Transforming growth factor β mediates the progesterone suppression of an epithelial metalloproteinase by adjacent stroma in the human endometrium

Kaylon L. Bruner, William H. Rodgers, Leslie I. Gold, Murray Korc, Joel T. Hargrove, Lynn M. Matrisian, Kevin G. Osteen

Research output: Contribution to journalArticle

203 Scopus citations

Abstract

Unlike most normal adult tissues, cyclic growth and tissue remodeling occur within the uterine endometrium throughout the reproductive years. The matrix metalloproteinases (MMPs), a family of structurally related enzymes that degrade specific components of the extracellular matrix are thought to be the physiologically relevant mediators of extracellular matrix composition and turnover. Our laboratory has identified MMPs of the stromelysin family in the cycling human endometrium, implicating these enzymes in mediating the extensive remodeling that occurs in this tissue. While the stromelysins are expressed in vivo during proliferation-associated remodeling and menstruation-associated endometrial breakdown, none of the stromelysins are expressed during the progesterone-dominated secretary phase of the cycle. Our in vitro studies of isolated cell types have confirmed progesterone suppression of stromal MMPs, but a stromal-derived paracrine factor was found necessary for suppression of the epithelial-specific MMP matrilysin. In this report, we demonstrate that transforming growth factor β (TGF-β) is produced by endometrial stroma in response to progesterone and can suppress expression of epithelial matrilysin independent of progesterone. Additionally, we find that an antibody directed against the mammalian isoforms of TGF-β abolishes progesterone suppression of matrilysin in stromal-epithelial cocultures, implicating TGF-β as the principal mediator of matrilysin suppression in the human endometrium.

Original languageEnglish (US)
Pages (from-to)7362-7366
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number16
DOIs
StatePublished - Aug 1 1995

Keywords

  • cell-cell interactions
  • matrilysin
  • stromelysin

ASJC Scopus subject areas

  • General

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