Low molecular weight protein tyrosine phosphatase (LMW-PTP) is highly conserved across almost all living organisms and is involved in the modulation of a number of cellular proteins related to important signaling pathways. In this study, we isolated lmwptp (Y94H6A.7) of Caenorhabditis elegans, the homolog of human ACP1, and set up an effective feeding-based RNA interference (RNAi) knockdown against this gene. We found that knockdown of lmwptp decreased damage associated with heat shock, oxidative stress and UV irradiation in wild-type worms, however, its deficiency didn't further reduce the stress resistance of daf-16 or hsf-1 mutants and didn't further increase the stress sensitivity associated with age-1, akt-1 or akt-2 mutants, but it enhanced the stress resistance of daf-2 mutants. Further studies demonstrated that this stress tolerance could be attributed to increased daf-16 nuclear accumulation and enhanced expression of both superoxide dismutase-3 protein (SOD-3) and heat shock protein-16.2 (HSP-16.2) in response to stress. Additionally, quantitative real-time PCR results showed that the expression of hsf-1 and its target genes were up-regulated in lmwptp-knockdown worms under stress conditions. Together these results indicated that lmwptp is related to stress resistance of worms, and it is likely associated with the insulin/IGF-1-like signaling (IIS) pathway.
Keywords: Caenorhabditis elegans; Stress resistance; lmwptp.
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