Molecular characterization and seasonal changes in gonadal expression of a thyrotropin receptor in the European sea bass

The thyroid stimulating hormone (TSH) is a glycoprotein synthesized and secreted from thyrotrophs of the anterior pituitary gland. It acts by binding to and activating its specific receptor, the TSHR, to induce the synthesis and secretion of thyroid hormones. Recent studies conducted in diverse fish species suggest a direct role of TSH on gonadal physiology. In this work, we describe the cloning of a cDNA encoding a TSHR which was isolated from the gonads of the European sea bass (Dicentrarchus labrax). The mature protein displays typical features of the members of the glycoprotein hormone receptor family and shows the highest amino acid sequence identity with the TSHRs of other fish species. An insertion of approximately 50 amino acids, specific for the TSHR subfamily is also present in the carboxyl end of the extracellular domain of the sbsTSHR. By RT-PCR analysis, we demonstrate the extrathyroidal expression of sbsTSHR in numerous tissues of the sea bass. Also, two transcripts that differ in the length of their 3′ untranslated regions were found. They reflect the use of alternative polyadenylation cleavage sites. Seasonal changes in sbsTSHR mRNA levels in female and male sea bass during the first ovarian and testicular recrudescence suggest that in females the TSHR could participate in active vitellogenesis and in the regulation of gamete maturation and ovulation, whereas in males, the TSHR would be involved in the regulation of processes that occur during the early stages of the gonadal development and also of gamete maturation and spermiation. The results of this work indicate that a sbsTSHR has been cloned from the testis of the European sea bass and they provide the basis for future studies concerning the function of TSHR in this species.