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J Biol Chem, Vol. 275, Issue 20, 15314-15320, May 19, 2000

Colocalization of Prostacyclin Synthase with Prostaglandin H Synthase-1 (PGHS-1) but Not Phorbol Ester-induced PGHS-2 in Cultured Endothelial Cells*

Jun-Yang LiouDagger , Song-Kun ShyueDagger , May-Jywan TsaiDagger , Chia-Lin ChungDagger , Kuan-Yu ChuDagger , and Kenneth K. WuDagger §

From the Dagger  Institute of Biomedical Sciences, Academia Sinica, 128 Academic Rd. Sec. 2, Taipei 115, Taiwan and § Vascular Biology Research Center, University of Texas-Houston Medical School, Houston, Texas 77030

The subcellular colocalization of prostacyclin synthase (PGIS) with prostaglandin H synthase (PGHS) has not been delineated. To test the hypothesis that its colocalization with PGHS is crucial for prostacyclin synthesis, we determined subcellular locations of PGIS, PGHS-1, and PGHS-2 in bovine aortic endothelial cells by immunofluorescent confocal microscopy. PGIS and PGHS-1 were colocalized to nuclear envelope (NE) and endoplasmic reticulum (ER) in resting and adenovirus-infected bovine aortic endothelial cells. PGIS and PGHS-2 were also colocalized to ER in serum-treated or adenovirus-cyclooxygenase-2-infected cells. By contrast, PGIS was not colocalized with PGHS-2 in cells induced with phorbol 12-myristate 13-acetate where PGHS-2 was visualized primarily in vesicle-like structures. The lack of colocalization was accompanied by failed prostacyclin production. Resting ECV304 cells did not produce prostacyclin and had no detectable PGHS-1 and PGIS proteins. Confocal analysis showed abnormal colocalization of PGIS and PGHS-1 to a filamentous structure. Interestingly, the abundant PGIS and PGHS-1 expressed in adenovirus-infected ECV304 cells were colocalized to NE and ER, which synthesized a large quantity of prostacyclin. These findings underscore the importance of colocalization of PGHS and PGIS to ER and NE in prostacyclin synthesis.

* This work is supported by Department of Health, Taipei, Taiwan Grant DOH89-TD-1132 and National Institutes of Health Grants P50 NS23327 and RO1 HL50675.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Vascular Biology Research Center, University of Texas-Houston Medical School, 6431 Fannin, MSB 5.016, Houston, TX 77030. Tel.: 713-500-6801; Fax: 713-500-6812; E-mail: kkwu@heart.med.uth.tmc.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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