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J. Biol. Chem., Vol. 278, Issue 31, 29153-29163, August 1, 2003

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Functional Endothelin Receptors Are Present on Nuclei in Cardiac Ventricular Myocytes^*

Benoit Boivin   ¶, Dominique Chevalier , Louis R. Villeneuve , Éric Rousseau || ** and Bruce G. Allen   

From the Institut de Cardiologie de Montréal, Centre de Recherche, 5000 rue Bélanger, Montréal, Québec H1T 1C8, Canada, the Département de Médecine et Biochimie and the Groupe de Recherche sur le Système Nerveux Autonome, Université de Montréal, Montréal, Quebec H3C 3J7, Canada, and the ^||Département de Physiologie et Biophysique, Faculté de Médecine, Université de Sherbrooke, Sherbrooke, Quebec J1H 5N4, Canada

Endothelins are thought to act through two specific, plasmalemmal G protein-coupled receptor subtypes, ET_AR and ET_BR. However, in subfractionated cardiac membranes, ET_AR immunoreactivity was detected only in the plasma membrane whereas ET_BR immunoreactivity was detected predominantly in membranes of intracellular origin. Confocal microscopy demonstrated the presence of intracellular ET_AR and ET_BR in ventricular myocytes. ET_AR were primarily on plasma membrane (surface membranes and transverse-tubules) and to a lesser extent on the nucleus while ET_BR localized primarily to the nuclei. Western blot analysis of nuclei isolated from the heart indicated the presence of endothelin receptors: both ET_AR and ET_BR copurified with nucleoporin 62, whereas markers of endoplasmic reticulum and Golgi membranes were depleted. Radioligand binding studies revealed that isolated nuclei contain specific [¹²⁵I]ET-1 binding sites. Specific [¹²⁵I]ET-1 binding was reduced by 70–80% using the ET_AR-selective antagonist BQ610 and 20–30% using the ET_BR-specific antagonist BQ788. IRL-1620, an ET_BR-specific agonist, also reduced [¹²⁵I]ET-1 binding. Furthermore, ET-1 and IRL-1620 altered the incorporation of ³²P into nuclear proteins and caused a transient increase in nuclear Ca²⁺ concentration. Hence, cardiac nuclei possess both ET_AR and ET_BR subtypes, which are functional with respect to ligand binding and are coupled to signaling mechanisms within the nuclear membrane.

Received for publication, February 19, 2003 , and in revised form, May 5, 2003.

^* This work was supported in part by Canadian Institutes of Health Research Grant MT-14725 and the Fonds de la Recherche de l'Institut de Cardiologie de Montréal. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Recipient of bursaries from the Fonds de la Recherche de l'Institut de Cardiologie de Montréal and Fonds de la Recherche en Santé du Québec (FRSQ).

^** National Scholar of the FRSQ.

Currently a Research Scholar of the Heart and Stroke Foundation of Canada. To whom correspondence should be addressed: Institut de Cardiologie de Montréal, Centre de Recherche, 5000, rue Bélanger, Montréal, Québec H1T 1C8, Canada. Tel.: 514-376-3330 (ext. 3591); Fax: 514-376-1355; E-mail: allen{at}icm.umontreal.ca.

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