Hsp20 Protects against Oxygen-Glucose DeprivationReperfusion-Induced Golgi Fragmentation and Apoptosis through FasFasL Pathway

Abstract EN

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.