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Endocrinology Vol. 143, No. 9 3207-3210
Copyright © 2002 by The Endocrine Society

ARTICLE

Minireview: A Novel Pathway of Prostacyclin Signaling—Hanging Out with Nuclear Receptors

Hyunjung Lim and Sudhansu K. Dey

Departments of Obstetrics and Gynecology and Cell Biology and Physiology (H.L.), Washington University School of Medicine, St. Louis, Missouri 63110; and Department of Molecular and Integrative Physiology (S.K.D), Ralph L. Smith Research Center, University of Kansas Medical Center, Kansas City, Kansas 66160

Address all correspondence and requests for reprints to: H. Lim, Department of Obstetrics and Gynecology, Washington University School of Medicine, St. Louis, Missouri 63110. E-mail: limj{at}msnotes.wustl.edu; or S. K. Dey, Department of Molecular and Integrative Physiology, Ralph L. Smith Research Center, University of Kansas Medical Center, Kansas City, Kansas 66160. E-mail: sdey{at}kumc.edu.

Prostacylin (PGI2), one of the major prostaglandins, is derived from arachidonic acid by the action of the cyclooxygenase (COX) system coupled to PGI2 synthase (PGIS). The presence of the COX-2/PGIS at the nuclear and endoplasmic reticular membrane suggests differential signaling pathways of PGI2 actions involving both cell surface and nuclear receptors. Although the signaling of PGI2 via its cell surface receptor, prostacyclin receptor (IP), is well documented in vascular biology, its action via nuclear receptors in other physiological responses is gradually being more appreciated. Peroxisomal proliferator-activated receptors (PPARs), PPAR{alpha}, PPAR{gamma}, and PPAR{delta}, though initially cloned as a family of orphan receptors, are now known for their ligand promiscuity. The ligands range from free fatty acids and their derivatives produced by the cyclooxygenase or lipoxygenase pathway to certain hypolipidemic drugs. The predisposition of PPARs to use a wide spectrum of ligands is well explained by their unusually large ligand-binding pocket. The promiscuous ligand usage by PPARs is also reflected by their involvement in various pathophysiological events. Several recent independent reports show that endogenously produced PGI2 indeed activates PPAR{delta} in vivo, indicating that a novel signaling mechanism for this abundant eicosanoid is operative in certain systems. This review attempts to cover recent developments in nuclear actions of PGI2 in diverse biological functions.




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