Relationship between cyclooxygenase-2 expression and K-ras gene mutation in colorectal adenomas

J Gastroenterol Hepatol. 2000 Nov;15(11):1277-81.

Abstract

Background and aims: Cyclooxygenase (COX)-2 has a trophic effect on gastrointestinal epithelial cells and is associated with the progression of colorectal adenomas. Mutation of the K-ras gene is also associated with the progression of colorectal adenomas and has recently been suggested to play an important role in the induction of COX-2. In the present study, we investigated the relationship between COX-2 expression and K-ras mutation in colorectal adenomas.

Methods: Twenty-nine colorectal adenomas were obtained from specimens resected by the use of surgery or endoscopic mucosal resection and analyzed clinicopathologically. Immunohistochemistry was performed to analyze COX-2 expression in the adenoma specimens. The K-ras codon 12 mutations were detected by using the polymerase chain reaction-restriction fragment length polymorphism method.

Results: An increase of COX-2-positive cells in adenoma was observed in 11 (37.9%) lesions, 10 (90.9%) of which had a K-ras gene mutation, suggesting a significant correlation between COX-2 expression and K-ras gene mutation in colorectal adenomas. Morphologically, COX-2-positive adenomas (13.8 +/- 2.6 mm) were significantly larger than COX-2-negative ones (5.8 +/- 0.9 mm). In addition, the increase of COX-2-positive cells in the lesion was observed more frequently in tubulovillous (63.6%) than in tubular (36.4%) adenoma.

Conclusions: Cycloxygenase-2 expression in colorectal adenoma cells is strongly correlated with K-ras gene mutation, suggesting that COX-2 and mutated K-ras are connectively associated with the progression of colorectal adenoma.

MeSH terms

  • Adenoma / genetics*
  • Adenoma / metabolism*
  • Adenoma / pathology
  • Colorectal Neoplasms / genetics*
  • Colorectal Neoplasms / metabolism*
  • Colorectal Neoplasms / pathology
  • Cyclooxygenase 2
  • Genes, ras*
  • Humans
  • Immunohistochemistry
  • Isoenzymes / metabolism*
  • Membrane Proteins
  • Mutation
  • Polymerase Chain Reaction
  • Polymorphism, Restriction Fragment Length
  • Prostaglandin-Endoperoxide Synthases / metabolism*

Substances

  • Isoenzymes
  • Membrane Proteins
  • Cyclooxygenase 2
  • PTGS2 protein, human
  • Prostaglandin-Endoperoxide Synthases