Glutathione S-transferase (GST) is an essential detoxification enzyme in eukaryotic cells, by catalysing the conjugation of electrophilic substrates to glutathione (GSH) and detoxification both in external and internal cellular enviornments. Previous studies of our team suggested that SjGST had profound on the growth of human breast cancer cells in vitro. In order to analyse the effect of SjGST on the proliferation and migration of human breast cancer cell line, MDA-MB 435s , we initially constructed plasmid containing gst fragment in pAcGFP-N1 and transfected into MDA-MB 435s cells. Assays for proliferation and migration of the transfected cells showed that no difference between transfected and non-transfected cells was found. Analysis of the transfected gene found a frameshift mutation occurred in the plasmid, and thus no expression was detedted. Thus, we carried out assays for proliferation and migration of the cancer cells using recombiation SjGST instead. Results from assays for proliferation and migration showed that SjGST enhance both proliferation and migration of MDA-MB 435s. Furthermore, the recombinant protein was a strong inhibitor to cell death, probably by detoxification pathway. But the mechanism of action of detoxification of shikonin by the recombinant protein, however remains unknow.
Identifer | oai:union.ndltd.org:NSYSU/oai:NSYSU:etd-1224108-182550 |
Date | 24 December 2008 |
Creators | Laio, Tsai-tsen |
Contributors | Chen-fu Shaw, Shiping He, Huang, Hung-Tu |
Publisher | NSYSU |
Source Sets | NSYSU Electronic Thesis and Dissertation Archive |
Language | Cholon |
Detected Language | English |
Type | text |
Format | application/pdf |
Source | http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-1224108-182550 |
Rights | withheld, Copyright information available at source archive |
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