Production of the elastase-like enzyme, Suc-(Ala)3-p-nitroanilide hydrolase, was examined in human uterine cervical fibroblasts. The metallo-dependent enzyme is present in both media and cellular fractions. Human recombinant interleukin-1 alpha stimulated cells to produce and secrete this elastase-like enzyme. These results suggest that modulation of this enzyme activity by interleukin-1 may play a significant role in the ripening and dilation of the cervix, because elastin is a component of the uterine cervix and its peptides are known to be chemotactic for leukocytes.