Q000502:physiology* / Q000528:radiation effects*; D006657:Histones / Q000378:metabolism* / Q000528:radiation effects*; D006358:Hot Temperature; D006801:Humans; D051379:Mice; D010766:Phosphorylation / Q000528:radiation effects; D011839:Radiation, Ionizing; D015533:Transcriptional Activation
C468783:H2AX protein, human; D006657:Histones