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Keywords {🔍}

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Topics {✒️}

carbobenzoxy-valyl-alanyl-aspartyl-[o-methyl]-fluoromethylketone n-methyl-d-aspartic acid oxygen-glucose deprivation injury pressure-induced ischaemia-reperfusion insult oxygen-glucose deprivation combined ischemia–reperfusion-induced retinal damage tnf-related apoptosis-inducing ligand hrp-conjugated secondary antibodies vitro oxygen-glucose deprivation apoptosis-inducing factor-mediated necroptosis glutamate-induced glutathione depletion dulbecco’s-modified essential medium 10 μg/ml pi-dye solution receptor-interacting protein 3 receptor interacting protein ethanol-induced hepatocyte injury caspase-independent cell death article download pdf anti-oxidative monomer extracted rabbit anti-rip3 antibody induce aif-mediated necroptosis oxygen glucose deprivation oxygen–glucose deprivation cdgsh iron-sulfur domain ubiquitin c-terminal hydrolase examined tnf-induced necrosis tnfalpha-induced necroptosis downstream central retinal artery anti-fading mounting medium rabbit anti-β-tubulin rip3-dependent protein phosphorylation anti-sense morpholino oligos retinal ganglion cell ogd-induced neuronal damage sds–polyacrylamide gel electrophoresis ogd-induced rgc-5 necroptosis full size image central south university reactive oxygen species ganglion cell layer neuronal injury induced rip3-knockdown cells compared rip3-knockdown rgc-5 necrosis li-xiang xue dopamine receptor agonist inflammatory responses induced glucose-free dmem tnf-induced necroptosis pressure-induced death related subjects

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         headline:Receptor interacting protein 3-induced RGC-5 cell necroptosis following oxygen glucose deprivation
         description:Necroptosis is a type of regulated form of cell death that has been implicated in the pathogenesis of various diseases. Receptor-interacting protein 3 (RIP3), a member of the RIP family of proteins, has been reported as an important necroptotic pathway mediator in regulating a variety of human diseases, such as myocardial ischemia, inflammatory bowel disease, and ischemic brain injury. Our previous study showed that RIP3 was expressed in rat retinal ganglion cells (RGCs), where it was significantly upregulated during the early stage of acute high intraocular pressure. Furthermore, RIP3 expression was co-localized with propidium iodide (PI)-positive staining (necrotic cells). These results suggested that RIP3 up-regulation might be involved in the necrosis of injured RGCs. In this study, we aimed to reveal the possible involvement of RIP3 in oxygen glucose deprivation (OGD)-induced retinal ganglion cell-5 (RGC-5) necroptosis. RGC-5 cells were cultured in Dulbecco’s-modified essential medium and necroptosis was induced by 8 h OGD. PI staining and flow cytometry were performed to detect RGC-5 necrosis. RIP3 expression was detected by western blot and flow cytometry was used to detect the effect of RIP3 on RGC-5 necroptosis following OGD in rip3 knockdown cells. Malondialdehyde (MDA) lipid peroxidation assay was performed to determine the degree of oxidative stress. PI staining showed that necrosis was present in the early stage of OGD-induced RGC-5 cell death. The presence of RGC-5 necroptosis after OGD was detected by flow cytometry using necrostatin-1, a necroptosis inhibitor. Western blot demonstrated that RIP3 up-regulation may be involved in RGC-5 necroptosis. Flow cytometry revealed that the number of OGD-induced necrotic RGC-5 cells was reduced after rip3 knockdown. Furthermore, MDA levels in the normal RGC-5 cells were much higher than in the rip3-knockdown cells after OGD. Our findings suggest that RGC-5 cell necroptosis following OGD is mediated by a RIP3-induced increase in oxidative stress.
         datePublished:2015-08-04T00:00:00Z
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            Receptor-interacting protein 3
            Oxygen glucose deprivation
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      headline:Receptor interacting protein 3-induced RGC-5 cell necroptosis following oxygen glucose deprivation
      description:Necroptosis is a type of regulated form of cell death that has been implicated in the pathogenesis of various diseases. Receptor-interacting protein 3 (RIP3), a member of the RIP family of proteins, has been reported as an important necroptotic pathway mediator in regulating a variety of human diseases, such as myocardial ischemia, inflammatory bowel disease, and ischemic brain injury. Our previous study showed that RIP3 was expressed in rat retinal ganglion cells (RGCs), where it was significantly upregulated during the early stage of acute high intraocular pressure. Furthermore, RIP3 expression was co-localized with propidium iodide (PI)-positive staining (necrotic cells). These results suggested that RIP3 up-regulation might be involved in the necrosis of injured RGCs. In this study, we aimed to reveal the possible involvement of RIP3 in oxygen glucose deprivation (OGD)-induced retinal ganglion cell-5 (RGC-5) necroptosis. RGC-5 cells were cultured in Dulbecco’s-modified essential medium and necroptosis was induced by 8 h OGD. PI staining and flow cytometry were performed to detect RGC-5 necrosis. RIP3 expression was detected by western blot and flow cytometry was used to detect the effect of RIP3 on RGC-5 necroptosis following OGD in rip3 knockdown cells. Malondialdehyde (MDA) lipid peroxidation assay was performed to determine the degree of oxidative stress. PI staining showed that necrosis was present in the early stage of OGD-induced RGC-5 cell death. The presence of RGC-5 necroptosis after OGD was detected by flow cytometry using necrostatin-1, a necroptosis inhibitor. Western blot demonstrated that RIP3 up-regulation may be involved in RGC-5 necroptosis. Flow cytometry revealed that the number of OGD-induced necrotic RGC-5 cells was reduced after rip3 knockdown. Furthermore, MDA levels in the normal RGC-5 cells were much higher than in the rip3-knockdown cells after OGD. Our findings suggest that RGC-5 cell necroptosis following OGD is mediated by a RIP3-induced increase in oxidative stress.
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         Receptor-interacting protein 3
         Oxygen glucose deprivation
         Necroptosis
         Oxidative stress
         Neurosciences
         Neurobiology
         Animal Models
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      name:Department of Anatomy and Neurobiology, Morphological Sciences Building, School of Basic Medical Sciences, Central South University, Changsha, China
      name:Department of Anatomy and Neurobiology, Morphological Sciences Building, School of Basic Medical Sciences, Central South University, Changsha, China
      name:Department of Anatomy and Neurobiology, Morphological Sciences Building, School of Basic Medical Sciences, Central South University, Changsha, China
      name:Department of Biochemistry and Molecular Biology, Health Science Center, Peking University, Beijing, China
      name:Department of Anatomy and Neurobiology, Morphological Sciences Building, School of Basic Medical Sciences, Central South University, Changsha, China

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