Expression and Cell Distribution of Neuroglobin in the Brain Tissue After Experimental Subarachnoid Hemorrhage in Rats: A Pilot Study
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Neuroglobin (Ngb) is a member of the globin superfamily expressed mainly in the nervous system and retina of vertebrates. Accumulated evidence has clearly demonstrated that Ngb has a neuro-protective role enhancing cell viability under hypoxia and other types of oxidative stress. It was suggested that oxidant stress could play an important role in neuronal injury after subarachnoid hemorrhage (SAH). The present study aims to examine the expression of Ngb in the temporal cortex and its cellular localization after SAH. We used a prechiasmatic cistern model of SAH. Ngb expression was examined at 3, 6, 12, 24, 48, and 72 h after SAH by western blot analysis and real-time polymerase chain reaction (PCR). Immunohistochemistry and immunofluorescence were performed to detect the localization of Ngb. Real-time PCR demonstrated that Ngb mRNA levels increased from 3 h after SAH, peaked at 6 h. Western blot showed Ngb protein levels were significantly increased in SAH groups in the temporal cortex and reached the peak at 24 h after SAH. The immunohistochemical staining demonstrated that Ngb was weakly expressed in the cortex in the control group while the enhanced expression of Ngb could be detected in the SAH groups. In addition, immunofluorescence results revealed that the over-expressed Ngb was located in the neuronal and microglia cell cytoplasm. These findings indicated that Ngb might play an important neuro-protective effect after SAH.
KeywordsSubarachnoid hemorrhage Neuroglobin Rat cortex Expression
This work was supported by grants from National Natural Science Foundation of China (No. 81171170, 81371294), and the Military Medical Scientific and Technological Innovation Project (10Z024).
Conflict of interest
The authors have declared no conflict of interest.
- Dewilde S, Kiger L, Burmester T, Hankeln T, Baudin-Creuza V, Aerts T, Marden MC, Caubergs R, Moens L (2001) Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family. J Biological Chem 276(42):38949–38955. doi: 10.1074/jbc.M106438200 CrossRefGoogle Scholar
- Duong TT, Witting PK, Antao ST, Parry SN, Kennerson M, Lai B, Vogt S, Lay PA, Harris HH (2009) Multiple protective activities of neuroglobin in cultured neuronal cells exposed to hypoxia re-oxygenation injury. J Neurochem 108(5):1143–1154. doi: 10.1111/j.1471-4159.2008.05846.x PubMedCrossRefGoogle Scholar
- Fago A, Hundahl C, Dewilde S, Gilany K, Moens L, Weber RE (2004) Allosteric regulation and temperature dependence of oxygen binding in human neuroglobin and cytoglobin. Molecular mechanisms and physiological significance. J Biological Chem 279(43):44417–44426. doi: 10.1074/jbc.M407126200 CrossRefGoogle Scholar
- Khan AA, Wang Y, Sun Y, Mao XO, Xie L, Miles E, Graboski J, Chen S, Ellerby LM, Jin K, Greenberg DA (2006) Neuroglobin-overexpressing transgenic mice are resistant to cerebral and myocardial ischemia. Proc Natl Acad Sci USA 103(47):17944–17948. doi: 10.1073/pnas.0607497103 PubMedCrossRefGoogle Scholar
- Pluta RM, Hansen-Schwartz J, Dreier J, Vajkoczy P, Macdonald RL, Nishizawa S, Kasuya H, Wellman G, Keller E, Zauner A, Dorsch N, Clark J, Ono S, Kiris T, Leroux P, Zhang JH (2009) Cerebral vasospasm following subarachnoid hemorrhage: time for a new world of thought. Neurological Res 31(2):151–158. doi: 10.1179/174313209X393564 CrossRefGoogle Scholar
- Sun Q, Dai Y, Zhang X, Hu YC, Zhang D, Li W, Zhang XS, Zhu JH, Zhou ML, Hang CH (2013) Expression and cell distribution of myeloid differentiation primary response protein 88 in the cerebral cortex following experimental subarachnoid hemorrhage in rats: a pilot study. Brain Res 1520:134–144. doi: 10.1016/j.brainres.2013.05.010 PubMedCrossRefGoogle Scholar
- Tiso M, Tejero J, Basu S, Azarov I, Wang X, Simplaceanu V, Frizzell S, Jayaraman T, Geary L, Shapiro C, Ho C, Shiva S, Kim-Shapiro DB, Gladwin MT (2011) Human neuroglobin functions as a redox-regulated nitrite reductase. J Biological Chem 286(20):18277–18289. doi: 10.1074/jbc.M110.159541 CrossRefGoogle Scholar