Abstract
Abstract Heat shock proteins (HSPs) are chaperones responsible for protein refolding, facilitated proteolysis of damaged proteins, and prevention of abnormal protein aggregation. The overexpressions of some heat shock proteins have been shown to increase lifespan, enhance stress resistance, prevent apoptosis and neurodegenerative diseases. Here, we overexpressed hsp27 in neuronal tissue of Drosophila and detected both lifespan extension and oxidative stress resistance. The overexpression of hsp27 in the neuronal tissue also rescued the paraquat-induced parkinsonism like disorder. Though unable to reduce the polyglutamine (127Q)-induced toxicity, it attenuated the 41Q toxicity which is a stage toward to a longer polyglutamine-induced toxicity. In addition, the overexpression of hsp27 rescued hid-induced but not reaper-induced lethality, suggesting that hsp27 is involved in the intervention of a specific apoptotic pathway. In order to identify which sub-regions responsible for lifespan and stress resistance, different GAL4 drivers were used to overexpress hsp27. It revealed that whole brain driver increase lifespan and stress resistance; antennae and optic lobes enhance lifespan but not stress resistance. In summary, it indicates that the overexpression of hsp27 in neuronal tissue possesses several important biological functions, which increases lifespan, enhances oxidative stress resistance, prevents neurodegenerative disorders like paraquat-induced parkinsonism and poly-glutamine induced toxicity, and prevents hid-induced apoptosis.