Molecular Cloning of Three Distinct cDNAs, Each Encoding a Different Adipokinetic Hormone Precursor, of the Migratory Locust, Locusta migratoria

Bogerd, Jan; Kooiman, Frank P.; Pijnenburg, M. A. P.; Hekking, Liesbeth H P; Oudejans, R.C.H.M.; Horst, Dick J. Van der

doi:10.1074/jbc.270.39.23038

Cited by 82 publications

(40 citation statements)

References 31 publications

(27 reference statements)

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“…Adipokinetic hormones (AKH) regulate the release of lipid and carbohydrate energy substrates during flight. Drosophila AKH (13) is encoded by the Akh gene, which is structurally similar to the three AKH genes in the locust, Locusta migratoria (14). Although the level of AKH expression in the corpora cardiaca of locusts is extremely high (6, 15), we observed only a weak Drm-AKH signal.…”

Section: Resultsmentioning

confidence: 39%

Peptidomics of the Larval Drosophila melanogasterCentral Nervous System

Baggerman

Cerstiaens

Loof

et al. 2002

Journal of Biological Chemistry

254

208

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Neuropeptides regulate most, if not all, biological processes in the animal kingdom, but only seven have been isolated and sequenced from Drosophila melanogaster. In analogy with the proteomics technology, where all proteins expressed in a cell or tissue are analyzed, the peptidomics approach aims at the simultaneous identification of the whole peptidome of a cell or tissue, i.e. all expressed peptides with their posttranslational modifications. Using nanoscale liquid chromatography combined with tandem mass spectrometry and data base mining, we analyzed the peptidome of the larval Drosophila central nervous system at the amino acid sequence level. We were able to provide biochemical evidence for the presence of 28 neuropeptides using an extract of only 50 larval Drosophila central nervous systems. Eighteen of these peptides are encoded in previously cloned or annotated precursor genes, although not all of them were predicted correctly. Eleven of these peptides were never purified before. Eight other peptides are entirely novel and are encoded in five different, not yet annotated genes. This neuropeptide expression profiling study also opens perspectives for other eukaryotic model systems, for which genome projects are completed or in progress.The most common approach in proteomic studies is to separate and visualize as many proteins as possible of an organism, tissue, or cell, by two-dimensional electrophoresis and to subsequently identify differentially expressed proteins by mass spectrometric techniques. One of the major constraints of this technology is that proteins of a molecular mass lower than 10 kDa are generally not retained and overlooked in most of the proteomic studies. Nevertheless this mass region contains a group of very important proteins, the peptide hormones and neurotransmitters.To date, many neuropeptides have been purified from vertebrate and invertebrate sources. Peptide physiology in the pregenomic era (before the realization of the genome projects) was time-consuming as a peptide present in tissue extracts had to be purified to homogeneity prior to sequencing, synthesis, and functional analysis.Drosophila is an outstanding model system for the molecular genetics and developmental biology in higher eukaryotes. Yet, its molecular endocrinology is poorly documented because only seven neuropeptides have been identified by traditional purification. Recently, a milestone was reached with the completion of the Drosophila genome project (1). Through the BLAST program, one can screen the genome of an organism for candidate-neuropeptides based on sequence homology with known neuropeptides from other organisms. In this way, 31 (neuro)peptide genes were found in Drosophila melanogaster (2-5). These findings, however, give no information on the temporal and spatial expression nor on the physiological relevance of these (neuro)peptide genes. Often, the precursors of biologically active peptides encode several peptides. In general, these peptides can be predicted from the precursor gene as it is assume...

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Section: Resultsmentioning

confidence: 39%

Peptidomics of the Larval Drosophila melanogasterCentral Nervous System

Baggerman

Cerstiaens

Loof

et al. 2002

Journal of Biological Chemistry

254

208

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“…Because of such dissimilarities, biological activities (if any) of the associated peptide are a matter of conjecture. Nevertheless, a similar tendency was also observed in members of other neuropeptide families (e.g., Bogerd et al, 1995;Park and Hall, 1998). In the case of adipokinetic hormone (AKH) precursors, the AKH-associated peptide domain is important for the formation of precursor dimers, which are subsequently processed to produce bioactive AKHs in locusts (O'Shea and Rayne, 1992).…”

Section: Comparative Analyses Of Corazonin Precursorsmentioning

confidence: 69%

Comparative analysis ofCorazonin‐encoding genes (Crz's) inDrosophilaspecies and functional insights intoCrz‐expressing neurons

