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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

Hsp20 interacts with Bax. Co-IP of Bax with Hsp20. The co-IP was performed with anti-Hsp20 antibodies and an IgG control, followed by Western blot with anti-Bax antibodies. The experiment was repeated independently for at least three times.
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fig4: Hsp20 interacts with Bax. Co-IP of Bax with Hsp20. The co-IP was performed with anti-Hsp20 antibodies and an IgG control, followed by Western blot with anti-Bax antibodies. The experiment was repeated independently for at least three times.

Mentions: In our previous results, Hsp20 was shown to protect against mitochondrial fragmentation, regulate Bcl-2 and Bax expression, and reduce the release of cytochrome c from mitochondria to cytosol upon OGDR insult [12, 13]. To further clarify the cytoprotective mechanism of Hsp20, coimmunoprecipitation (co-IP) assay was used to examine whether Hsp20 may interact with Bax. As shown in Figure 4, we found that anti-Hsp20 antibodies, but not the IgG control, specifically coimmunoprecipitated Bax, suggesting that Bax interacted with Hsp20 in N2a cells, which is in consistency with the results in human hepatocellular carcinoma cells [18].


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)

Hsp20 interacts with Bax. Co-IP of Bax with Hsp20. The co-IP was performed with anti-Hsp20 antibodies and an IgG control, followed by Western blot with anti-Bax antibodies. The experiment was repeated independently for at least three times.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

fig4: Hsp20 interacts with Bax. Co-IP of Bax with Hsp20. The co-IP was performed with anti-Hsp20 antibodies and an IgG control, followed by Western blot with anti-Bax antibodies. The experiment was repeated independently for at least three times.
Mentions: In our previous results, Hsp20 was shown to protect against mitochondrial fragmentation, regulate Bcl-2 and Bax expression, and reduce the release of cytochrome c from mitochondria to cytosol upon OGDR insult [12, 13]. To further clarify the cytoprotective mechanism of Hsp20, coimmunoprecipitation (co-IP) assay was used to examine whether Hsp20 may interact with Bax. As shown in Figure 4, we found that anti-Hsp20 antibodies, but not the IgG control, specifically coimmunoprecipitated Bax, suggesting that Bax interacted with Hsp20 in N2a cells, which is in consistency with the results in human hepatocellular carcinoma cells [18].

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