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1 Nephrology Research and Training Center, Department of Medicine, Division of Nephrology, University of Alabama at Birmingham, Birmingham, AL, USA
* To whom correspondence should be addressed. E-mail: petjan{at}uab.edu.
Prostaglandin E2 (PGE2), the major cyclooxygenase metabolite of arachidonic acid, is an important paracrine regulator of numerous tubular and vascular functions in the kidney. To date, cyclooxygenase (COX) activity has been considered the key step in prostaglandin synthesis, and is well characterized. However, much less is known about the recently cloned microsomal prostaglandin E2 synthase (mPGES), the terminal enzyme of PGE2 synthesis, which converts COX-derived PGH2 to the biologically important PGE2. Present studies provide the detailed localization of mPGES protein in the rabbit kidney using immunohistochemistry. In the cortex, strong mPGES labeling was found in the macula densa (MD) and principal cells of the connecting segment and cortical collecting tubule but not in intercalated cells. The medulla was abundant in mPGES positive structures, with heavy labeling in the collecting duct system. In descending thin limbs and renal medullary interstitial cells mPGES expression was less intense, and it was below the limits of detection in the vasa recta. Expression of MD mPGES, similarly to COX-2, was greatly increased in response to low salt diet and ACE inhibition by captopril. These findings suggest autocrine regulation of renal salt and water transport by PGE 2 in descending thin limb and collecting tubule, and a paracrine effect of PGE2 on the glomerular and medullary vasculature. Like in other organs, mPGES in the kidney is an inducible enzyme and may be similarly regulated and acts in concert with COX-2.
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