Cellular localization of neuronal nitric oxide synthase (NOS-1) in the human and rat retina

Neufeld, Arthur H.; Shareef, Shakeel; Peña, J

doi:10.1002/(sici)1096-9861(20000110)416:2<269::aid-cne11>3.0.co;2-2

Cited by 48 publications

(25 citation statements)

References 34 publications

(46 reference statements)

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“…In the retina, Ngb and NOS-expressing cell layers partially overlap, but do not show consistent co-localization: cells of the inner nuclear layer are Ngb-negative, but NOS-immunoreactive (41). The same is true for brain, where, e.g., the cerebellar Purkinje cells very actively produce Ngb under nonpathological conditions (20,21).…”

Section: In Good Company? Co-localization Of Ngb (And Cygb) With Othementioning

confidence: 99%

The Cellular and Subcellular Localization of Neuroglobin and Cytoglobin ‐ A Clue to Their Function?

Hankeln¹,

Wystub²,

Laufs³

et al. 2004

IUBMB Life

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SummaryNeuroglobin and cytoglobin are recently discovered respiratory proteins of vertebrates with yet ill-defined physiological functions. Neuroglobin is widely expressed in neurons, but not glia, in the vertebrate central and peripheral nervous systems. Other major expression sites are the retina and endocrine tissues. This distribution is indicative of a function of neuroglobin in metabolically most active, oxygen-consuming cell types, but does not yet allow to safely distinguish between different cellular roles, such as oxygen homeostasis, scavenging of reactive oxygen species or sustaining energy metabolism. Cytoglobin is predominantly expressed in connective tissue fibroblasts and related cell types in the body organs. Its main function may therefore be related to the specific metabolic properties of these cells, namely the production of massive amounts of extracellular matrix. Cytoglobin may hypothetically be involved in the oxygen-consuming maturation of collagen proteins. Cytoglobin is also expressed in distinct cell types of brain and retina. Its distribution strikingly differs from neuroglobin, suggesting an independent, yet unknown function. IUBMB Life, 56: 671-679, 2004

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Section: In Good Company? Co-localization Of Ngb (And Cygb) With Othementioning

confidence: 99%

The Cellular and Subcellular Localization of Neuroglobin and Cytoglobin ‐ A Clue to Their Function?

Hankeln¹,

Wystub²,

Laufs³

et al. 2004

IUBMB Life

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“…Previous studies reported the presence of NOSs in retinal neurons including RGCs. 29 These results may indicate that low amount of NO is essential for survival of RGCs.…”

Section: Discussionmentioning

confidence: 99%

Dual action of nitric oxide on purely isolated retinal ganglion cells

Kashiwagi

Ikoma²,

Tanaka³

et al. 2001

Current Eye Research

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“…Nitric oxide (NO) is a short-lived signaling molecule which is synthesized in the retina by vascular, neuronal, and glial cells in the presence of nitric oxide synthase (NOS) (Haberecht et al 1998;Neufeld et al 2000). NO is known to regulate various retinal functions including blood flow (Kiel 1999), neurotransmission (Koch et al 1994), inflammation (Bae et al 2007;Miura-Takeda et al 2008), and apoptosis (Liversidge et al 2002;Neufeld 1999;Tezel and Wax 2000).…”

Section: Introductionmentioning

confidence: 99%

Nitric Oxide Potentiates TNF-α-Induced Neurotoxicity Through Suppression of NF-κB

et al. 2011

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Modulation of enzyme activity through nitrosylation has recently been identified as a new physiological activity of nitric oxide (NO). We hypothesized that NO enhances the TNF-α-induced death of retinal neurons through a suppression of nuclear factor-κB (NF-κB) by nitrosylation. In this study, cells from the RGC-5 line were exposed to different concentrations (2.0, 10, and 50 ng/ml) of TNF-α, and the degree of TNF-α-induced cell death was determined by the WST-8 assay and by flow cytometric measurements of the externalization of phosphatidylserine. The effects of etanercept, a soluble TNFR-Fc fusion protein, and S-nitroso-N-penicillamine (SNAP), an NO donor, on the toxicity were determined. Experiments were also performed to determine whether nitric oxide synthase (NOS) was associated with the toxicity of TNF-α. The activation of NF-κB was determined by the detection of the p65 subunit in the nuclear extracts. Our results showed that exposure of RGC-5 cells to different concentrations of TNF-α significantly decreased the number of living cells in a dose-dependent way. The death was partially due to apoptosis with an externalization of phosphatidylserine, and the death was suppressed by etanercept. Exposure to TNF-α increased the activation of NF-κB and the expression of iNOS. Although NF-κB inhibitors suppressed the increase of iNOS, they also potentiated the TNF-α-induced death. Both L-NAME and aminoguanidine, both NOS inhibitors, rescued the cells from death. In contrast, addition of SNAP caused nitrosylation of the inhibitory κB kinase, and suppressed the NF-κB activation and potentiated the TNF-α-induced neurotoxicity. These results indicate that NO potentiates the neurotoxicity of TNF-α by suppressing NF-κB.

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Cellular localization of neuronal nitric oxide synthase (NOS-1) in the human and rat retina

Cited by 48 publications

References 34 publications

The Cellular and Subcellular Localization of Neuroglobin and Cytoglobin ‐ A Clue to Their Function?

The Cellular and Subcellular Localization of Neuroglobin and Cytoglobin ‐ A Clue to Their Function?

Dual action of nitric oxide on purely isolated retinal ganglion cells

Nitric Oxide Potentiates TNF-α-Induced Neurotoxicity Through Suppression of NF-κB

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