A vertebrate globin expressed in the brain

Burmester, Thorsten; Weich, Bettina; Reinhardt, Sigrid; Hankeln, Thomas

doi:10.1038/35035093

Cited by 944 publications

(1,075 citation statements)

References 24 publications

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“…Neuroglobin (NGB) is a novel member of the globin superfamily that is distantly related to hemoglobin and myoglobin. 1 A highly conserved protein in evolution, human and mouse Ngb, both comprised of 151 amino acids, are 94% identical. 2,3 In mammals, expression of NGB is found in the brain, retina, and other nerve tissues, predominantly in neurons but absent from glial cells.…”

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confidence: 99%

Neuroglobin Is an Endogenous Neuroprotectant for Retinal Ganglion Cells against Glaucomatous Damage

Wei

Cho

et al. 2011

The American Journal of Pathology

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Neuroglobin (NGB), a newly discovered member of the globin superfamily, may regulate neuronal survival under hypoxia or oxidative stress. Although NGB is greatly expressed in retinal neurons, the biological functions of NGB in retinal diseases remain largely unknown. We investigated the role of NGB in an experimental model of glaucoma, a neurodegenerative disorder that usually involves elevation of intraocular pressure (IOP). Elevated IOP is thought to induce oxidative stress in retinal ganglion cells (RGCs), thereby causing RGC death and, eventually, blindness. We found that NGB plays a critical role in increasing RGC resistance to ocular hypertension and glaucomatous damage. Neuroglobin (NGB) is a novel member of the globin superfamily that is distantly related to hemoglobin and myoglobin. 1 A highly conserved protein in evolution, human and mouse Ngb, both comprised of 151 amino acids, are 94% identical. 2,3 In mammals, expression of NGB is found in the brain, retina, and other nerve tissues, predominantly in neurons but absent from glial cells. 4 -7 Distribution of NGB protein in the normal human retina is very similar to what has been described in mice: NGB is detected primarily in the plexiform layers and photoreceptor inner segments, which are rich in mitochondria and synapses and consume high amounts of oxygen. 8,9 NGB has been shown to act as an endogenous neuroprotective molecule that enhances neuronal survival under hypoxic-ischemic insults in the brain 10 -12 ; however, its physiological functions and molecular mode of actions are not fully understood. Of note, NGB is present at a 100-fold greater concentration in the retina than in the brain, 8,[13][14][15] suggesting that the retina may be its most important site of function; however, among the many unknown roles of NGB, functional significance of NGB expression in the retina has been largely unexplored.

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confidence: 99%

Neuroglobin Is an Endogenous Neuroprotectant for Retinal Ganglion Cells against Glaucomatous Damage

Wei

Cho

et al. 2011

The American Journal of Pathology

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“…Organisms express multiple globins that have variant characteristics and functions. Vertebrates typically express hemoglobin in blood, myoglobin in muscle, neuroglobin in nervous tissue, and cytoglobin in several tissues (3,4). GbE, the eye-specific globin in the domestic chicken and ''globin X'' (GbX) in fish and amphibians were recently discovered (5,6).…”

Section: Introductionmentioning

confidence: 99%

GLB‐13 is associated with oxidative stress resistance in caenorhabditis elegans

Ren

Han

et al. 2013

IUBMB Life

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Globins constitute a superfamily of heme-binding proteins that is widely present in many species. There are 33 putative globins in the genome of Caenorhabditis elegans, where glb-13 is a homolog of neuroglobin (Ngb) based on sequence analysis and specific expression in neurons. Here we examined whether glb-13 as well as Ngb is also associated with resistance to reactive oxygen species (ROS) induced by paraquat. Our results showed that the mRNA level of glb-13 was significantly upregulated after paraquat exposure. Expression of a green fluorescent protein (GFP) reporter gene directed by the glb-13 promoter was increased by paraquat exposure. The mutant C. elegans strain glb-13(tm2825) was sensitive to paraquat-induced oxidative stress. Overexpression of human Ngb (hNgb) in C. elegans neuronal cells can rescue the paraquat sensitive phenotype of the mutant strain. glb-13 mutation or hNgb overexpression did not affect the expression of antioxidant enzymes such as superoxide dismutase (SOD). To examine the ROS-scavenging capabilities of hNgb and glb-13, we further examined the level of ROS in glb-13 mutant and hNgb transgenic (hNgb-Tg) worms. There was no statistical difference in ROS levels in the untreated controls; however in paraquattreated worms, the ROS level was statistically repressed in the hNgb-Tg relative to enhanced green fluorescent protein (EGFP)-Tg worms or wildtype animals. Additionally, the ROS level of glb-13 mutant was statistically higher than the wildtype animals. Furthermore, hNgb overexpression diminished the ROS level of glb-13 mutant. In conclusion, hNgb can rescue the ROS sensitive phenotype of the glb-13 mutant strain. The protein GLB-13 seems to have an hNgb-like function, suggesting the importance of the globin protein family in maintaining the homeostasis of ROS signals. Our data provided evidence for the first time that glb-13 is associated with the resistance against oxidative stress-induced toxicity.

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“…Neuroglobin (Ngb) is a recently discovered globin [1][2][3][4] and it is thought to be of ancient evolutionary origin. Ngb is found in all vertebrates in small amounts, and is expressed mainly in nervous tissues [1].…”

Section: Introductionmentioning

confidence: 99%

“…Ngb is found in all vertebrates in small amounts, and is expressed mainly in nervous tissues [1]. The biological function of Ngb is still not clear, but it has been hypothesised that it is involved in transport and storage of O 2 , in scavenging of ROS (reactive oxygen species) and NO (nitric oxide), and in Gprotein signalling and binding of CO [5].…”

Section: Introductionmentioning

confidence: 99%

Cloning, expression and purification of Atlantic salmon (Salmo salar, L.) neuroglobin

Bjørlykke

Kvamme

Slinde

et al. 2012

Protein Expression and Purification

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Abbreviations: Ngb: neuroglobin, sNgb: salmon neuroglobin, hNgb: human neuroglobin, CO: carbon monoxide, ROS: reactive oxygen species, MBP: maltose binding protein. AbstractNeuroglobin (Ngb) exists only in small amounts in salmon brain. In order to study the protein in more detail salmon neuroglobin (sNgb) was cloned, hetereologously expressed in E.coli and purified. The protein had red color and showed the characteristic peaks at 411 nm (metNgb), 415 nm (carboxyNgb) and 424 nm (deoxyNgb). Western analysis showed that sNgb reacted weakly against a rabbit anti human neuroglobin (hNgb) and strongly to a sNgb specific antibody. Our 3D-homology model of the sNgb indicated modifications adjacent to and in the O 2 /CO binding site. This may correlate to differences in substrate affinities for the sNgb compared to the hNgb. Also sNgb contained shorter helixes and longer interhelical loops typical for psycrophilic proteins.

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A vertebrate globin expressed in the brain

Cited by 944 publications

References 24 publications

Neuroglobin Is an Endogenous Neuroprotectant for Retinal Ganglion Cells against Glaucomatous Damage

Neuroglobin Is an Endogenous Neuroprotectant for Retinal Ganglion Cells against Glaucomatous Damage

GLB‐13 is associated with oxidative stress resistance in caenorhabditis elegans

Cloning, expression and purification of Atlantic salmon (Salmo salar, L.) neuroglobin

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