NGB

Official Full Name

neuroglobin

Organism

Homo sapiens

GeneID

58157

Background

This gene encodes an oxygen-binding protein that is distantly related to members of the globin gene family. It is highly conserved among other vertebrates. It is expressed in the central and peripheral nervous system where it may be involved in increasing oxygen availability and providing protection under hypoxic/ischemic conditions. [provided by RefSeq, Jul 2008]

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Detailed Information

Neuroglobin (NGB) is a new oxygen-carrying globulin discovered by Burmester in Germany in 2000. It was first discovered in human and mouse brains. NGB is widely distributed in brain tissues such as cerebral cortex, hippocampus, thalamus, olfactory bulb, hypothalamus and cerebellum, which are active in metabolism and consumes oxygen. It is also thought to exist in the peripheral nervous system as well as in the retina and endocrine system. It is rare in reticular structures and nucleus of the pons; it is mainly located in the cytoplasm of neurons. In recent years, evidences of immunohistochemical staining, yeast two-hybrid assays, and biochemical studies suggest that NGB is also present in mitochondria.

NGB Structure and Biological Function

The structure of human NGB is a typical globular fold, which contains 151 amino acids (molecular weight 17 kDa) and has only 20% to 25% sequence identity with myoglobin (MB) and hemoglobin (HGB). According to the study, under normal physiological conditions, NGB accounts for about 30% of the total cell concentration. Under hypoxic conditions, many neuroprotective hypoxia-inducible genes (such as hypoxia-inducible factor-1α, vascular endothelial growth factor, heme plus Oxygenase-1 and erythropoietin are upregulated to help promote cell survival, which causes NGB to rise rapidly to approximately 80%, and studies suggest that this increase occurs between a few seconds. In combination with these hypoxia-inducible genes, NGB expression is thought to increase neuronal responses to hypoxia, and increased expression protects neurons from cell death and reactive oxygen species damage. In cerebral ischemia and hypoxia, increased expression of NGB mRNA leads to an increase in NGB in neurons. As an endogenous neuroprotective factor, it can enhance the tolerance of brain tissue to ischemia and hypoxia injury. Endogenous NGB and NGB overexpressed by gene transfection have neuroprotective functions.

Figure 1. Currently known mechansims of neuroglobin (Ngb) functions in the brain. (Xie, L. K., et al. 2016)

Clinical Application of NGB

Neuroglobin plays an important role in oxygen storage and oxygen utilization, and is therefore of great significance in clinical diseases such as hypoxic-ischemic neurological diseases and neurodegenerative diseases. The study proposes to use protein transduction technology to introduce neuroprotective proteins into the brain of ischemic models to treat cerebral hypoxic ischemic diseases. Therefore, if the NGB oxygen-carrying carrier can be used in the early stage to intervene in the development of cerebral ischemia and hypoxia, it is possible to fundamentally prevent and treat cerebral hypoxia.

Stroke has a very high mortality and morbidity, and the current treatment effect is limited. The study found that the area of cerebral ischemic infarction after the middle cerebral artery occlusion of mice overexpressing NGB was reduced, and NGB was proposed as a new target for stroke treatment. Ischemic preconditioning in patients undergoing intracranial aneurysm clipping can up-regulate NGB expression and improve the body's tolerance to hypoxia. Post-traumatic brain injury is also caused by cerebral ischemia and hypoxia due to insufficient cerebral hypoperfusion or direct short-term respiratory depression. Taylor et al. found that overexpression of NGB significantly improved traumatic brain injury in mice. Lan et al. found that rats transfected with NGB recovered better after spinal cord injury (SCI), and the number of neuronal apoptosis was greatly reduced, which also confirmed the protective effect of NGB in cerebral ischemia and anoxia. In the episode, nerve impulses erupt, oxygen needs to increase, and local neuron is relatively hypoxic. If NGB is used as an oxygen carrier in clinical practice, its neuroprotective effect will reduce neuronal damage caused by epileptic seizures.

References:

Xie, L. K. , & Yang, S. H. . (2016). Brain globins in physiology and pathology. Medical Gas Research, 6(3), 154-163.
Diego, G. , Cinzia, T. , Manuela, M. , Guido, M. , & Luigi, A. . (2016). Neuroglobin, a factor playing for nerve cell survival. International Journal of Molecular Sciences, 17(11), 1817-.
Taylor, J. M. , Kelley, B. , Gregory, E. J. , & Berman, N. E. J. . (2014). Neuroglobin overexpression improves sensorimotor outcomes in a mouse model of traumatic brain injury. Neuroscience Letters, 577, 125-129.

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