Limits...
Hsp20 Protects against Oxygen-Glucose Deprivation/Reperfusion-Induced Golgi Fragmentation and Apoptosis through Fas/FasL Pathway.

Zhong B, Hu Z, Tan J, Lu T, Lei Q, Chen C, Zeng L - Oxid Med Cell Longev (2015)

Bottom Line: Finding effective neuroprotective agents has become a priority in the treatment of ischemic stroke.However, transfection with Hsp20 significantly attenuates OGDR-induced Golgi fragmentation and apoptosis.Hsp20 interacts with Bax, decreases FasL and Bax expression, and inhibits caspases 3 and p115 cleavage in N2a cells exposed to OGDR.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurology, Second Xiangya Hospital, Central South University, Changsha, Hunan 410011, China ; Department of Traditional Chinese Medicine, Second Xiangya Hospital, Central South University, Changsha, Hunan 410011, China.

ABSTRACT
Cerebral ischemia-reperfusion injury plays an important role in the development of tissue injury after acute ischemic stroke. Finding effective neuroprotective agents has become a priority in the treatment of ischemic stroke. The Golgi apparatus (GA) is a pivotal organelle and its protection is an attractive target in the treatment of cerebral ischemia-reperfusion injury. Protective effects of Hsp20, a potential cytoprotective agent due to its chaperone-like activity and involvement in regulation of many vital processes, on GA were assessed in an ischemia-reperfusion injury model. Mouse neuroblastoma Neuro2a (N2a) cells were subjected to oxygen-glucose deprivation/reperfusion (OGDR) insult. OGDR induces Golgi fragmentation, apoptosis, and p115 cleavage in N2a cells. However, transfection with Hsp20 significantly attenuates OGDR-induced Golgi fragmentation and apoptosis. Hsp20 interacts with Bax, decreases FasL and Bax expression, and inhibits caspases 3 and p115 cleavage in N2a cells exposed to OGDR. Our data demonstrate that increased Hsp20 expression protects against OGDR-induced Golgi fragmentation and apoptosis, likely through interaction with Bax and subsequent amelioration of the OGDR-induced elevation in p115 cleavage via the Fas/FasL signaling pathway. This neuroprotective potential of Hsp20 against OGDR insult and the underlying mechanism will pave the way for its potential clinical application for cerebral ischemia-reperfusion related disorders.

No MeSH data available.


Related in: MedlinePlus

The potential neuroprotective mechanism of Hsp20 upon OGDR insult.
© Copyright Policy - open-access
Related In: Results  -  Collection


getmorefigures.php?uid=PMC4495232&req=5

fig6: The potential neuroprotective mechanism of Hsp20 upon OGDR insult.

Mentions: In conclusion, our study demonstrates that OGDR disrupts GA and induces apoptosis and p115 cleavage in mouse N2a neuroblastoma cells. Hsp20 protects against OGDR-induced Golgi fragmentation and apoptosis, indicating its cytoprotective role in cerebral ischemia-reperfusion injury. The neuroprotective mechanism may be related to interacting with Bax and subsequently ameliorating the OGDR-induced elevation in cleavage of p115, which is mediated by Fas/FasL signaling pathway (Figure 6). Our results showed the beneficial effects of Hsp20 against OGDR, which would pave the way for its potential clinical application. Further efforts may lead to the development of novel therapies for disorders whose etiology is based upon cerebral ischemia-reperfusion injury by using of Hsp20.


Hsp20 Protects against Oxygen-Glucose Deprivation/Reperfusion-Induced Golgi Fragmentation and Apoptosis through Fas/FasL Pathway.

Zhong B, Hu Z, Tan J, Lu T, Lei Q, Chen C, Zeng L - Oxid Med Cell Longev (2015)

The potential neuroprotective mechanism of Hsp20 upon OGDR insult.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4495232&req=5

fig6: The potential neuroprotective mechanism of Hsp20 upon OGDR insult.
Mentions: In conclusion, our study demonstrates that OGDR disrupts GA and induces apoptosis and p115 cleavage in mouse N2a neuroblastoma cells. Hsp20 protects against OGDR-induced Golgi fragmentation and apoptosis, indicating its cytoprotective role in cerebral ischemia-reperfusion injury. The neuroprotective mechanism may be related to interacting with Bax and subsequently ameliorating the OGDR-induced elevation in cleavage of p115, which is mediated by Fas/FasL signaling pathway (Figure 6). Our results showed the beneficial effects of Hsp20 against OGDR, which would pave the way for its potential clinical application. Further efforts may lead to the development of novel therapies for disorders whose etiology is based upon cerebral ischemia-reperfusion injury by using of Hsp20.

Bottom Line: Finding effective neuroprotective agents has become a priority in the treatment of ischemic stroke.However, transfection with Hsp20 significantly attenuates OGDR-induced Golgi fragmentation and apoptosis.Hsp20 interacts with Bax, decreases FasL and Bax expression, and inhibits caspases 3 and p115 cleavage in N2a cells exposed to OGDR.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurology, Second Xiangya Hospital, Central South University, Changsha, Hunan 410011, China ; Department of Traditional Chinese Medicine, Second Xiangya Hospital, Central South University, Changsha, Hunan 410011, China.

ABSTRACT
Cerebral ischemia-reperfusion injury plays an important role in the development of tissue injury after acute ischemic stroke. Finding effective neuroprotective agents has become a priority in the treatment of ischemic stroke. The Golgi apparatus (GA) is a pivotal organelle and its protection is an attractive target in the treatment of cerebral ischemia-reperfusion injury. Protective effects of Hsp20, a potential cytoprotective agent due to its chaperone-like activity and involvement in regulation of many vital processes, on GA were assessed in an ischemia-reperfusion injury model. Mouse neuroblastoma Neuro2a (N2a) cells were subjected to oxygen-glucose deprivation/reperfusion (OGDR) insult. OGDR induces Golgi fragmentation, apoptosis, and p115 cleavage in N2a cells. However, transfection with Hsp20 significantly attenuates OGDR-induced Golgi fragmentation and apoptosis. Hsp20 interacts with Bax, decreases FasL and Bax expression, and inhibits caspases 3 and p115 cleavage in N2a cells exposed to OGDR. Our data demonstrate that increased Hsp20 expression protects against OGDR-induced Golgi fragmentation and apoptosis, likely through interaction with Bax and subsequent amelioration of the OGDR-induced elevation in p115 cleavage via the Fas/FasL signaling pathway. This neuroprotective potential of Hsp20 against OGDR insult and the underlying mechanism will pave the way for its potential clinical application for cerebral ischemia-reperfusion related disorders.

No MeSH data available.


Related in: MedlinePlus