Anatomical characterization of cytoglobin and neuroglobin mRNA and protein expression in the mouse brain

Hundahl, Christian Ansgar; Allen, Gregg C.; Hannibal, Jens; Kjær, Katrine; Rehfeld, Jens F.; Dewilde, Sylvia; Nyengaard, Jens Randel; Kelsen, Jens; Hay‐Schmidt, Anders

doi:10.1016/j.brainres.2010.03.056

Cited by 97 publications

(105 citation statements)

References 39 publications

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“…In brain, the elevated normoxic level of Cygb in Spalax vs. rat suggests involvement in the chronic hypoxia tolerance, as seen for Ngb and Mb. The colocalization of Cygb with nNOS in the GCL of the Spalax retina has been observed before in specific neuronal populations of the mouse brain (47,56) and may indicate that Cygb and nNOS interact functionally, for example by a delivery of O 2 from Cygb to nNOS during the production of NO or by scavenging excess NO.…”

Section: Increased Globin Levels In Spalax Indicate a Function In Hypsupporting

confidence: 61%

Neuroglobin, cytoglobin, and myoglobin contribute to hypoxia adaptation of the subterranean mole rat Spalax

Avivi

Gerlach²,

Joel³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

122

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The subterranean mole rat Spalax is an excellent model for studying adaptation of a mammal toward chronic environmental hypoxia. Neuroglobin (Ngb) and cytoglobin (Cygb) are O 2 -binding respiratory proteins and thus candidates for being involved in molecular hypoxia adaptations of Spalax. Ngb is expressed primarily in vertebrate nerves, whereas Cygb is found in extracellular matrix-producing cells and in some neurons. The physiological functions of both proteins are not fully understood but discussed with regard to O 2 supply, the detoxification of reactive oxygen or nitrogen species, and apoptosis protection. Spalax Ngb and Cygb coding sequences are strongly conserved. However, mRNA and protein levels of Ngb in Spalax brain are 3-fold higher than in Rattus norvegicus under normoxia. Importantly, Spalax expresses Ngb in neurons and additionally in glia, whereas in hypoxia-sensitive rodents Ngb expression is limited to neurons. Hypoxia causes an approximately 2-fold downregulation of Ngb mRNA in brain of rat and mole rat. A parallel regulatory response was found for myoglobin (Mb) in Spalax and rat muscle, suggesting similar functions of Mb and Ngb. Cygb also revealed an augmented normoxic expression in Spalax vs. rat brain, but not in heart or liver, indicating distinct tissue-specific functions. Hypoxia induced Cygb transcription in heart and liver of both mammals, with the most prominent mRNA up-regulation (12-fold) in Spalax heart. Our data suggest that tissue globins contribute to the remarkable tolerance of Spalax toward environmental hypoxia. This is consistent with the proposed cytoprotective effect of Ngb and Cygb under pathological hypoxic/ischemic conditions in mammals.

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Section: Increased Globin Levels In Spalax Indicate a Function In Hypsupporting

confidence: 61%

Neuroglobin, cytoglobin, and myoglobin contribute to hypoxia adaptation of the subterranean mole rat Spalax

Avivi

Gerlach²,

Joel³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

122

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“…Subcellular expression of Ngb in mitochondria of neuronal cells in regions of the brain with high metabolic activity (10,57) is an indicator of the implication of Ngb in cellular homeostasis in extant organisms and, by extension, in early metazoan neuronal cells. The Ngb-like sequences of certain cnidarians, protostomes, and deuterostomes exhibit a predicted N-terminal myristoylation site, indicating a possible interaction with membranes, putatively including those of the mitochondria (Fig.…”

Section: In the Cnidarian C Hemisphaerica Two Globins (Chengb1 And mentioning

confidence: 99%

Neuroglobins, Pivotal Proteins Associated with Emerging Neural Systems and Precursors of Metazoan Globin Diversity

Lechauve

Jager

Laguerre

et al. 2013

Journal of Biological Chemistry

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Background: Neuroglobins are expressed in vertebrate neurons. Results: Neuroglobins are located in neural systems of two basal animals (acoels and jellyfish) and are ubiquitous in metazoan transcriptomes. Conclusion: Neuroglobin was recruited in neural cell prototypes and later co-opted in hemoglobin-based blood systems. Significance: The universality of neuroglobins sheds new light on the origin and evolution of globins.

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“…Cygb has, despite low sequence homology with the canonical hemoglobin and myoglobin, retained the classical globin fold and can reversibly bind oxygen and other diatomic gasses (7). Cygb is expressed in a number of tissues and is also found in neurons of the brain where Cygb is localized in the soma, neuronal processes and nuclei (8,9). Within the mouse brain, Cygb is expressed in distinct areas with large regional differences in the expression levels.…”

Section: Introductionmentioning

confidence: 99%

Neurochemical phenotype of cytoglobin-expressing neurons in the rat hippocampus

2014

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Abstract. Cytoglobin (Cygb), a novel oxygen-binding protein, is expressed in the majority of tissues and has been proposed to function in nitric oxide (NO) metabolism in the vasculature and to have cytoprotective properties. However, the overall functions of Cygb remain elusive. Cygb is also expressed in a subpopulation of brain neurons. Recently, it has been shown that stress upregulates Cygb expression in the brain and the majority of neuronal nitric oxide synthase (nNOS)-positive neurons, an enzyme that produces NO, co-express Cygb. However, there are more neurons expressing Cygb than nNOS, thus a large number of Cygb neurons remain uncharacterized by the neurochemical content. The aim of the present study was to provide an additional and more detailed neurochemical phenotype of Cygb-expressing neurons in the rat hippocampus. The rat hippocampus was chosen due to the abundance of Cygb, as well as this limbic structure being an important target in a number of neurodegenerative diseases. Using triple immunohistochemistry, it was demonstrated that nearly all the parvalbumin-and heme oxygenase 1-positive neurons co-express Cygb and to a large extent, these neuron populations are distinct from the population of Cygb neurons co-expressing nNOS. Furthermore, it was shown that the majority of neurons expressing somastostatin and vasoactive intestinal peptide also co-express Cygb and nNOS. Detailed information regarding the neurochemical phenotype of Cygb neurons in the hippocampus can be a valuable tool in determining the function of Cygb in the brain.

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Anatomical characterization of cytoglobin and neuroglobin mRNA and protein expression in the mouse brain

Cited by 97 publications

References 39 publications

Neuroglobin, cytoglobin, and myoglobin contribute to hypoxia adaptation of the subterranean mole rat Spalax

Neuroglobin, cytoglobin, and myoglobin contribute to hypoxia adaptation of the subterranean mole rat Spalax

Neuroglobins, Pivotal Proteins Associated with Emerging Neural Systems and Precursors of Metazoan Globin Diversity

Neurochemical phenotype of cytoglobin-expressing neurons in the rat hippocampus

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