Characterization of insulin-like peptides (ILPs) in the sea urchin Strongylocentrotus purpuratus: insights on the evolution of the insulin family.

The evolutionary history of the insulin-like peptides (ILPs), members of the insulin family, is still a matter of debate. Although ILPs structure and expression have been described in different metazoans, little is known about these molecules in non-chordate deuterostomes, such as the echinoderms. In order to fill this gap in the current literature, we have characterized two members of the insulin family found in the sea urchin Strongylocentrotus purpuratus genome (SpIgf1 and SpIgf2 that, after our analysis, we suggest to rename SpILP1 and SpILP2, respectively) together with their putative receptor (SpInsr). We found that SpILP1 gene structure is more similar to the cephalochordate amphioxus ILP, while the SpILP2 gene shows a completely different organization. In addition, we have revealed that SpILP1 and SpILP2 transcripts are expressed in different compartments during embryo/larva development and that the SpILP1 protein mature form differs in the egg and the larva, suggesting different biological roles. Finally, we have analyzed SpILP1 transcript and protein expression in response to different feeding regimes through real-time quantitative PCR, Western blot and immunohistochemistry methodologies, and found that its expression and localization are feeding-dependent. We discuss our findings in a comparative evolutionary perspective including data available in other animal models and provide new insights into the evolution of the insulin family molecules. In the model we put forward, the last common ancestor of all deuterostomes presented an ILP composed of the B-C-A-D-E domains, and successive lineage specific independent gene duplication events resulted in the presence of several ILPs in vertebrates and in echinoderms.