Human recombinant interleukin‐1α‐mediated stimulation of procollagenase production and suppression of biosynthesis of tissue inhibitor of metalloproteinases in rabbit uterine cervical fibroblasts

Abstract
Influence of human recombinant interleukin‐1 (hrIL‐1) on collagen metabolism was investigated with rabbit uterine cervical fibroblasts. Enzyme‐linked immunosorbent assays for collagenase and tissue inhibitor of metalloproteinases (TIMP) indicated that hrIL‐1 participates in both stimulation of procollagenase production and suppression of TIMP synthesis by uterine cervical cells. IL‐1 did not modulate collagen synthesis. In addition, the sensitivity to IL‐1 of uterine cervix from ovariectomized rabbits was augmented by estradiol‐17β treatment. Thus it is proposed that IL‐1 accelerates collagenolysis in the cervical tissue and its effect on uterine cervix is hormonally regulated.

This publication has 24 references indexed in Scilit: