neuroglobin


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neuroglobin

A monomeric, intracellular haemoprotein encoded by NGB on chromosome 14q24.3, which is present in the central and peripheral nervous systems, CSF, retina and endocrine tissues, and involved in oxygen homeostasis. It reversibly binds oxygen with an affinity higher than that of haemoglobin, increases oxygen availability to the brain via nitric oxide and protects the brain during hypoxia and ischaemia, improving neurone survival and recovery.

neuroglobin

An oxygen-transport material in the brain analogous to haemoglobin in the blood and myoglobin in the muscles. Neuroglobin is a small protein of 151 amino acids. It is thought to have a neuroprotective effect in cerebral ischaemia, but its full function remains unelucidated.
References in periodicals archive ?
Leone et al., "Neuroglobin in Breast Cancer Cells: Effect of Hypoxia and Oxidative Stress on Protein Level, Localization, and Anti-Apoptotic Function," PLoS ONE, vol.
Xiong et al., "Neuroglobin promotes neurite outgrowth via differential binding to PTEN and Akt," Molecular Neurobiology, vol.
It has been demonstrated that non-symbiotic hemoglobin is predominantly expressed in different parts of beetroot, including leaves and roots and has structural similarity to neuroglobin, a hexacoordinated Fe-centred hemoglobin present in thebrain (Leiva-Eriksson et al., 2014).
Expression and role of neuroglobin in rats with sepsis-associated encephalopathy.
Neuroglobin, a protein that needs to be identified by in-depth research lab, and cannot be detected by current MS-based proteomics technology (54).
Marino, "Neuroglobin upregulation induced by 17[beta]-estradiol sequesters cytocrome c in the mitochondria preventing [H.sub.2][O.sub.2]induced apoptosis of neuroblastoma cells," Cell Death and Disease, vol.
2010: Neuroglobin, cytoglobin, and myoglobin contribute to hypoxia adaptation of the subterranean mole rat Spalax.
Effects of neuroglobin overexpression on mitochondrial function and oxidative stress following hypoxia/reoxygenation in cultured neurons.
CYGB is the fourth member of the globin family, which previously consisted of hemoglobin (Hb, first member), myoglobin (Mb, second), and neuroglobin (Ngb, third), whose common feature is their high affinity for molecular oxygen ([O.sub.2]) through the heme iron located at the center of the porphyrin ring.
Transgenic overexpression of neuroglobin attenuates formation of smoke-inhalation-induced oxidative DNA damage, in vivo, in the mouse brain.