A Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
Open accessAbstract
Calcium/calmodulin (Ca2+/CaM)-dependent protein kinase II (CaMKII) couples increases in cellular Ca2+ to fundamental responses in excitable cells. CaMKII was identified over 20 years ago by activation dependence on Ca2+/CaM, but recent evidence shows that CaMKII activity is also enhanced by pro-oxidant conditions. Here we show that oxidation of paired regulatory domain methionine residues sustains CaMKII activity in the absence of Ca2+/CaM. CaMKII is activated by angiotensin II (AngII)-induced oxidation, leading to apoptosis in cardiomyocytes both in vitro and in vivo. CaMKII oxidation is reversed by methionine sulfoxide reductase A (MsrA), and MsrA-/- mice show exaggerated CaMKII oxidation and myocardial apoptosis, impaired cardiac function, and increased mortality after myocardial infarction. Our data demonstrate a dynamic mechanism for CaMKII activation by oxidation and highlight the critical importance of oxidation-dependent CaMKII activation to AngII and ischemic myocardial apoptosis.
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Myocardial infarction increases NOX2-derived ROS that activate apoptotic pathways such as ASK-1-p38MAPK and CAMKII.
“It has been reported that the myocardial infarction increases NOX2-derived ROS that activated apoptotic pathways such as Apoptosis signal-regulating kinase 1-p38 pathway ((ASK-1)-p38MAPK) and Ca2+/calmodulin-dependent protein kinase II (CAMKII).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Erickson et al. 2008
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Self-citation
- Authors
- Erickson, J. R., Joiner, M.-L. A., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O'Donnell, S. E., Aykin-Burns, N., Zimmerman, M. C., Zimmerman, K., Ham, A.-J. L., Weiss, R. M., Spitz, D. R., Shea, M. A., Colbran, R. J., Mohler, P. J., & Anderson, M. E.
- Affiliations
- University of Iowa (US)
- Vanderbilt University (US)
- Vanderbilt University Medical Center (US)
- Veterans Health Administration (US)
- Corresponding author
- Anderson, Mark E.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2008-05
- Volume
- 133
- Issue
- 3
- Pages
- 462-474
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC2435269
- OpenAlex
- W2091583229
- Cited by
- 1,122
- References
- 52
- Citations by year
- 2026: 35 · 2025: 52 · 2024: 37 · 2023: 53 · 2022: 62 · 2021: 79 · 2020: 68 · 2019: 61 · 2018: 60 · 2017: 64 · 2016: 64 · 2015: 73 · 2014: 89 · 2013: 93 · 2012: 74
- FWCI
- 21.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1903 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5r01hl083422-11)
- National Heart, Lung, and Blood Institute (R01HL084583, R01-HL-083422, R01HL079031, R01HL070250, R01HL062494)
- National Institute of Mental Health (R01MH063232)
- National Institute of General Medical Sciences (R01GM057001)
- National Center for Research Resources (K26RR017369, RR017369)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac electrophysiology and arrhythmias
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- CaMKII, methionine oxidation, angiotensin II, MsrA, cardiomyocyte apoptosis, myocardial infarction, oxidative stress, cardiac function
- MeSH terms
- Angiotensin II, Animals, Calcium, Calmodulin, Heart Diseases, Methionine, Oxidation-Reduction, Oxidoreductases, Signal Transduction, Mutagenesis, Site-Directed, Apoptosis, Reactive Oxygen Species, Myocytes, Cardiac, Methionine Sulfoxide Reductases, Mice, Rats, Calcium-Calmodulin-Dependent Protein Kinase Type 2
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