Relaxin induces matrix metalloproteinase-9 through activation of nuclear factor kappa B in human THP-1 cells.
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.
Ho
Teh-Yuan
TY
Department of Animal Sciences, Rutgers University, New Brunswick, NJ 08901, USA.
Bagnell
Carol A
CA
D002460:Cell Line; D004247:DNA / Q000378:metabolism; D004790:Enzyme Induction / Q000187:drug effects; D006801:Humans; D020778:Matrix Metalloproteinase 2 / Q000378:metabolism; D020780:Matrix Metalloproteinase 9 / Q000378:metabolism*; D009000:Monocytes / Q000187:drug effects / Q000378:metabolism; D016328:NF-kappa B / Q000378:metabolism*; D012065:Relaxin / Q000494:pharmacology*
D016328:NF-kappa B; D012065:Relaxin; D004247:DNA; D020778:Matrix Metalloproteinase 2; D020780:Matrix Metalloproteinase 9