Preterm premature rupture of membranes (pPROMs) account for one-third of preterm births, a leading cause of neonatal death. Understanding the mechanism of membrane rupture is thus of clinical significance in the prevention of preterm birth. Parturition at both term and preterm is associated with increased abundance of proinflammatory cytokines in the fetal membranes regardless of the presence of infection, which is believed to induce rupture of membranes through activation of the matrix metalloproteinases. It remains unknown whether there are any alternative mechanisms underpinning proinflammatory cytokine-induced rupture of membranes. Here we showed that there were reciprocal increases in interleukin-1β (IL-1β) and decreases in lysyl oxidase (LOX), a collagen crosslinking enzyme, in the human amnion tissue following spontaneous rupture of membrane at term and pPROM. Studies using human amnion tissue explants revealed that IL-1β inhibited the expression of LOX, which can be reproduced in cultured human amnion fibroblasts. Mechanistic study revealed that IL-1β inhibited LOX expression through activation of p38 and Erk1/2 mitogen-activated protein kinase pathways, which resulted in the phosphorylation of the nuclear factor kappa light-chain enhancer of activated B (NF-κB) cell subunit p65 as well as GATA binding protein 3 (GATA3). Subsequently, activated NF-κB interacted with GATA3 at the NF-κB binding site of LOX promoter to inhibit its expression. Conclusively, this study has revealed an alternative mechanism that IL-1β may contribute to the rupture of membranes by attenuating collagen crosslinking through downregulation of LOX expression in amnion fibroblasts.