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15-Hydroxyprostaglandin Dehydrogenase Protein Expression in Human Fetal Membranes With and Without Subclinical Inflammation

Departments of Obstetrics and Gynecology and Physiology, University of Toronto and Mount Sinai Hospital, Toronto, Ontario, Canada, Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington

Carole S. Watson, PhD

Departments of Obstetrics and Gynecology and Physiology, University of Toronto and Mount Sinai Hospital, Toronto, Ontario, Canada, Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington

Sarah Keating, MD, MSc

Departments of Obstetrics and Gynecology and Physiology, University of Toronto and Mount Sinai Hospital, Toronto, Ontario, Canada, Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington

Hsin-Hsiung Tai, PhD

Departments of Obstetrics and Gynecology and Physiology, University of Toronto and Mount Sinai Hospital, Toronto, Ontario, Canada, Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington

John R. G. Challis, PhD

Departments of Obstetrics and Gynecology and Physiology, University of Toronto and Mount Sinai Hospital, Toronto, Ontario, Canada, Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington

Alan D. Bocking, MD

Departments of Obstetrics and Gynecology and Physiology, University of Toronto and Mount Sinai Hospital, Toronto, Ontario, Canada, abocking{at}mtsinai.on.ca, Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington

Prostaglandins play a central role in the stimulation and maintenance of both term and preterm labor. 15-Hydroxyprostaglandin dehydrogenase (PGDH), localized primarily to chorion trophoblasts, is the key enzyme responsible for the metabolism of prostaglandins. In preterm chorion, levels of PGDH protein and activity were lower when compared to term and were further reduced with the presence of infection, but effects of subclinical inflammation and membrane rupture on PGDH expression are not known. Our objectives were (1) to determine the relative expression of PGDH in amnion and chorion and (2) to determine the effect of preterm premature rupture of membranes (PPROM) and (3) subclinical inflammation on PGDH protein expression in preterm fetal membranes. Fetal membranes were collected from women with idiopathic preterm labor. Patients were divided into preterm birth (1) <32 weeks with PPROM (n = 6), (2) <32 weeks with intact membranes (n = 11), (3) 32 and <37 weeks with PPROM (n = 10), and (4) 32 and <37 weeks with intact membranes (n = 10). Different antibodies were used to detect protein expression and localization of PGDH in amnion and chorion from these patients using both Western blotting and immunohistochemistry. Antibody T (AbT) localized PGDH to chorion trophoblasts, whereas antibody C (AbC) detected immunoreactive (ir) PGDH predominantly in the amnion mesenchyme. By Western blot, AbT showed a stronger 29-kDa ir-PGDH band whereas with AbC, a stronger 55-kDa ir-PGDH signal was detected. 55-kDa ir-PGDH was significantly higher in PPROM amnion, specifically in the <32 weeks group (P < .05) and with PPROM >24 hours (P < .05). No change was detected in the 29-kDa ir-PGDH in either amnion or chorion with gestational age or the presence and absence of PPROM. In addition, neither form of ir-PGDH was altered significantly with or without subclinical inflammation. ir-PGDH is detectable in both chorion trophoblasts and amnion, especially in the mesenchyme; however, the predominant form of the enzyme differs in the 2 tissues. PPROM and subclinical inflammation do not appear to affect the levels of 29-kDa ir-PGDH protein in the fetal membranes. The differential expression of 55-kDa ir-PGDH in preterm amnion with and without PPROM supports the need for a better understanding of the different forms of PGDH.

Key Words: Prostaglandin dehydrogenase • fetal membranes • preterm birth • preterm premature rupture of membranes • inflammation.

Reproductive Sciences, Vol. 14, No. 3, 260-269 (2007)
DOI: 10.1177/1933719107302433


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