Families of allatoregulator sequences: a 2011 perspective1This review is part of a virtual symposium on recent advances in understanding a variety of complex regulatory processes in insect physiology and endocrinology, including development, metabolism, cold hardiness, food intake and digestion, and diuresis, through the use of omics technologies in the postgenomic era.

2012 ◽  
Vol 90 (4) ◽  
pp. 521-544 ◽  
Author(s):  
William G. Bendena ◽  
Stephen S. Tobe

Three different peptide families have been named “allatostatins” (ASTs), based on their initial purifications which were based on their ability to inhibit juvenile hormone (JH) biosynthesis. These include (i) a family of peptides that have a consensus C-terminal sequence Y/FXFGL-NH2; (ii) a family of peptides with a conserved C-terminal sequence W(X)6W-NH2; and(iii) a family of peptides with C-terminal sequence PISCF, some of which are C-terminally-amidated. Each allatostatin family has functions distinct and apart from the inhibition of JH biosynthesis. A peptide family known as the “allatotropins” serve to stimulate JH biosynthesis. This family of peptides also has been proven to exert multiple effects dependent on the species in question. Genome and peptidome projects are uncovering new members of these families and it is clear that these structures are not just confined to Insecta but are found in a range of invertebrates. The receptors for these neuropeptides have been identified and tested experimentally for specific ligand binding. The Y/FXFGLa-ASTs exert their action through galanin-like receptors, W(X)6Wa-ASTs through a sex peptide-binding receptor, and PISCF-ASTs through somatostatin-like receptors. These receptors are conserved through evolutionary time and are being identified in numerous invertebrates by way of genome projects.

2012 ◽  
Vol 90 (4) ◽  
pp. 435-439 ◽  
Author(s):  
I. Orchard ◽  
A.B. Lange

This series of the Canadian Journal of Zoology brings together scientists actively working on insect physiology and endocrinology in this postgenomic era. This issue is timely and appropriate. Timely, because of the pace of change brought about by genome projects, functional genomics and genetics (omics technologies), including gene microarrays, mutations, RNAi, and sophisticated mass spectrometry techniques, which are helping to unravel complex regulatory processes. Appropriate, because Canada, and the Canadian Journal of Zoology, has a rich history and strong tradition of cutting-edge research in insect biology—with particular strengths in insect physiology and endocrinology. The first review illustrates how these very modern omics technologies can be embraced and applied to insect physiology and endocrinology, and the subsequent reviews illustrate this in practice, with regard to insect cold hardiness, insulin signaling and stress, peptidergic control of food intake and digestion, endocrine control of diuresis, and finally allatoregulatory peptides. These reviews set the scene and context for the exciting era that we find ourselves in, and the depth of understanding that has come from this postgenomic revolution.


2012 ◽  
Vol 90 (4) ◽  
pp. 440-455 ◽  
Author(s):  
Bart Boerjan ◽  
Dries Cardoen ◽  
Rik Verdonck ◽  
Jelle Caers ◽  
Liliane Schoofs

As more and more insect genomes are fully sequenced and annotated, omics technologies, including transcriptomic, proteomic, peptidomics, and metobolomic profiling, as well as bioinformatics, can be used to exploit this huge amount of sequence information for the study of different biological aspects of insect model organisms. Omics experiments are an elegant way to deliver candidate genes, the function of which can be further explored by genetic tools for functional inactivation or overexpression of the genes of interest. Such tools include mainly RNA interference and are currently being developed in diverse insect species. In this manuscript, we have reviewed how omics technologies were integrated and applied in insect biology.


2008 ◽  
Vol 198 (2) ◽  
pp. 429-437 ◽  
Author(s):  
Christopher J Charles ◽  
Takeshi Katafuchi ◽  
Timothy G Yandle ◽  
Naoto Minamino

We have recently reported the isolation of three new members of the calcitonin (CT) gene-related peptide family of peptides, the CT receptor (CT-R)-stimulating peptides (CRSPs). We now report the sequencing and characterization of ovine/caprine CRSP-1 and caprine CRSP-2. Mature ovine and caprine CRSP-1 are identical and have strong structural homology to CRSP-1s identified to date from other species. As with other CRSP-1s, ovine/caprine CRSP-1 binds to and activates the CT-R but not the CT-like receptor (CL-R) in combination with the receptor activity-modifying proteins (RAMPs). By contrast, caprine CRSP-2 does not activate any of these receptor-RAMP complexes. Intravenous infusions of ovine CRSP-1 to normal conscious sheep induced dose-dependent reduction in plasma total Ca levels (P=0.02) and corrected Ca levels (P=0.017) associated with increases in plasma cAMP (P=0.002). CRSP-1 reduced both plasma amino-terminal pro-C-type natriuretic peptide levels (P=0.006) and plasma renin activity (P=0.028). There were no significant effects observed on hemodynamic or renal indices measured. In conclusion, we have sequenced ovine/caprine CRSP-1 and caprine CRSP-2 precursors. This newly identified CRSP-1 has been shown to share the structural and biological features of CRSP-1s known to date. In vivo studies confirm that ovine CRSP-1 reduces plasma Ca levels in sheep, presumably via a cAMP-mediated mechanism. By contrast, caprine CRSP-2 did not stimulate any combination of CT-R, CL-R, and RAMPs. Accession numbers of cDNA determined in this study are caprine CRSP-1, AB364646; caprine CRSP-2, AB364647; and ovine CRSP-1, AB364648.


