Primary structure of an adipokinetic neuropeptide from the rhinoceros beetle, Oryctes rhinoceros L (Coleoptera: Dynastidae)

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Abstract

Background

Neuropeptides play an important role in cellular communication in vertebrates. This is also true for insects in which many physiological, developmental and behavioral processes are affected by neuropeptides produced in neurosecretory cells of the retrocerebral complex. Small neuropeptides of the adipokinetic hormone/red pigment concentrating hormone family (AKH/RPCH) are one of the important groups of peptides that regulate physiological homeostasis.

Purpose

The present investigation was carried out to elucidate the primary structure of adipokinetic neuropeptides in the rhinoceros beetle, O. rhinoceros.

Methods and Results

In the present investigation, an adipokinetic neuropeptide from the coconut pest, Oryctes rhinoceros was isolated from corpora cardiaca by HPLC; the chromatographic fractions were tested for adipokinetic activity in the plant bug, Iphita limbata in vivo. Two UV absorbance peaks were found to be significantly active in elevating haemolymph lipid levels. MALDI-MS analysis of the extract indicated that the molecular mass, 1003.70 Da is similar to the already known AKH from another beetle, Melolontha melolontha. MALDI-MS/MS analysis confirmed that its primary structure is exactly similar to the structure reported for the Melme-AKH (pE-L-N-Y-S-P-D-W-NH ₂).

Coclusion

The findings suggest that the distribution of AKH peptides has shown that there exists a taxonomic order or family specificity. This data can be used as additional information to aid in the construction of phylogenetic trees by means of computer programme and protein parsimony algorithms.

Related collections

Most cited references 22

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Regulation of intermediary metabolism and water balance of insects by neuropeptides.

Gerd Gäde (2003)

Neuropeptides regulate all important physiological, developmental, and behavioral processes in insects. Here, I review two major physiological events that are hormonally controlled, namely intermediary metabolism and ion and water transport. Peptides belonging to the family of adipokinetic hormones (AKHs) increase hemolymph carbohydrates, lipids, and proline by activating the enzyme glycogen phosphorylase or lipase in the fat body. Moreover, these pleiotropic and multifunctional peptides inhibit protein-, lipid-, and RNA synthesis, and stimulate the frequency of contraction of certain muscles. Diuretic hormones that are related to the vertebrate corticotropin-releasing factor (CRF-related DHs) or belong to the family of kinins (which also have a myotropic action) or the cardioacceleratory peptides (CAPs), which increase the frequency of the heartbeat, all stimulate the secretion of fluid in Malpighian tubules (MTs) in vitro. Only a few true antidiuretic hormones are known: those from mealworms that inhibit the fluid transport in MTs in vitro, probably neuroparsins that stimulate water absorption by everted rectal sacs in vitro, and the desert locust's ion-transport peptide (ITP). Biosynthesis, release, receptors, mode of action, inactivation, structure-activity studies, and biological functions are discussed for the various peptides.