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1 Division of Nephrology, Departments of Medicine, 4 Molecular Physiology and Biophysics, and 3 Pharmacology, Vanderbilt University Medical Center, Nashville, Tennessee 37212; and 2 Merck Frosst Centre for Therapeutic Research, Kirkland, Quebec, Canada H9H 3L1
First published August 15, 2001;
10.1152/ajprenal.00116.2001.
PGE2 plays a critical role in
regulating renal function and facilitating reproduction. One of the
rate-limiting biosynthetic enzymes in PGE2 synthesis is the
terminal PGE2 synthase (PGES). In the present studies, we
report the functional expression of a membrane-associated murine PGES
(mPGES) and its expression in urogenital tissues. Two independent cDNA
clones sharing an identical open reading frame of 459 bp and encoding a
peptide of 153 amino acids, but differing in the 3'-untranslated
region, were identified. Assays for enzymatic activity, using
microsomes prepared from cells transfected with mPGES cDNA, showed that
these cDNA sequences encode a functional protein that catalyzes the
conversion of PGH2 to PGE2. Constitutive
expression of mPGES was highest in the mouse kidney, ovary, and urinary
bladder but was also expressed at lower levels in uterus and testis.
Renal mPGES expression was predominantly localized to epithelia of
distal tubules and medullary collecting ducts. High expression was also
seen in transitional epithelial cells of bladder and ureter and in the
primary and secondary follicles in the ovary. In conclusion, mPGES is
constitutively expressed along the urogenital tract, where it may have
important roles in normal physiology and disease.
prostaglandin E2; membrane-associated prostaglandin E synthase; gene expression; urogenital tissue
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