Baicalin attenuates oxygen–glucose deprivation-induced injury via inhibiting NMDA receptor-mediated 5-lipoxygenase activation in rat cortical neurons

2007 ◽  
Vol 55 (2) ◽  
pp. 148-157 ◽  
Author(s):  
Q GE ◽  
X HU ◽  
Z MA ◽  
J LIU ◽  
W ZHANG ◽  
...  
Keyword(s):  
Nmda Receptor ◽  
Cortical Neurons ◽  
Glucose Deprivation ◽  
Oxygen Glucose Deprivation ◽  
Rat Cortical Neurons

Activation of 5-lipoxygenase after oxygen-glucose deprivation is partly mediated via NMDA receptor in rat cortical neurons

2006 ◽  
Vol 97 (4) ◽  
pp. 992-1004 ◽  
Author(s):  
Qiu-Fu Ge ◽  
Er-Qing Wei ◽  
Wei-Ping Zhang ◽  
Xin Hu ◽  
Xiao-Jia Huang ◽  
...  
Keyword(s):  
Nmda Receptor ◽  
Cortical Neurons ◽  
Glucose Deprivation ◽  
Oxygen Glucose Deprivation ◽  
Rat Cortical Neurons

scholarly journals Proteolysis of Oxidized Proteins after Oxygen–Glucose Deprivation in Rat Cortical Neurons is Mediated by the Proteasome

2001 ◽  
Vol 21 (9) ◽  
pp. 1090-1096 ◽  
Author(s):  
Markus Weih ◽  
Marion Schmitt ◽  
Janette Gieche ◽  
Christoph Harms ◽  
Karsten Ruscher ◽  
...  
Keyword(s):  
Cerebral Ischemia ◽  
Cortical Neurons ◽  
Oxidative Injury ◽  
Glucose Deprivation ◽  
Cellular Damage ◽  
Protein Carbonyls ◽  
Oxygen Glucose Deprivation ◽  
Radical Scavenger ◽  
Oxidized Proteins ◽  
Rat Cortical Neurons

Oxidative injury contributes to cellular damage during and after cerebral ischemia. However, the downstream catabolic pathways of damaged cellular components in neurons are largely unknown. In the current study, the authors examined the formation of oxidized proteins and their active degradation by the proteasome. In near-pure rat primary cortical neurons, it was found that protein-bound carbonyls as markers for oxidized proteins are increased after oxygen-glucose deprivation (OGD). During and after OGD, degradation of proteins metabolically radiolabeled before OGD increases two-to threefold compared with the normal protein turnover. Proteolysis after reoxygenation was attenuated by the presence of dimethylthiourea, a radical scavenger, and was blocked by lactacystin, a specific proteasome inhibitor. Lactacystin also increased the amount of protein carbonyls formed. In contrast, the activity of the proteasome complex itself after OGD was not different from sham-washed controls. The authors suggest that oxygen-glucose deprivation increases free radicals, which, in turn, oxidize proteins that are recognized and actively degraded by the proteasome complex. This protease itself is relatively resistant against oxidative injury. The authors conclude that the proteasome may be an active part of the cellular defense system against oxidative stress after cerebral ischemia.

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