Cyclooxygenase-2 overexpression is related to polypoid growth and K-ras gene mutation in T1 colorectal carcinomas

Dis Colon Rectum. 2004 Nov;47(11):1915-21. doi: 10.1007/s10350-004-0684-y.

Abstract

Purpose: Cyclooxygenase-2 is thought to play a role in the development of intestinal tumors and levels are elevated in approximately 80 to 90 percent of human colorectal carcinomas. To clarify the role that cyclooxygenase-2 plays in the development of colorectal carcinoma, we studied the relationship between cyclooxygenase-2 expression and tumor morphology and that between cyclooxygenase-2 expression and K-ras mutation.

Methods: We classified 48 T1 colorectal carcinomas as polypoid or nonpolypoid and analyzed the clinicopathologic features. The expression of cyclooxygenase-2 was determined immunohistochemically, and nested polymerase chain reaction-restriction fragment length polymorphism detected a K-ras codon 12 mutation.

Results: Cyclooxygenase-2 expression was higher in polypoid carcinomas than in nonpolypoid carcinomas (P < 0.001). The K-ras codon 12 mutation was associated with higher levels of cyclooxygenase-2 expression compared with carcinomas without this mutation (P = 0.028).

Conclusions: Polypoid growth and K-ras gene mutation are both associated with increased levels of cyclooxygenase-2 expression in T1 tumors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenoma / genetics*
  • Adenoma / metabolism*
  • Adenoma / pathology
  • Adenomatous Polyps / genetics*
  • Adenomatous Polyps / metabolism*
  • Adenomatous Polyps / pathology
  • Adult
  • Aged
  • Aged, 80 and over
  • Chi-Square Distribution
  • Codon
  • Colorectal Neoplasms / genetics*
  • Colorectal Neoplasms / metabolism*
  • Colorectal Neoplasms / pathology
  • Cyclooxygenase 2
  • Female
  • Genes, ras / genetics*
  • Humans
  • Immunoenzyme Techniques
  • Isoenzymes / metabolism*
  • Male
  • Membrane Proteins
  • Middle Aged
  • Mutation
  • Polymerase Chain Reaction
  • Polymorphism, Restriction Fragment Length
  • Prostaglandin-Endoperoxide Synthases / metabolism*
  • Statistics, Nonparametric

Substances

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