碩士 / 國立臺灣海洋大學 / 生物科技研究所 / 100 / Heat shock protein 70 (Hsp70) is rapidly synthesized in living organisms after heat stress. Hsp70 facilitates the refolding of heat denatured peptides to minimize degradation and is therefore called molecular chaperone. Previous studies showed that Hsp70 binds human apurinic / apyrimidinic endonuclease (HAP1) which is an endonuclease in base excision repair (BER) and enhances its activity after heat shock. This study examined whether heat shock regulated the gene activities of DNA mismatch repair(MMR) factors MSH2/MSH6 in zebrafish (Danio rerio) embryos. Semipuantitative RT-PCR and whole-mount in situ hybridization were used to analyze msh2/msh6 expressions in heat-stressed (37℃, 30 min) zebrafish embryos at 12 ~ 36 hour post fertilization (hpf). Whole-mount in situ hybridization indicated that msh6 expression was activated in embryos at 12 and 24 hpf. The expression of msh6 was down-regulated in 36 hpf embryos and this mRNA was found to accumulate in head tissues. Heat shock induced the expression of msh2/msh6 and this induction was detectable after delivering embryos to normal temperature water at 28℃for 1-2 h. Increased levels of MSH6 synthesis and G-T DNA mismatch binding activities in heat-treated embryos were also detected by immunoblot analysis and band shift assay, respectively. The mechanisms of heat shock-induced MSH gene expression await further investigation.
| Identifer | oai:union.ndltd.org:TW/100NTOU5613037 |
| Date | January 2012 |
| Creators | Shin-Wei Chen, 陳新濰 |
| Contributors | Todd Hsu, Shiow-Yi Chen, 許濤, 陳秀儀 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 51 |
Page generated in 0.0158 seconds