Choi

Lee

Hall

et al. 2005

J of Comparative Neurology

108

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To gain insight into regulatory mechanisms of tissue-specific Corazonin (Crz) gene expression and its functions in Drosophila, we cloned the Crz genes from four Drosophila species (D. melanogaster, D. simulans, D. erecta, and D. virilis) and performed comparative analyses of Crz gene sequences and expression patterns using in situ hybridization and immunohistochemistry. Although Crz gene sequences showed a great deal of diversity, its expression patterns in the CNS were highly conserved in the Drosophila species examined here. In D. melanogaster larva, Crz expression was found in four pairs of neurons per cerebral lobe and in eight pairs of bilateral neurons in the ventral nerve cord; in adult, the number of Crz-producing neurons increased to 6-8 in the pars lateralis of each brain lobe, whereas neurons in the ventral nerve cord were no longer detectable. Crz transcripts were also found in the optic lobes; however, these mRNAs do not seem to be translated. Such adult-like Crz expression patterns were established within 48 hours after pupation. Somata of Crz-neurons in the pars lateralis are located in the vicinity of terminals emanating from PDF-containing pacemaking neurons, indicating a functional connection between the two peptidergic nervous systems. A subset of Crz neurons coexpressed the period clock gene; however, normal Crz transcription was unaffected by central clockworks. Two pairs of ectopic Crz cells were detected in the adult brains of behaviorally arrhythmic Clock(Jrk) or cycle(02) mutants, suggesting that CLOCK and CYCLE proteins negatively regulate Crz transcription in a cell-specific manner.

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“…In locusts, all 3 prohormones present form homodimeric precursors but only the AKH-III prohormone has 2 Cys residues (28,29). This locust AKH-III prohormone, in contrast to locust AKH-I and AKH-II prohormones (which have only a single cysteine residue), resembles best the other insect AKH prohormones and all other protostomian AKH-GnRH prohormones, which also contain 2 cysteines (Fig.…”

Section: Discussionmentioning

confidence: 98%

Adipokinetic hormone signaling through the gonadotropin-releasing hormone receptor modulates egg-laying in Caenorhabditis elegans

Lindemans

Liu

Janssen

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

140

136

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In mammals, hypothalamic gonadotropin-releasing hormone (GnRH) is a neuropeptide that stimulates the release of gonadotropins from the anterior pituitary. The existence of a putative functional equivalent of this reproduction axis in protostomian invertebrates has been a matter of debate. In this study, the ligand for the GnRH receptor in the nematode Caenorhabditis elegans (Ce-GnRHR) was found using a bioinformatics approach. The peptide and its precursor are reminiscent of both insect adipokinetic hormones and GnRH-preprohormone precursors from tunicates and higher vertebrates. We cloned the AKH-GnRH-like preprohormone and the Ce-GnRHR and expressed the GPCR in HEK293T cells. The GnRHR was activated by the C. elegans AKH-GnRH-like peptide (EC50 ‫؍‬ 150 nM) and by Drosophila AKH and other nematode AKH-GnRHs that we found in EST databases. Analogous to both insect AKH receptor and vertebrate GnRH receptor signaling, Ce-AKH-GnRH activated its receptor through a G␣q protein with Ca 2؉ as a second messenger. Gene silencing of Ce-GnRHR, Ce-AKHGnRH, or both resulted in a delay in the egg-laying process, comparable to a delay in puberty in mammals lacking a normal dose of GnRH peptide or with a mutated GnRH precursor or receptor gene. The present data support the view that the AKH-GnRH signaling system probably arose very early in metazoan evolution and that its role in reproduction might have been developed before the divergence of protostomians and deuterostomians.C. elegans ͉ G protein-coupled receptor ͉ molecular evolution ͉ neuropeptide ͉ neuroendocrinology

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Molecular Cloning of Three Distinct cDNAs, Each Encoding a Different Adipokinetic Hormone Precursor, of the Migratory Locust, Locusta migratoria

Cited by 82 publications

References 31 publications

Peptidomics of the Larval Drosophila melanogasterCentral Nervous System

Peptidomics of the Larval Drosophila melanogasterCentral Nervous System

Comparative analysis ofCorazonin‐encoding genes (Crz's) inDrosophilaspecies and functional insights intoCrz‐expressing neurons

Adipokinetic hormone signaling through the gonadotropin-releasing hormone receptor modulates egg-laying in Caenorhabditis elegans

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