The Role of HSPA12B in Regulating Neuronal Apoptosis |
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Authors: | Lihua Kang Guowei Zhang Yaohua Yan Kaifu Ke Xinmin Wu Yilu Gao Jing Li Lin Zhu Qiyun Wu Zhengming Zhou |
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Affiliation: | 1. The Jiangsu Key Laboratory of Neuroregeneration, Nantong University, Nantong, 226001, Jiangsu, People’s Republic of China 2. Department of Ophthalmology, Affiliated Hospital of Nantong University, Nantong, 226001, People’s Republic of China 4. Department of Osteology, Affiliated Jiangyin Hospital, Nantong University, Wuxi, 214400, People’s Republic of China 3. Department of Neurosurgery, Affiliated Hospital of Nantong University, Nantong, 226001, People’s Republic of China
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Abstract: | Heat shock protein A12B (HSPA12B) is the newest member of a recently defined subfamily of proteins distantly related to the 70-kDa family of heat shock proteins (HSP70) family. HSP70s play a crucial role in protecting cells, tissues, organs and animals from various noxious conditions. Here we studied the dynamic expression changes and localization of HSPA12B after middle cerebral artery occlusion (MCAO) with reperfusion induced ischemic insult processes in adult rats. Apoptosis, as indicated by terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) staining, was also increased in the peri-ischemic cortex compared to non-ischemic hemisphere. The expression of HSPA12B was strongly induced in the ischemic hemisphere of MCAO reperfusion rats in vivo. In vitro studies indicated that the up-regulation of HSPA12B may be involved in oxygen-glucose deprivation-induced PC12 cell death. And knockdown of HSPA12B in cultured differentiated PC12 cells by siRNA showed that HSPA12B inhibited the expression of active caspase-3. Collectively, these results suggested that HSPA12B may be required for protecting neurons from ischemic insults. |
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