An aldose reductase with 20 alpha-hydroxysteroid dehydrogenase activity is most likely the enzyme responsible for the production of prostaglandin f2 alpha in the bovine endometrium. Academic Article uri icon

abstract

  • Prostaglandins are important regulators of reproductive function. In particular, prostaglandin F2 alpha (PGF(2 alpha)) is involved in labor and is the functional mediator of luteolysis to initiate a new estrous cycle in many species. These actions have been extensively studied in ruminants, but the enzymes involved are not clearly identified. Our objective was to identify which prostaglandin F synthase is involved and to study its regulation in the endometrium and in endometrial primary cell cultures. The expression of all previously known prostaglandin F synthases (PGFSs), two newly discovered PGFS-like genes, and a 20 alpha-hydroxysteroid dehydrogenase was studied by Northern blot and reverse transcription PCR. These analyses revealed that none of the known PGFS or the PGFS-like genes were significantly expressed in the endometrium. On the other hand, the 20 alpha-hydroxysteroid dehydrogenase gene was strongly expressed in the endometrium at the time of luteolysis. The corresponding recombinant enzyme has a K(m) of 7 microM for PGH(2) and a PGFS activity higher than the lung PGFS. This enzyme has two different activities with the ability to terminate the estrous cycle; it metabolizes progesterone and synthesizes PGF(2 alpha). Taken together, these data point to this newly identified enzyme as the functional endometrial PGFS.

published proceedings

  • J Biol Chem

altmetric score

  • 3

author list (cited authors)

  • Madore, E., Harvey, N., Parent, J., Chapdelaine, P., Arosh, J. A., & Fortier, M. A.

citation count

  • 131

complete list of authors

  • Madore, Eric||Harvey, Nathalie||Parent, Julie||Chapdelaine, Pierre||Arosh, Joe A||Fortier, Michel A

publication date

  • March 2003