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Role of NF‐κB activation in matrix metalloproteinase 9, vascular endothelial growth factor and interleukin 8 expression and secretion in human breast cancer cells
Author(s) -
Li Caijuan,
Guo Sufen,
Shi Tiemei
Publication year - 2013
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.2899
Subject(s) - parthenolide , western blot , vascular endothelial growth factor , microbiology and biotechnology , secretion , cell culture , electrophoretic mobility shift assay , matrix metalloproteinase , interleukin 8 , cancer research , cancer cell , cytokine , chemistry , biology , immunology , cancer , transcription factor , medicine , endocrinology , apoptosis , biochemistry , vegf receptors , gene , genetics
The aims of this study were to assess the effects and potential mechanisms of parthenolide on the expression of vascular endothelial growth factor (VEGF), interleukin 8 (IL‐8) and matrix metalloproteinase 9 (MMP‐9) in human breast cancer cell line MDA‐MB‐231. After incubation with different concentrations of parthenolide for 24 h, MDA‐MB‐231 cells were collected, and the expressions of VEGF, IL‐8 and MMP‐9 were measured by real‐time PCR and Western blot. The secretions of VEGF, IL‐8 and MMP‐9 in culture supernatant of MDA‐MB‐231 cells were then measured with ELISA assays. The NF‐κB DNA‐binding activity of breast cancer cells treated with parthenolide was analyzed using electrophoretic mobility assays. The real‐time PCR and Western blot data showed that the expressions of VEGF, IL‐8 and MMP‐9 were significantly inhibited by parthenolide at both transcription level and protein level in MDA‐MB‐231 cells. ELISA results also confirmed these effects at a secretion level. The electrophoretic mobility assay results demonstrated that parthenolide can inhibit NF‐κB DNA‐binding activity of the breast cancer cells. Hence, the expression of VEGF, IL‐8 and MMP‐9 may be suppressed by parthenolide through the inhibition of NF‐κB DNA‐binding activity in MDA‐MB‐231 cells. Copyright © 2012 John Wiley & Sons, Ltd.

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