Abstract:
:Matrix metalloproteinase-9 (MMP-9) is implicated in the invasion and metastasis of breast cancer cells. We investigated the modulatory effects of nitric oxide (NO) on the 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced MMP-9 expression in MCF-7 cells. Different chemical NO donors inhibited the extracellular content of TPA-induced MMP-9 protein and MMP-9 activity as assessed by gelatin-zymography and ELISA, respectively. Concomitant with the reduction in the extracellular MMP-9 content NO strongly decreased the steady-state levels of MMP-9 mRNA which in turn leads to a lower recruitment of MMP-9 transcripts to polysomes and to a diminished MMP-9 translation. Reporter gene assays revealed that the inhibition in MMP-9 expression by NO is mainly attributed to a 0.67 kb fragment of the 5'-promoter region of the MMP-9 gene but independent of the 3'untranslated region thus indicating that MMP-9 suppression by NO mainly results from transcriptional events. Electrophoretic mobility shift assays (EMSA), showed that NO specifically interferes with the TPA-induced DNA binding affinity of c-Jun and c-Fos without affecting the TPA-induced increase in the levels of the transcription factors. Using pharmacological inhibitors and small interfering (si)RNA we found that PKCdelta is indispensably involved in the TPA-triggered MMP-9 expression. Concomitantly, the TPA-evoked increase in total PKC activity was strongly attenuated in the lysates from NO-treated MCF-7 cells, thus suggesting that NO attenuates TPA-triggered MMP-9 mainly through a direct inhibition of PKCdelta. Modulation of MMP-9 by NO highlights the complex roles of NO in the regulation of MMP-9 in breast cancer cells.
journal_name
J Cell Physioljournal_title
Journal of cellular physiologyauthors
Jespersen C,Doller A,Akool el-S,Bachmann M,Müller R,Gutwein P,Mühl H,Pfeilschifter J,Eberhardt Wdoi
10.1002/jcp.21658subject
Has Abstractpub_date
2009-05-01 00:00:00pages
276-87issue
2eissn
0021-9541issn
1097-4652journal_volume
219pub_type
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