Anoxia or oxygen and glucose deprivation in SH-SY5Y cells: A step closer to the unraveling of neuroglobin and cytoglobin functions

Fordel, Elke; Thijs, Liesbet; Martinet, Wim; Schrijvers, Dorien M.; Moëns, Luc; Dewilde, Sylvia

doi:10.1016/j.gene.2007.03.022

Cited by 111 publications

(86 citation statements)

References 35 publications

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“…However, the low concentration (in the micromolar range) of Ngb in brain tissues except for the retina perhaps argues against a role for Ngb in storing and carrying significant amounts of O 2 . Alternatively, Ngb may act as an intracellular scavenger of ROS and/or nitric oxide (NO) (5,(52)(53)(54). It has been reported that both H64V HNgb and Mb generate very reactive cytotoxic ferryl (Fe 4ϩ ) species upon treatment of the ferric form with peroxide (42).…”

Section: Discussionmentioning

confidence: 99%

Human Neuroglobin Functions as an Oxidative Stress-responsive Sensor for Neuroprotection

Watanabe

Takahashi

Uchida

et al. 2012

Journal of Biological Chemistry

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Background: Mammalian neuroglobin (Ngb) is involved in neuroprotection under oxidative stress conditions. Results: Only under oxidative stress, human Ngb was recruited to lipid rafts by interacting with flotillin-1 and suppressed the activation of G␣ i/o by acting as its guanine nucleotide dissociation inhibitor. Conclusion: Human Ngb acts as an intracellular oxidative stress-responsive sensor to protect against cell death. Significance: The neuroprotective mechanism of human Ngb was revealed.

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Section: Discussionmentioning

confidence: 99%

Human Neuroglobin Functions as an Oxidative Stress-responsive Sensor for Neuroprotection

Watanabe

Takahashi

Uchida

et al. 2012

Journal of Biological Chemistry

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“…Hypoxia followed by reoxygenation causes overproduction of reactive oxygen species (ROS), and there is evidence to suggest that CYGB may protect cells against these ROS under conditions of limited oxygen supply by acting as a ROS scavenger (73,74). As cancer cells are exposed to oxidative stress (75,76), it is possible that CYGB may func-tion as a ROS scavenger in a developing tumour, and loss or decreased CYGB expression may contribute to tumourigenesis.…”

Section: Discussionmentioning

confidence: 99%

Chromosome 17q25 genes, RHBDF2 and CYGB, in ovarian cancer

et al. 2012

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Abstract. It has been proposed that the frequent loss of heterozygosity (LOH) of an entire chromosome 17 contig in epithelial ovarian cancers (EOC) is the consequence of the inactivation of multiple tumour suppressor genes on this chromosome. We report the characterization of a 453 Kb 17q25 locus shown previously to exhibit a high frequency of LOH in EOC samples. LOH analysis further defined the minimal region of deletion to a 65 Kb interval flanked by D17S2239 and D17S2244, which contains RHBDF2, CYGB and PRCD as tumour suppressor gene candidates. Tissue specific expression excluded PRCD as a candidate. RHBDF2 was expressed at low levels in the majority of benign and low malignant potential (LMP) tumours, and in a subset of malignant ovarian tumour samples, as compared with primary cultures of normal ovarian surface epithelial cell (NOSE) samples. CYGB was expressed at low levels in the majority of LMP and malignant samples compared with benign and NOSE samples. In contrast to CYGB expression, RHBDF2 was expressed at low or undetectable levels in EOC cell lines exhibiting tumourigenic characteristics and up-regulated in a genetically modified EOC cell line rendered non-tumourigenic. DNA sequence analysis identified variants but no apparent deleterious mutations in either gene. Methylation-specific PCR analysis suggested that promoter methylation of CYGB but not RHBDF2 occurred in 6 of 31 malignant samples. The results combined suggest that RHBDF2 and CYGB may play distinctive roles in ovarian cancer and could be added to the growing roster of chromosome 17 genes implicated in this disease.

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“…Reverse transcription was performed using Moloney murine leukemia virus reverse transcriptase (M-MLV-RT) (Invitrogen, Carlsbad, CA) to obtain cDNA. In a nuclease-free microcentrifuge tube, 1 L of 50 mol/L oligo(dT) 20 , 11 L of total RNA (1 ng to 5 g total RNA), and 1 L of 10 mmol/L dNTP mix were added into 12 L sterile distilled water. The mixture was heated at 65°C for 5 minutes and quickly chilled on ice.…”

Section: Quantification Of Ngb Expression With Rt-qpcr and Western Blotmentioning

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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Anoxia or oxygen and glucose deprivation in SH-SY5Y cells: A step closer to the unraveling of neuroglobin and cytoglobin functions

Cited by 111 publications

References 35 publications

Human Neuroglobin Functions as an Oxidative Stress-responsive Sensor for Neuroprotection

Human Neuroglobin Functions as an Oxidative Stress-responsive Sensor for Neuroprotection

Chromosome 17q25 genes, RHBDF2 and CYGB, in ovarian cancer

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

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