The effects of glutathionylation of p65 in NF-kB activity
| Autor: | Huang Kuan-Dar, 黃冠達 |
|---|---|
| Rok vydání: | 2010 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 98 The recent research found that NF-kB, a transcription factor, can transcribe about 150 categories of proteins which regulate many cellular physiological responses, such as cellular inflammation, growth and apoptosis. Therefore, NF-kB is an important transcription factor. Previous studies indicated glutathionylation of protein can inhibit protein activities. Recently, our study found cinnamaldehyde can increase GSH in ECs, which inhibits TNF-a-induced NF-kB activity in ECs. Therefore, this research will investigate GSSG and H2O2/GSH in TNF-a-induced ECs and discuss protein glutathionylation on NF-kB-p65. We found GSSG、H2O2/GSH and NAC can increase total glutathionylated protein and NF-kB-p65 glutathionylation. Moreover, GSSG and H2O2/GSH inhibit TNF-a-induced ICAM-1 expression in transcriptional level by decrease NF-kB-p65 translocation. In addition, GSSG and H2O2/GSH inhibit NF-kB-p65 translocation independent with IkB-a degradation. Taken together, these data suggest GSSG and H2O2/GSH decrease NF-kB-p65 translocation by increasing NF-kB-p65 glutathionylation. Therefore, We also transfected with GFP-p65 wild-type and GFP-p65 mutation c38s、c120s、c160s、c216s and then treat with GSSG to analyze NF-kB promoter activity. The result show NF-kB-p65 cystein 38、160、216 mutation will change GSSG inhibits TNF-a-induced NF-kB-p65 activation. To summarize, this research verifies that glutathionylation of NF-B-p65 in cystein 38、160、216 will affect the NF-kB-p65 protein activity. |
| Databáze: | Networked Digital Library of Theses & Dissertations |
| Externí odkaz: |
|