Recombinant human lactoferrin inhibits matrix metalloproteinase (MMP-2, MMP-3, and MMP-9) activity in a rabbit preterm delivery model

J Obstet Gynaecol Res. 2008 Dec;34(6):931-4. doi: 10.1111/j.1447-0756.2008.00827.x.

Abstract

Aim: To investigate the effect of recombinant human lactoferrin (rh-LF) on the expression of matrix metalloproteinase as a marker of cervical maturation, using a rabbit preterm delivery model in which preterm labor was induced by bacteria.

Methods: We used cervical tissues that had been excised in a previous study in which rabbits were randomly assigned to receive either inoculation with Escherichia coli (E. coli) or saline solution and to receive pretreatment with or without rh-LF inserted into the cervix two hours before bacterial inoculation (Condition A: saline + saline; Condition B: rh-LF + E. coli; Condition C: saline +E. coli). E. coli, saline solution, and rh-LF were inserted into the cervix using a hysteroscope and a sterile polyethylene cannula. Both cervices of the rabbit uterus, which is bicorpus-bicolli, were taken out and preserved, and expression of matrix metalloproteinases MMP-2,-3, and -9 in the cervix was evaluated using Western blot.

Results: MMP-2,-3, and -9 levels in the cervix under Conditions A and B were significantly lower than that under Condition C.

Conclusions: These results suggest that the prevention of preterm delivery by rh-LF in a rabbit model has been achieved through inhibition of cervical maturation promoted by matrix metalloproteinase activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Cervix Uteri / enzymology*
  • Female
  • Lactoferrin / pharmacology*
  • Matrix Metalloproteinase Inhibitors*
  • Matrix Metalloproteinases / metabolism
  • Obstetric Labor, Premature / enzymology*
  • Pregnancy
  • Rabbits
  • Random Allocation
  • Recombinant Proteins / pharmacology

Substances

  • Matrix Metalloproteinase Inhibitors
  • Recombinant Proteins
  • Lactoferrin
  • Matrix Metalloproteinases