Hormonal control of mRNA expression of immunoglobulin binding factor in uterine cervix

Biochem Biophys Res Commun. 2000 Dec 29;279(3):898-903. doi: 10.1006/bbrc.2000.4036.


Uterine cervical mucus contains an immunoglobulin binding factor (IgBF). It may play a role in preventing antibody production against sperm in the female reproductive tract. To elucidate the mechanism involved in the production of activated IgBF, we determined the effects of hormones on the expression of mRNAs of IgBF and of protein disulfide isomerase (PDI), activating enzyme, in uterine cervix by quantitative RT-PCR. The uterine cervices of female rats were excised at preovulatory, ovulatory, and postovulatory phases. The human uterine cervical adenocarcinoma cells (TCO-2) were cultured for 24 h in serum-free medium containing 17beta-estradiol or progesterone. Expression of IgBF and PDI mRNAs was significantly highest during the ovulatory phase. 17beta-estradiol stimulated the expression of both mRNAs in TCO-2; whereas progesterone was ineffective. In conclusion, estrogen regulates the production of IgBF by the endocervix and PDI in vivo, thereby increasing the level of activated IgBF in the female reproductive tract during the ovulatory phase, allowing sperm to enter the uterine cavity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cervix Uteri / physiology*
  • Estradiol / blood
  • Estradiol / physiology*
  • Female
  • Gene Expression Regulation*
  • Humans
  • In Situ Hybridization
  • Lymphokines / biosynthesis
  • Lymphokines / genetics*
  • Progesterone / blood
  • Progesterone / physiology*
  • Prostatic Secretory Proteins*
  • Protein Disulfide-Isomerases / biosynthesis
  • Protein Disulfide-Isomerases / genetics
  • RNA, Messenger / biosynthesis
  • Rats
  • Reverse Transcriptase Polymerase Chain Reaction
  • Tumor Cells, Cultured


  • Lymphokines
  • Prostatic Secretory Proteins
  • RNA, Messenger
  • beta-microseminoprotein
  • immunoglobulin-binding factors
  • Progesterone
  • Estradiol
  • Protein Disulfide-Isomerases