Adult human colonic subepithelial myofibroblasts express extracellular matrix proteins and cyclooxygenase-1 and -2

Am J Physiol. 1997 Dec;273(6):G1341-8. doi: 10.1152/ajpgi.1997.273.6.G1341.

Abstract

Interactions between epithelial cells and subepithelial myofibroblasts are increasingly recognized as important in the regulation of epithelial cell function. We have established primary cultures of subepithelial myofibroblasts from adult human colonic mucosal samples denuded of epithelial cells and maintained in culture. During culture of mucosal tissue, subepithelial myofibroblasts migrated out via basement membrane pores before establishment in culture. Despite prolonged culture and passage, the myofibroblasts maintained their phenotype, as demonstrated by expression of alpha-smooth muscle actin and vimentin. The cells expressed transcripts and protein for cyclooxygenase (COX)-1 and -2 enzymes, and their release of prostaglandin E2 (PGE2) was inhibited by selective COX-1 and -2 inhibitors. The myofibroblasts also expressed the extracellular matrix (ECM) proteins collagen type IV, laminin-beta 1 and -gamma 1, and fibronectin. Adult human colonic subepithelial myofibroblasts may influence epithelial cell function via products of COX-1 and -2 enzymes, such as PGE2 and secreted ECM proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actins / biosynthesis
  • Adult
  • Cell Culture Techniques / methods
  • Cells, Cultured
  • Colon / cytology
  • Colon / metabolism*
  • Colon / ultrastructure
  • Cyclooxygenase 1
  • Cyclooxygenase 2
  • Extracellular Matrix Proteins / metabolism*
  • Humans
  • Intestinal Mucosa / cytology
  • Intestinal Mucosa / metabolism*
  • Intestinal Mucosa / ultrastructure
  • Isoenzymes / analysis
  • Isoenzymes / biosynthesis*
  • Membrane Proteins
  • Microscopy, Electron
  • Muscle, Smooth / cytology
  • Muscle, Smooth / metabolism*
  • Muscle, Smooth / ultrastructure
  • Organelles / ultrastructure
  • Prostaglandin-Endoperoxide Synthases / analysis
  • Prostaglandin-Endoperoxide Synthases / biosynthesis*
  • Vimentin / biosynthesis

Substances

  • Actins
  • Extracellular Matrix Proteins
  • Isoenzymes
  • Membrane Proteins
  • Vimentin
  • Cyclooxygenase 1
  • Cyclooxygenase 2
  • PTGS1 protein, human
  • PTGS2 protein, human
  • Prostaglandin-Endoperoxide Synthases