scholarly journals No Superoxide Dismutase Activity of Cellular Prion Protein in vivo

2003 ◽  
Vol 384 (9) ◽  
Author(s):  
G. Hutter ◽  
F.L. Heppner ◽  
A. Aguzzi
Keyword(s):  
Superoxide Dismutase ◽  
Prion Protein ◽  
Cellular Prion Protein ◽  
Superoxide Dismutase Activity

Differential Contribution of Superoxide Dismutase Activity by Prion Protein in Vivo

2000 ◽  
Vol 273 (1) ◽  
pp. 136-139 ◽  
Author(s):  
Boon-Seng Wong ◽  
Tao Pan ◽  
Tong Liu ◽  
Ruliang Li ◽  
Pierluigi Gambetti ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Prion Protein ◽  
Superoxide Dismutase Activity ◽  
Differential Contribution

The cellular prion protein binds copper in vivo

Nature ◽  
10.1038/37783 ◽  
1997 ◽  
Vol 390 (6661) ◽  
pp. 684-687 ◽  
Author(s):  
David R. Brown ◽  
Kefeng Qin ◽  
Jochen W. Herms ◽  
Axel Madlung ◽  
Jean Manson ◽  
...  
Keyword(s):  
Prion Protein ◽  
Cellular Prion Protein

scholarly journals In VivoAntioxidant Activity of Deacetylasperulosidic Acid in Noni

2013 ◽  
Vol 2013 ◽  
pp. 1-5 ◽  
Author(s):  
De-Lu Ma ◽  
Mai Chen ◽  
Chen X. Su ◽  
Brett J. West
Keyword(s):  
Antioxidant Activity ◽  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Catalase Activity ◽  
Antioxidant Properties ◽  
Superoxide Dismutase Activity ◽  
Morinda Citrifolia ◽  
Control Group ◽  
Dose Dependent

Deacetylasperulosidic acid (DAA) is a major phytochemical constituent ofMorinda citrifolia(noni) fruit. Noni juice has demonstrated antioxidant activityin vivoand in human trials. To evaluate the role of DAA in this antioxidant activity, Wistar rats were fed 0 (control group), 15, 30, or 60 mg/kg body weight per day for 7 days. Afterwards, serum malondialdehyde concentration and superoxide dismutase and glutathione peroxidase activities were measured and compared among groups. A dose-dependent reduction in malondialdehyde was evident as well as a dose-dependent increase in superoxide dismutase activity. DAA ingestion did not influence serum glutathione peroxidase activity. These results suggest that DAA contributes to the antioxidant activity of noni juice by increasing superoxide dismutase activity. The fact that malondialdehyde concentrations declined with increased DAA dose, despite the lack of glutathione peroxidase-inducing activity, suggests that DAA may also increase catalase activity. It has been previously reported that noni juice increases catalase activityin vivobut additional research is required to confirm the effect of DAA on catalase. Even so, the current findings do explain a possible mechanism of action for the antioxidant properties of noni juice that have been observed in human clinical trials.

Effect of nickel chloride on streptozotocin-induced diabetes in rats

1988 ◽  
Vol 66 (5) ◽  
pp. 663-665 ◽  
Author(s):  
Ethel L. B. Novelli ◽  
Ney L. Rodrigues ◽  
Bartolomé O. Ribas
Keyword(s):  
Superoxide Dismutase ◽  
Body Weight ◽  
Single Dose ◽  
Protective Effect ◽  
Plasma Insulin ◽  
Nickel Chloride ◽  
Superoxide Dismutase Activity ◽  
Streptozotocin Induced Diabetes

The potential of nickel chloride to prevent streptozotocin-induced hyperglycemia was tested in rats in vivo. To induce diabetes, streptozotocin (100 mg/kg body weight) was injected as a single dose. Streptozotocin treatment resulted in a significant decrease in plasma insulin and ceruloplasmin, and pancreatic Cu, protein, and Cu–Zn superoxide dismutase activity. In rats treated with nickel chloride (10 mg/kg body weight) and streptozotocin, these values were comparable with those observed in control rats. The results indicate that nickel chloride injected before streptozotocin prevented streptozotocin-induced hyperglycemia, and suggest that the protective effect was related to Cu–Zn superoxide dismutase activity, mediated by copper.

scholarly journals Neuroprotective role of PrPC against kainate-induced epileptic seizures and cell death depends on the modulation of JNK3 activation by GluR6/7–PSD-95 binding

2011 ◽  
Vol 22 (17) ◽  
pp. 3041-3054 ◽  
Author(s):  
Patricia Carulla ◽  
Ana Bribián ◽  
Alejandra Rangel ◽  
Rosalina Gavín ◽  
Isidro Ferrer ◽  
...  
Keyword(s):  
Prion Protein ◽  
Knockout Mice ◽  
Neuronal Excitability ◽  
Epileptic Seizures ◽  
Cellular Prion Protein ◽  
Transmissible Spongiform Encephalopathies ◽  
Spongiform Encephalopathies ◽  
Glycosyl Phosphatidylinositol

