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Recombinant human lactoferrin inhibits matrix metalloproteinase (MMP‐2, MMP‐3, and MMP‐9) activity in a rabbit preterm delivery model
Author(s) -
Nakayama Ken,
Otsuki Katsufumi,
Yakuwa Kyoko,
Hasegawa Akitoshi,
Sawada Maki,
Mitsukawa Kaori,
Chiba Hiroshi,
Nagatsuka Masaaki,
Okai Takashi
Publication year - 2008
Publication title -
journal of obstetrics and gynaecology research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.597
H-Index - 50
eISSN - 1447-0756
pISSN - 1341-8076
DOI - 10.1111/j.1447-0756.2008.00827.x
Subject(s) - cervix , saline , matrix metalloproteinase , medicine , lactoferrin , andrology , escherichia coli , western blot , recombinant dna , uterus , gynecology , chemistry , biochemistry , cancer , gene
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.