Peptidomics of CNS‐associated neurohemal systems of adult Drosophila melanogaster: A mass spectrometric survey of peptides from individual flies

Abstract

Neuropeptides are important messenger molecules that influence nearly all physiological processes. In insects, they can be released as neuromodulators within the central nervous system (CNS) or as neurohormones into the hemolymph. We analyzed the peptidome of neurohormonal release sites and associated secretory peptidergic neurons of adult Drosophila melanogaster. MALDI-TOF mass spectrometric analyzes were performed on single organs or cell cluster from individual flies. This first peptidomic characterization in adult fruit flies revealed 32 different neuropeptides. Peptides not directly predictable from previously cloned or annotated precursor genes were sequenced by tandem mass spectrometry. These peptides turned out to be either intermediate products of neuropeptide processing or shorter versions of known peptides. We found that the peptidome of the CNS-associated neurohemal organs is tagma-specific in Drosophila. Abdominal neurohemal organs and their supplying peptidergic neurons contain the capa gene products periviscerokinins and pyrokinin-1, thoracic neurohemal organs contain FMRFamides, and the neurohemal release sites of the brain contain pyrokinin-1(2-15), pyrokinin-2, corazonin, myosuppressin, and sNPF as their major putative release products. Our results show that peptidomic approaches are well suited to study differential neuropeptide expression or posttranslational modifications in morphologically defined parts of the nervous system and in a developmental and physiological context in animals as small as Drosophila melanogaster.

Peptidomics of Neuropeptidergic Tissues of the Tsetse FlyGlossina morsitans morsitans

“…In accordance with this finding, it has been shown that AKH peptides are present in the brain and in neuronal projections innervating the midgut in mosquitoes [24,28]. In several peptidomics studies on D. melanogaster, the signal of mature AKH was very weak [29,30], whereas intermediate AKH peptides were clearly detected [31]. The same was found in the Australian sheep blowfly Lucilia cuprina, and the anautogenous flesh fly Sarcophaga crassipalpis [25].…”

Processed short neuropeptide F peptides regulate growth through the ERK‐insulin pathway in Drosophila melanogaster

“…Body sizes of the The Western blot analysis with phospho-ERK in Drosophila BG2-c6 cells shows that sNPF1 and sNPF2 peptide treatments increased the activation of ERK compared to those of the non-treated and the sNPF2 [1][2][3][4][5][6][7][8][9][10] peptide treated controls. However, sNPF3 and sNPF4 peptide treatments did not increase ERK activation.…”

“…2A). However, in previous mass spectrometry studies using larval and adult tissues, AQRSPSLRLRFa (sNPF1), SPSLRLRFa (sNPF2 [12][13][14][15][16][17][18][19] ), SDPDMLNSIVE (sNPF-AP-1), WFGDVNQKPI (sNPF2 [1][2][3][4][5][6][7][8][9][10] ), SPSLRLRFa (sNPF2 [12][13][14][15][16][17][18][19] ) peptides are found [7][8][9]. PQRLRWa (sNPF3) and PMRLRWa (sNPF4) are also identified in adult body extract [10,11].…”

Comparative Neuroanatomy and Genomics ofhuginand Pheromone Biosynthesis Activating Neuropeptide (PBAN)

“…13 Furthermore, hugin-PK, but not hugin-gamma, was found in the corpora cardiaca/ring gland of D. melanogaster 14,15 and other Drosophila species. 16 What is the explanation for not finding hugin-gamma?…”

“…In this respect, hugin may be part of a neuronal circuit involved not only in making a decision between feeding and not feeding, but also in making perhaps an even tougher decision: between feeding and mating. Chemically identified peptides [14][15][16][26][27][28] are boxed in red, the PRXa C-termini are boxed in blue. Peptide designations (see Roman numbers) refer to common peptide designations from M. sexta, H. zea, and D. melanogaster.…”