Cellular prion protein (PrPC) is a glycosyl-phosphatidylinositol–anchored glycoprotein. When mutated or misfolded, the pathogenic form (PrPSC) induces transmissible spongiform encephalopathies. In contrast, PrPC has a number of physiological functions in several neural processes. Several lines of evidence implicate PrPC in synaptic transmission and neuroprotection since its absence results in an increase in neuronal excitability and enhanced excitotoxicity in vitro and in vivo. Furthermore, PrPC has been implicated in the inhibition of N-methyl-d-aspartic acid (NMDA)–mediated neurotransmission, and prion protein gene (Prnp) knockout mice show enhanced neuronal death in response to NMDA and kainate (KA). In this study, we demonstrate that neurotoxicity induced by KA in Prnp knockout mice depends on the c-Jun N-terminal kinase 3 (JNK3) pathway since Prnpo/oJnk3o/o mice were not affected by KA. Pharmacological blockage of JNK3 activity impaired PrPC-dependent neurotoxicity. Furthermore, our results indicate that JNK3 activation depends on the interaction of PrPC with postsynaptic density 95 protein (PSD-95) and glutamate receptor 6/7 (GluR6/7). Indeed, GluR6–PSD-95 interaction after KA injections was favored by the absence of PrPC. Finally, neurotoxicity in Prnp knockout mice was reversed by an AMPA/KA inhibitor (6,7-dinitroquinoxaline-2,3-dione) and the GluR6 antagonist NS-102. We conclude that the protection afforded by PrPC against KA is due to its ability to modulate GluR6/7-mediated neurotransmission and hence JNK3 activation.

Chronic UVB irradiation induces superoxide dismutase activity in human epidermis in vivo

1995 ◽  
Vol 30 (1) ◽  
pp. 43-48 ◽  
Author(s):  
Kari Punnonen ◽  
Kirsi Lehtola ◽  
Pekka Autio ◽  
Urpo Kiistala ◽  
Markku Ahotupa
Keyword(s):  
Superoxide Dismutase ◽  
Superoxide Dismutase Activity ◽  
Human Epidermis ◽  
Uvb Irradiation

scholarly journals Toxicological Evaluation of Anti-Scrapie Trimethoxychalcones and Oxadiazoles

2015 ◽  
Vol 87 (2 suppl) ◽  
pp. 1421-1434 ◽  
Author(s):  
CLAUDIA P. FIGUEIREDO ◽  
NATALIA C. FERREIRA ◽  
GISELLE F. PASSOS ◽  
ROBSON DA COSTA ◽  
FERNANDA S. NEVES ◽  
...  
Keyword(s):  
Prion Protein ◽  
Aromatic Compounds ◽  
Prion Diseases ◽  
Intraperitoneal Administration ◽  
Neuroblastoma Cells ◽  
Cellular Prion Protein ◽  
Transmissible Spongiform Encephalopathies ◽  
Toxicological Evaluation ◽  
Spongiform Encephalopathies

An altered form of the cellular prion protein, the PrPScor PrPRes, is implicated in the occurrence of the still untreatable transmissible spongiform encephalopathies. We have previously synthesized and characterized aromatic compounds that inhibit protease-resistant prion protein (PrPRes) accumulation in scrapie-infected cells. These compounds belong to different chemical classes, including acylhydrazones, chalcones and oxadiazoles. Some of the active compounds were non-toxic to neuroblastoma cells in culture and seem to possess drugable properties, since they are in agreement with the Lipinski´s rule of 5 and present desirable pharmacokinetic profiles as predicted in silico. Before the evaluation of the in vivo efficacy of the aromatic compounds in scrapie-infected mice, safety assessment in healthy mice is needed. Here we used Swiss mice to evaluate the acute toxicity profile of the six most promising anti-prionic compounds, the 2,4,5-trimethoxychalcones (J1, J8, J20 and J35) and the 1,3,4-oxadiazoles (Y13 and Y17). One single oral administration (300 mg/kg) of J1, J8, J20, J35, Y13 and Y17 or repeated intraperitoneal administration (10 mg/kg, 3 times a week, for 4 weeks) of J1, J8 and J35, did not elicit toxicity in mice. We strongly believe that the investigated trimethoxychalcones and oxadiazoles are interesting compounds to be further analyzed in vivo against prion diseases.

scholarly journals mGlu5 receptors and cellular prion protein mediate amyloid-β-facilitated synaptic long-term depression in vivo

2014 ◽  
Vol 5 (1) ◽  
Author(s):  
Neng-Wei Hu ◽  
Andrew J. Nicoll ◽  
Dainan Zhang ◽  
Alexandra J. Mably ◽  
Tiernan O’Malley ◽  
...  
Keyword(s):  
Prion Protein ◽  
Amyloid Β ◽  
Cellular Prion Protein ◽  
Long Term Depression ◽  
Mglu5 Receptors
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