2012 ◽  
Vol 90 (4) ◽  
pp. 489-506 ◽  
Author(s):  
J. Spit ◽  
L. Badisco ◽  
H. Verlinden ◽  
P. Van Wielendaele ◽  
S. Zels ◽  
...  

Like all heterotrophic organisms, insects require a strict control of food intake and efficient digestion of food into nutrients to maintain homeostasis and to fulfill physiological tasks. Feeding and digestion are steered by both external and internal signals that are transduced by a multitude of regulatory factors, delivered either by neurons innervating the gut or mouthparts, or by midgut endocrine cells. The present review gives an overview of peptide regulators known to control feeding and digestion in insects. We describe the discovery and functional role in these processes for insect allatoregulatory peptides, diuretic hormones, FMRFamide-related peptides, (short) neuropeptide F, proctolin, saliva production stimulating peptides, kinins, and tachykinins. These peptides control either gut myoactivity, food intake, and (or) release of digestive enzymes. Some peptides exert their action at multiple levels, possibly having a biological function that depends on their site of delivery. Many regulatory peptides have been physically extracted from different insect species. However, multiple peptidomics, proteomics, transcriptomics, and genome sequencing projects have led to increased discovery and prediction of peptide (precursor) and receptor sequences. In combination with physiological experiments, these large-scale projects have already led to important steps forward in unraveling the physiology of feeding and digestion in insects.


2009 ◽  
Vol 296 (6) ◽  
pp. H2022-H2029 ◽  
Author(s):  
Takeshi Nakamura ◽  
Hreday N. Sapru

Urocortin 1 (Ucn1) and urocortin 3 (Ucn3) are new members of the corticotrophin-releasing factor (CRF) peptide family. Ucn1 is a ligand for both the CRF type 1 receptors (CRF1Rs) and the CRF type 2 receptors (CRF2Rs), whereas Ucn3 is a high-affinity ligand for the CRF2Rs. Recently, we reported that Ucn3 microinjections into the medial nucleus tractus solitarius (mNTS) elicit decreases in mean arterial pressure (MAP) and heart rate (HR) (Nakamura T, Kawabe K, Sapru HN. Am J Physiol Heart Circ Physiol 296: H325–H332, 2009). The presence of CRF2Rs on afferent terminals has been reported in the mNTS of the rat. It was hypothesized that activation of CRF2Rs on afferent terminals in the mNTS may release glutamate, which, in turn, may elicit decreases in MAP and HR via activation of ionotropic glutamate receptors (iGLURs). This hypothesis was tested in urethane-anesthetized, artificially ventilated, adult male Wistar rats. Microinjections (100 nl) of Ucn1 (0.12 mM) into the mNTS elicited decreases in MAP and HR. The responses were partially blocked by microinjections of iGLUR antagonists into the mNTS. On the other hand, the decreases in MAP and HR elicited by microinjections of Ucn3 (0.06 mM) into the mNTS were completely blocked by microinjections of iGLUR antagonists into the mNTS. These results indicate that activation of CRF2Rs in the mNTS, by Ucn1 and Ucn3, releases glutamate, which, in turn, elicits decreases in MAP and HR via activation of iGLURs.


mSystems ◽  
2016 ◽  
Vol 1 (1) ◽  
Author(s):  
Cornelia Große ◽  
Martin Herzberg ◽  
Marcel Schüttau ◽  
Nicole Wiesemann ◽  
Gerd Hause ◽  
...  

