Prostaglandin endoperoxide synthase: Why two isoforms?

Christopher S. Williams, Raymond N. DuBois

Research output: Contribution to journalReview articlepeer-review

514 Scopus citations


Prostaglandin endoperoxide synthase-1 [prostaglandin G/H synthase-1 (PGHS- 1)] and PGHS-2 are key enzymes in the conversion of arachidonic acid to prostaglandins and other eicosanoids. We refer to these isoforms as cyclooxygenase-1 (COX-1) and COX-2 in this review. This brief review focuses on recent developments in the study of these enzymes. Alterations in the expression levels of COX-2 result in distinct phenotypic changes in intestinal epithelial cells. Overexpression of COX-2 in intestinal epithelial cells results in increased adhesion to extracellular matrix proteins and inhibition of apoptosis. Disruption of the COX-2 gene in mice results in renal dysplasia, cardiac fibrosis, and defects in the ovary. Interestingly, disruption of the COX-1 gene results in distinct phenotypic changes different from those observed for COX-2. COX-1 null mice survive well, have no gastric pathology, and show less indomethacin-induced gastric ulceration than wild- type mice. These two closely related enzymes must have distinct functions in the organism, since lack of their expression causes distinct phenotypic changes for each respective isoform.

Original languageEnglish (US)
Pages (from-to)G393-G400
JournalAmerican Journal of Physiology - Gastrointestinal and Liver Physiology
Issue number3 33-3
StatePublished - 1996
Externally publishedYes


  • colorectal cancer
  • cyclooxygenase
  • eicosanoid
  • intestinal epithelial cells

ASJC Scopus subject areas

  • Physiology
  • Hepatology
  • Gastroenterology
  • Physiology (medical)


Dive into the research topics of 'Prostaglandin endoperoxide synthase: Why two isoforms?'. Together they form a unique fingerprint.

Cite this