Relaxin induces matrix metalloproteinase-9 through activation of nuclear factor kappa B in human THP-1 cells

Teh Yuan Ho, Carol A. Bagnell

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

Matrix metalloproteinase (MMP) and relaxin are important for tissue remodeling and wound repair. Macrophages populate wound sites and secrete MMPs. Nuclear factor kappa B (NF-κB) is linked to MMP gene regulation. Thus, a monocyte/macrophage cell line, THP-1, was used to study the mechanism of relaxin's action on MMPs. Relaxin increased MMP-9 protein and activity in THP-1 cell-conditioned media, with no significant change in MMP-2 activity. NF-κB DNA binding activity was elevated in response to relaxin, and supershift assay showed activation of both NF-κB subunits p50 and p65. Relaxin also reduced NF-κB inhibitor protein, IκB-α. In conclusion, these data suggest that relaxin-induced MMP-9 expression in THP-1 cells involves NF-κB activation.

Original languageEnglish (US)
Pages (from-to)314-316
Number of pages3
JournalAnnals of the New York Academy of Sciences
Volume1041
DOIs
StatePublished - Jan 1 2005

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • History and Philosophy of Science

Keywords

  • Matrix metalloproteinase-9
  • Nuclear factor-κB
  • Relaxin
  • THP-1 cell line

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