Differential roles of ATR and ATM in p53, Chk1, and histone H2AX phosphorylation in response to hyperoxia: ATR-dependent ATM activation
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Elevated level of oxygen (hyperoxia) is widely used in critical care units and in respiratory insufficiencies. In addition, hyperoxia has been implicated in many diseases such as bronchopulmonary dysplasia or acute respiratory distress syndrome. Although hyperoxia is known to cause DNA base modifications and strand breaks, the DNA damage response has not been adequately investigated. We have investigated the effect of hyperoxia on DNA damage signaling and show that hyperoxia is a unique stress that activates the ataxia telangiectasia mutant (ATM)- and Rad3-related protein kinase (ATR)-dependent p53 phosphorylations (Ser6, -15, -37, and -392), phosphorylation of histone H2AX (Ser139), and phosphorylation of checkpoint kinase 1 (Chk1). In addition, we show that phosphorylation of p53 (Ser6) and histone H2AX (Ser139) depend on both ATM and ATR. We demonstrate that ATR activation precedes ATM activation in hyperoxia. Finally, we show that ATR is required for ATM activation in hyperoxia. Taken together, we report that ATR is the major DNA damage signal transducer in hyperoxia that activates ATM.
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Hyperoxic conditions (95% oxygen versus normal 21%) cause phosphorylation of Chk1 at serine 345 and p53 at serine 15, serine 37, and serine 392 in an ATR-dependent but ATM-independent manner in A549 lung adenocarcinoma cells.
“Hyperoxic conditions (95 % oxygen versus the normal 21 % oxygen) resulted in the phosphorylation of Chk1 (Serine 345) and p53 (Serine 15, Serine 37, and Serine 392) in an ATR-dependent but ATM-independent fashion in the lung adeno-carcinoma cell line A549 [136].”
From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [136]
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A systems biology approach to DNA damage repair
Dolan, D. (2013)
- Authors
- Kulkarni, A., & Das, K. C.
- Affiliations
- University of Arkansas for Medical Sciences (US)
- Venue
- American Journal of Physiology-Lung Cellular and Molecular Physiology
- Publisher
- American Physiological Society
- Published
- 2008-05
- Volume
- 294
- Issue
- 5
- Pages
- L998-L1006
- ISSN
- 1040-0605 (ISSN-L)
- 1522-1504
- PMC
- PMC8786037
- OpenAlex
- W2110998353
- Cited by
- 56
- References
- 53
- Citations by year
- 2026: 6 · 2025: 1 · 2024: 4 · 2022: 4 · 2021: 2 · 2020: 2 · 2019: 2 · 2018: 1 · 2017: 3 · 2016: 5 · 2015: 2 · 2014: 7 · 2013: 5
- FWCI
- 1.65
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- American Journal of Physiology-Lung Cellular and Molecular Physiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (1r43hl055807-01)
- National Heart, Lung, and Blood Institute (HL-55807, R01HL071558)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Effects of Radiation Exposure
- Keywords
- hyperoxia, ATR kinase, ATM kinase, p53 phosphorylation, Chk1 phosphorylation, H2AX phosphorylation, DNA damage response, oxygen toxicity, DNA strand breaks, DNA base modification
- MeSH terms
- Checkpoint Kinase 1, Adenocarcinoma, DNA Repair, DNA-Binding Proteins, Histones, Humans, Lung Neoplasms, Phosphorylation, Protein Kinases, Serine, Signal Transduction, Tumor Suppressor Protein p53, Apoptosis, Protein Serine-Threonine Kinases, Hyperoxia, Cell Cycle Proteins, Tumor Suppressor Proteins, RNA Interference, Cell Line, Tumor, Casein Kinase II, Adaptor Proteins, Signal Transducing, Ataxia Telangiectasia Mutated Proteins
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