The DOI matches its Crossref record; 216 of the 216 references it cites were found in a registry or an index.
2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process
Open accessAbstract
Recent studies have revealed that the members of an ancient family of nonheme Fe(2+)/2-oxoglutarate-dependent dioxygenases (2-OGDO) are involved in the functions associated with the aging process. 2-Oxoglutarate and O2 are the obligatory substrates and Fe(2+) a cofactor in the activation of 2-OGDO enzymes, which can induce the hydroxylation of distinct proteins and the demethylation of DNA and histones. For instance, ten-eleven translocation 1-3 (TET1-3) are the demethylases of DNA, whereas Jumonji C domain-containing histone lysine demethylases (KDM2-7) are the major epigenetic regulators of chromatin landscape, known to be altered with aging. The functions of hypoxia-inducible factor (HIF) prolyl hydroxylases (PHD1-3) as well as those of collagen hydroxylases are associated with age-related degeneration. Moreover, the ribosomal hydroxylase OGFOD1 controls mRNA translation, which is known to decline with aging. 2-OGDO enzymes are the sensors of energy metabolism, since the Krebs cycle intermediate 2-oxoglutarate is an activator whereas succinate and fumarate are the potent inhibitors of 2-OGDO enzymes. In addition, O2 availability and iron redox homeostasis control the activities of 2-OGDO enzymes in tissues. We will briefly elucidate the catalytic mechanisms of 2-OGDO enzymes and then review the potential functions of the above-mentioned 2-OGDO enzymes in the control of the aging process.
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“The cause of these so-called 2-hydroxyglutaric acidurias (2HGAs) was attributed to germline mutations in L-2-HG dehydrogenase (L2HGDH) and D-2-HG dehydrogenase (D2HGDH), the mitochondrial enzymes responsible for the conversion of 2-HG to α-KG and thus its breakdown107-109.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [109]
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Metadata
- Authors
- Salminen, A., Kauppinen, A., & Kaarniranta, K.
- Affiliations
- University of Eastern Finland (FI)
- Corresponding author
- Kaarniranta, Kai
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2015-06-29
- Volume
- 72
- Issue
- 20
- Pages
- 3897-3914
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC11114064
- OpenAlex
- W1010999108
- Cited by
- 99
- References
- 216
- Citations by year
- 2026: 6 · 2025: 4 · 2024: 9 · 2023: 12 · 2022: 11 · 2021: 7 · 2020: 12 · 2019: 6 · 2018: 10 · 2017: 10 · 2016: 9 · 2015: 3
- FWCI
- 0.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Kuopion Yliopistollinen Sairaala
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- 2-oxoglutarate-dependent dioxygenase, aging, energy metabolism, oxygen availability, iron homeostasis, histone demethylation, DNA demethylation, mRNA translation, epigenetic regulation
- MeSH terms
- Aging, Animals, Hypoxia, Energy Metabolism, Homeostasis, Iron, Oxygen, Protein Biosynthesis, DNA Methylation, Epigenesis, Genetic, Dioxygenases
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