التفاصيل البيبلوغرافية
| العنوان: |
Anti-proliferative effects of recombinant iron superoxide dismutase on HepG2 cells via a redox-dependent PI3k/Akt pathway. |
| المؤلفون: |
Min Lu, Chong-shan Bi, Xing-guo Gong, Han-min Chen, Xie-huang Sheng, Tong-le Deng, Ke-di Xu |
| المصدر: |
Applied Microbiology & Biotechnology; Aug2007, Vol. 76 Issue 1, p193-201, 9p, 2 Black and White Photographs, 3 Graphs |
| مصطلحات موضوعية: |
SUPEROXIDE dismutase, GENOMES, ESCHERICHIA coli, MANGANESE enzymes, GENETICS, ENTEROBACTERIACEAE |
| مستخلص: |
The coding sequence for an iron superoxide dismutase ( fe-sod) was amplified from the Nostoc commune genome. Recombinant Fe-SOD was overexpressed in Escherichia coli, accounting for ∼76% of total bacterial protein. Fe-SOD was purified from bacterial lysate by Ni-NTA column chromatography and used to generate an anti-SOD antibody. The purified Fe-SOD was encapsulated in liposomes and delivered to HepG2 liver tumor cells to eliminate cellular superoxide anions. The SOD-loaded cells exhibited lower reactive oxygen species (ROS) levels and higher reduced glutathione (GSH) levels. In Fe-SOD-treated cells, the cell cycle was delayed in the G1 phase, and HepG2 cell growth slowed in association with dephosphorylation of the serine–threonine kinase Akt. Low-dose H2O2 stimulated Akt phosphorylation, implying that Akt activation in HepG2 cells is redox-sensitive. Akt phosphorylation was abrogated by phosphatidylinositol 3-kinase (PI3K) inhibitors, suggesting that PI3K is an upstream mediator of Akt activation in HepG2 cells. This study provides insight into recombinant Fe-SOD-induced signaling mechanisms in liver tumor cells and suggests the feasibility of using Fe-SOD as an antitumor agent. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
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