Elafin, an antiprotease, is likely to protect pulmonary epithelial cells from inflammatory damages. We aimed to explore the molecule mechanisms of recombinant human elafin on protecting A549 cells integrity against inflammatory assault. We transfected A549 airway epithelial cells with eukaryotic expression vector pEGFP-N1-Elafin and negative control vector pEGFP-N1, respectively. Cells were co-incubated with polymorphonuclear neutrophils (PMN) and then were stimulated with lipopolysaccharide (LPS). Results revealed that, in pEGFP-N1-Elafin transfected cells, neutrophil elastase (NE) activity significantly decreased after LPS stimulation, accompanied with elevated elafin mRNA level and protein production, whereas in cells transfected with pEGFP-N1, NE activity was higher and elafin expression was lower, compared with pEGFP-N1-Elafin transfected group (P < 0.05). In pEGFP-N1 transfected cells, LPS suppressed tight junctions protein zonula occludens-1 (ZO-1) production, while in recombinant pEGFP-N1-Elafin cells, LPS did not cause significantly decrease of ZO-1, compared with normal control cells. LPS stimulation also significantly weakened the collagen adhesion capability of pEGFP-N1 transfected cells (P < 0.01), but there was no significant difference in recombinant pEGFP-N1-Elafin cells (P > 0.05). These results suggest that elafin can maintain airway epithelium integrity by protecting airway epithelial cells and enhancing the anti-inflammatory capability of airway.