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  • Author or Editor: H. Satake x
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Gonadotropin-releasing hormone (GnRH) is a ten-amino acid peptide hormone that plays pivotal roles in reproduction in vertebrates and octopus. Recently, six GnRH forms (t-GnRH-3-8) and four GnRH receptor subtypes (Ci-GnRHR-1-4) were identified in the protochordate, Ciona intestinalis . In this study, we show the functional modulation of Ci-GnRHR-1 via heterodimerization with the orphan receptor subtype, Ci-GnRHR-4. The dimerization between Ci-GnRHR-1 and R-4 was detected by co-immunoprecipitation and immunoblot analysis. Binding assays confirmed the binding of t-GnRHs to Ci-GnRHR-1 but not to R-4, and verified no alternation in ligand-binding affinity between Ci-GnRHR-1 homodimer and Ci-GnRHR1&4 heterodimer. The heterodimer was found to stimulate the elevation of intracellular calcium, time-extension of ERK phosphorylation, and up-regulation of cell proliferation, all in a ligand specific manner, compared with the Ci-GnRHR-1 homodimer. In combination, these results indicated that Ci-GnRHR-4 is not an inactive receptor, but a modulatory factor for Ci-GnRHR-1 in C. intestinalis .

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Ci-TK and Ci-TK-R are authentic tachykinin (TK) and TK receptor isolated from a protochordate, Ciona intestinalis . In this study, we investigated a novel function of TK as an enhancer of oocyte growth. Ci-TK-R is expressed specifically in the Ciona vitellogenic oocytes. Moreover, administration of Ci-TK to the Ciona ovary resulted in upregulation of gene expression and enzymatic activity of several proteases. Moreover, maturation of the Ciona oocytes from the vitellogenic stage to the post-vitellogenic stage was induced in the presence of Ci-TK, which was completely blocked by addition of protease inhibitors.

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