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Title: Relaxin induces matrix metalloproteinase-9 through activation of nuclear factor kappa B in human THP-1 cells. Author: Ho TY, Bagnell CA. Journal: Ann N Y Acad Sci; 2005 May; 1041():314-6. PubMed ID: 15956726. 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-kappaB) 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-kappaB DNA binding activity was elevated in response to relaxin, and supershift assay showed activation of both NF-kappaB subunits p50 and p65. Relaxin also reduced NF-kappaB inhibitor protein, IkappaB-alpha. In conclusion, these data suggest that relaxin-induced MMP-9 expression in THP-1 cells involves NF-kappaB activation.[Abstract] [Full Text] [Related] [New Search]