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J. Biol. Chem., Vol. 279, Issue 3, 1899-1906, January 16, 2004

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Identification and Structural Characterization of the Neuronal Luteinizing Hormone Receptor Associated with Sensory Systems^*

Pirjo M. Apaja, Kirsi T. Harju¶, Jyrki T. Aatsinki||, Ulla E. Petäjä-Repo**, and Hannu J. Rajaniemi

From the Biocenter Oulu and the Departments of Anatomy and Cell Biology, ^¶Pediatrics, and ^||Dentistry, University of Oulu, Oulu FIN-90014, Finland

The luteinizing hormone receptor (LHR) is a G protein-coupled receptor involved in regulation of ovarian and testicular functions. Here we show that the receptor is present also in specific areas of the peripheral and central nervous system and may thus have a broader functional role than has been anticipated. Full-length LHR mRNA and two receptor protein species of M_r 90,000 and 73,000, representing mature and precursor forms, respectively, were expressed in adult and developing rat nervous tissue, starting at fetal day 14.5. The receptor was capable of ligand binding because it was purified by ligand affinity chromatography, and human chorionic gonadotropin and LH were able to displace ¹²⁵I-labeled human chorionic gonadotropin binding to fetal head membranes in a dose-dependent manner. Finally, two 5'-flanking sequences ( 2 and 4 kb) of the rat LHR gene were shown to direct expression of the lacZ reporter to specific areas of the peripheral and central nervous system in fetal and adult transgenic mice, especially to structures associated with sensory, memory, reproductive behavior, and autonomic functions. Importantly, the transgene activity was confined to neurons and colocalized with the cytochrome P450 side chain cleavage enzyme. Taken together, these results indicate that the neuronal LHR is a functional protein, implicating a role in neuronal development and function, possibly by means of regulating synthesis of neurosteroids.

Received for publication, October 16, 2003

^* This work was supported by Biocenter Oulu and the Academy of Finland Grant 202008. 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.

^** Fellow of the Academy of Finland.

These authors contributed equally to this work.

To whom correspondence may be addressed: Dept. of Anatomy and Cell Biology, University of Oulu, P. O. Box 5000, Oulu FIN-90014, Finland. Tel.: 358-8-537-5193 (U. P.-R.) or 358-8-537-5174 (H. R.); Fax: 358-8-537-5172; E-mail: Ulla.Petaja-Repo{at}oulu.fi or Hannu.Rajaniemi{at}oulu.fi.

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