Traumatic spinal cord injury (TSCI) is a serious nervous system insult, and apoptosis in secondary injury is an important barrier to recovery from TSCI. Heat shock protein family A member 1A (HSPA1A) is a protective protein whose expression is elevated after stress. However, whether HSPA1A can inhibit apoptosis after spinal cord injury, and the potential mechanism of this inhibition, remain unclear. In this study, we established in vivo and in vitro models of TSCI and induced HSPA1A overexpression and silencing. HSPA1A upregulation promoted the recovery of neurological function and pathological morphology at the injury site, enhanced neurological cell survival, and inhibited apoptosis in rats following TSCI. In the in vitro model, HSPA1A overexpression inhibited H2O2-induced apoptosis, indicating that HSPA1A suppressed the expression of Bax, caspase-9, and cleaved-caspase-3, promoted the expression of Bcl-2. Furthermore, inhibition of HSPA1A expression can aggravate H2O2-induced apoptosis. We also found that HSPA1A overexpression activated the Wnt/β-catenin signaling pathway, and that inhibition of this pathway attenuated the inhibitory effect of HSPA1A overexpression on apoptosis. Together, these results indicate that HSPA1A has neuroprotective effects against TSCI that may be exerted through activation of the Wnt/β-catenin signaling pathway to inhibit apoptosis.
Keywords: Apoptosis; Heat shock protein family A member 1A; Traumatic spinal cord injury; Wnt/β-catenin signaling pathway.
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