What is the function of neuroglobin?
Abstract
For a long time, haemoglobin and myoglobin had been assumed to represent the only globin types of vertebrates. In 2000, however, we discovered a third globin type by mining the genome sequence data. Based on a preferential expression in the nervous system, this globin is referred to as neuroglobin. Despite nine years of research, its function is still uncertain and a number of hypotheses have been put forward. Neuroglobin enhances cell viability under hypoxia and under various types of oxidative stress in transgenic systems, but does not appear to be strongly upregulated in response to stress. A close phylogenetic relationship with invertebrate nerve globins and its positive correlation with the oxidative metabolism and mitochondria suggest a role in O(2) supply. In vitro studies and cell culture experiments imply that neuroglobin may detoxify reactive oxygen or nitric oxide. Still other studies propose neuroglobin as being part of a signalling chain that transmits the redox state of the cell or that inhibits apoptosis. Although some functions are more probable than others, we conclude that it is still too early to definitively decide what may be the physiological role(s) of neuroglobin in vertebrates. Nevertheless, there is no doubt that neuroglobin has an essential, conserved function and is beneficial to neurons.
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Physiological levels of Ngb have been reported to be between 1 μM in the brain and up to 100 μM in the retina.
“Physiological levels of Ngb have been reported to be between 1 μM in the brain and up to 100 μM in the retina [63, 64].”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [64]
The rate of reduction of nitrite by Ngb in physiology depends on oxygenation state, pentacoordination, and pH.
“The rate of reduction of nitrite by Ngb in physiology depends on oxygenation state (with Ngb having an oxygen affinity similar to Mb [64]), pentacoordination, and pH.”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [64]
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- Authors
- Burmester, T., & Hankeln, T.
- Affiliations
- Universität Hamburg (DE)
- Johannes Gutenberg University Mainz (DE)
- Venue
- Journal of Experimental Biology
- Publisher
- The Company of Biologists
- Published
- 2009-05-15
- Volume
- 212
- Issue
- 10
- Pages
- 1423-1428
- ISSN
- 0022-0949 (ISSN-L)
- 1477-9145
- OpenAlex
- W2083043354
- Cited by
- 244
- References
- 50
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 3 · 2023: 8 · 2022: 8 · 2021: 9 · 2020: 13 · 2019: 13 · 2018: 9 · 2017: 21 · 2016: 18 · 2015: 19 · 2014: 22 · 2013: 24 · 2012: 17
- FWCI
- 10.24
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Experimental Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Health Sciences › Medicine › Surgery › Biomedical and Chemical Research
- Keywords
- neuroglobin, globin, hypoxia, oxidative stress, reactive oxygen species, nitric oxide, mitochondria, redox signaling, apoptosis, neurons, oxygen supply, phylogenetic relationships, oxidative metabolism
- MeSH terms
- Neuroglobin, Animals, Hypoxia, Gene Expression Regulation, Globins, Nerve Tissue Proteins, Nervous System, Neurons, Oxygen, Vertebrates, Reactive Oxygen Species, Reactive Nitrogen Species
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