ABSTRACT Bacteria, including pathogenic strains, need to make use of the metal composition and speciation of their environment to fulfill the requirement of the cytoplasmic metal content and composition. This task is performed by the bacterial metal transportome, composed of uptake and efflux systems. Seven interacting secondary metal uptake systems are at the core of the metal transportome in C. metallidurans. This publication verifies that posttranscriptional events are responsible for activation of even more, yet-unknown, metal import systems in the 7-fold deletion mutant Δ7. Two P-type ATPases were identified as new members of the metal uptake transportome. This publication demonstrates the complexity of the metal transportome and the regulatory processes involved. Central to the ability of Cupriavidus metallidurans to maintain its metal homoeostasis is the metal transportome, composed of uptake and efflux systems. Seven secondary metal import systems, ZupT, PitA, CorA1, CorA2, CorA3, ZntB, and HoxN, interact and are at the core of the metal uptake transportome. The 7-fold deletion mutant Δ7 (ΔzupT ΔpitA ΔcorA 1 ΔcorA 2 ΔcorA 3 ΔzntB ΔhoxN) of parent strain AE104 is still able to maintain its cellular metal content, although at the cost of reduced fitness (M. Herzberg, L. Bauer, A. Kirsten, and D. H. Nies, Metallomics, in press, http://dx.doi.org/10.1039/C5MT00295H ). Strain Δ7 does not express genes for backup importers, and so Δ7 should use metal uptake systems also produced in the AE104 parent cells. These systems should be activated in Δ7 by posttranscriptional regulatory processes. The decreased fitness of Δ7 correlated with a zinc-dependent downregulation of the overall metabolic backbone of the cells even at nontoxic external zinc concentrations. Responsible for this decreased fitness of Δ7 was a negative interference of the activity of two P-type ATPases, MgtA and MgtB, which, on the other hand, kept Δ7 at a fitness level higher than that of the Δ9 (Δ7 ΔmgtA::kan ΔmgtB) mutant strain. This revealed a complicated interplay of the metal uptake transportome of C. metallidurans, which is composed of the seven secondary uptake systems, MgtA, MgtB, and yet-unknown components, with cytoplasmic transition metal pools and posttranscriptional regulatory processes. IMPORTANCE Bacteria, including pathogenic strains, need to make use of the metal composition and speciation of their environment to fulfill the requirement of the cytoplasmic metal content and composition. This task is performed by the bacterial metal transportome, composed of uptake and efflux systems. Seven interacting secondary metal uptake systems are at the core of the metal transportome in C. metallidurans. This publication verifies that posttranscriptional events are responsible for activation of even more, yet-unknown, metal import systems in the 7-fold deletion mutant Δ7. Two P-type ATPases were identified as new members of the metal uptake transportome. This publication demonstrates the complexity of the metal transportome and the regulatory processes involved.


2020 ◽  
Vol 8 ◽  
Author(s):  
Nicholas G. Welch ◽  
Wenyi Li ◽  
Mohammed Akhter Hossain ◽  
Frances Separovic ◽  
Neil M. O'Brien-Simpson ◽  
...  

As we rapidly approach a post-antibiotic era in which multi-drug resistant bacteria are ever-pervasive, antimicrobial peptides (AMPs) represent a promising class of compounds to help address this global issue. AMPs are best-known for their membrane-disruptive mode of action leading to bacteria cell lysis and death. However, many AMPs are also known to be non-lytic and have intracellular modes of action. Proline-rich AMPs (PrAMPs) are one such class, that are generally membrane permeable and inhibit protein synthesis leading to a bactericidal outcome. PrAMPs are highly effective against Gram-negative bacteria and yet show very low toxicity against eukaryotic cells. Here, we review both the PrAMP family and the past and current definitions for this class of peptides. Computational analysis of known AMPs within the DRAMP database (http://dramp.cpu-bioinfor.org/) and assessment of their PrAMP-like properties have led us to develop a revised definition of the PrAMP class. As a result, we subsequently identified a number of unknown and unclassified peptides containing motifs of striking similarity to known PrAMP-based DnaK inhibitors and propose a series of new sequences for experimental evaluation and subsequent addition to the PrAMP family.


2012 ◽  
Vol 90 (4) ◽  
pp. 476-488 ◽  
Author(s):  
Dick R. Nässel

Insulin-like peptide signaling regulates development, growth, reproduction, metabolism, stress resistance, and life span in a wide spectrum of animals. Not only the peptides, but also their tyrosine kinase receptors and the downstream signaling pathways are conserved over evolution. This review summarizes roles of insulin-like peptides (DILPs) in physiology and behavior of Drosophila melanogaster Meigen, 1830. Seven DILPs (DILP1–7) and one receptor (dInR) have been identified in Drosophila. These DILPs display cell and stage specific expression patterns. In the adult, DILP2, 3, and 5 are expressed in insulin-producing cells (IPCs) among the median neurosecretory cells of the brain, DILP7 in 20 neurons of the abdominal ganglion, and DILP6 in the fat body. The DILPs of the IPCs regulate starvation resistance, responses to oxidative and temperature stress, and carbohydrate and lipid metabolism. Furthermore, the IPCs seem to regulate feeding, locomotor activity, sleep and ethanol sensitivity, but the mechanisms are not elucidated. Insulin also alters the sensitivity in the olfactory system that affects food search behavior, and regulates peptidergic neurons that control aspects of feeding behavior. Finally, the control of insulin production and release by humoral and neuronal factors is discussed. This includes a fat body derived factor and the neurotransmitters GABA, serotonin, octopamine, and two neuropeptides.


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