scholarly journals SUMO2/3 Conjugation is an Endogenous Neuroprotective Mechanism

2011 ◽  
Vol 31 (11) ◽  
pp. 2152-2159 ◽  
Author(s):  
Anna Lena Datwyler ◽  
Gisela Lättig-Tünnemann ◽  
Wei Yang ◽  
Wulf Paschen ◽  
Sabrina Lin Lin Lee ◽  
...  
Keyword(s):  
Stress Response ◽  
Cerebral Ischemia ◽  
Cortical Neurons ◽  
Neuronal Loss ◽  
Glucose Deprivation ◽  
Transient Cerebral Ischemia ◽  
Oxygen Glucose Deprivation ◽  
Primary Cortical Neurons ◽  
Microrna Delivery

Small ubiquitin-like modifier (SUMO)2/3 but not SUMO1 conjugation is activated after transient cerebral ischemia. To investigate its function, we blocked neuronal SUMO2/3 translation through lentiviral microRNA delivery in primary cortical neurons. Viability was unaffected by SUMO2/3 silencing unless neurons were stressed by transient oxygen–glucose deprivation (OGD). Both 15 and 45 minutes of OGD were tolerated by control microRNA-expressing neurons but damaged >60% of neurons expressing SUMO2/3 microRNA. Damaging OGD (75 minutes) increased neuronal loss to 54% (control microRNA) and to 99% (SUMO2/3 microRNA). This suggests that activation of SUMO2/3 conjugation is an endogenous neuroprotective stress response.

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.

The p38/CYLD Pathway is Involved in Necroptosis Induced by Oxygen-glucose Deprivation Combined with ZVAD in Primary Cortical Neurons

2017 ◽  
Vol 42 (8) ◽  
pp. 2294-2304 ◽  
Author(s):  
Tao Feng ◽  
WeiWei Chen ◽  
CaiYi Zhang ◽  
Jie Xiang ◽  
HongMei Ding ◽  
...  
Keyword(s):  
Cortical Neurons ◽  
Glucose Deprivation ◽  
Oxygen Glucose Deprivation ◽  
Primary Cortical Neurons
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