Abstract

Allatotropins (ATs) are pleiotropic neuropeptides initially isolated from the tobacco hornworm, Manduca sexta. In 2008, the first receptor for AT-like peptides (ATR) was characterized in Bombyx mori. Since then, ATRs have also been characterized in M. sexta, Tribolium castaneum, Aedes aegypti and Bombus terrestris. These receptors show sequence similarity to vertebrate orexin (ORX) receptors. When generating an EST-database of the desert locust (Schistocerca gregaria) central nervous system, we found cDNA sequences encoding the Schgr-AT precursor and a fragment of its putative receptor. This receptor cDNA has now been completed and functionally expressed in mammalian cell lines. Activation of this receptor, designated as Schgr-ATR, by Schgr-AT caused an increase in intracellular calcium ions, as well as cyclic AMP (cAMP), with an EC50 value in the nanomolar range. In addition, the transcript distribution of both the Schgr-AT precursor and Schgr-ATR was investigated by means of quantitative real-time PCR. Moreover, we found more evidence for the myotropic and allatostimulatory actions of Schgr-AT in the desert locust. These data are discussed and situated in a broader context by comparison with literature data on AT and ATR in insects.

Highlights

  • Allatotropin (AT) was originally identified as an amidated tridecapeptide isolated from the nervous system of the lepidopteran Manduca sexta

  • Cloning and Sequence Analysis As described in the S. gregaria EST paper (Badisco et al, 2011b), a partial fragment of an orexin 2 receptor-like/ AT receptors (ATRs)-like receptor and the Schistocerca gregaria (Schgr)-AT precursor are represented in the EST database

  • We further completed the sequence of the SchgrATR by rapid amplification of cDNA ends (RACE)

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Summary

Introduction

Allatotropin (AT) was originally identified as an amidated tridecapeptide isolated from the nervous system of the lepidopteran Manduca sexta. It was named after its first known biological function, namely the ability to stimulate juvenile hormone (JH) biosynthesis in the corpora allata (CA) in vitro (Kataoka et al, 1989). Related peptides have been reported in other phyla beyond Arthropoda. These were isolated in mollusks (Harada et al, 1993; Li et al, 1993; Veenstra, 2010), flatworms (Adami et al, 2011) and annelids (Ukena et al, 1995; Veenstra, 2011), and recent phylogenetic analysis showed the presence of this peptidergic system in other protostomes, but not in nematodes, and in some deuterostomes (Mirabeau and Joly, 2013)

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