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      The discovery of novel neuropeptides takes flight

      review-article
      Author(s): 1 ,
      Publication date (Electronic):
      Journal: Genome Biology
      Publisher: BioMed Central

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          Abstract

          Recent studies have used nanoscale chromatography and mass spectrometry to determine the structures of novel neuropeptides in rat and Drosophila. The results shed light on neuropeptide synthesis and function(s) in both vertebrates and insects.

          Abstract

          Structural data are critical for the elucidation of how peptides are synthesized and how they function. Two recent studies have used nanoscale chromatography together with mass spectrometry to determine the structures of novel neuropeptides in rat and Drosophila. The results shed light on neuropeptide synthesis and function(s) in both vertebrates and insects.

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          Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study.

          Odile van den Heuvel, Sabrina Joseph, Christopher J Hoffmann … (1998)
          We have developed an approach based on a differential mass spectrometric analysis to detect molecules induced during the immune response of Drosophila, regardless of their biological activities. For this, we have applied directly matrix-assisted laser desorption/ionization MS to hemolymph samples from individual flies before and after an immune challenge. This method provided precise information on the molecular masses of immune-induced molecules and allowed the detection, in the molecular range of 1.5-11 kDa, of 24 Drosophila immune-induced molecules (DIMs). These molecules are all peptides, and four correspond to already characterized antimicrobial peptides. We have further analyzed the induction of the various peptides by immune challenge in wild-type flies and in mutants with a compromised antimicrobial response. We also describe a methodology combining matrix-assisted laser desorption ionization time-of-flight MS, HPLC, and Edman degradation, which yielded the peptide sequence of three of the DIMs. Finally, molecular cloning and Northern blot analyses revealed that one of the DIMs is produced as a prepropeptide and is inducible on a bacterial challenge.
          Article 0 comments Cited 40 times – based on 0 reviews     Review now
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            A neuroproteomic approach to targeting neuropeptides in the brain.

            Karl Sköld, J Aström, Marcus Svensson-Frej … (2002)
            A novel universal neuropeptide display approach in the mass range of 300-5000 Da was developed to complement two-dimensional gel electrophoresis in the analysis of peptides and small proteins from brain tissue samples. For the analysis of neuropeptides we utilized on-line nanoscale capillary reversed phase liquid chromatography and electrospray ionization quadrupole-time of flight mass spectrometry. The method was employed for the analysis of a large number of peptides from three specific rat brain regions. Approximately 1500 peptides from each brain region were detected in the same analysis. Several of these peptides were sequenced using collision-induced dissociation and identified by database search tools. In addition, a method for comparing peptide elution profiles between samples was developed, to provide two- and three-dimensional computer graphics of the profiles and to pinpoint differences for statistical measurements. Among the characterized peptides were fragments from proteins such as hemoglobin, alpha-synuclein, stathmin, cyclophilin, actin, NADH dehydrogenase, cytochrome c oxidase and prosomatostatin, as well as the bioactive neuropeptides W-hemorphin-4, and LW-hemorphin-7. The present study showed that the combination of nanoscale reversed phase liquid chromatography and high-resolution tandem mass spectrometry provides a novel and powerful approach to investigate a large number of peptides and protein fragments in the brain.
            Article 0 comments Cited 7 times – based on 0 reviews     Review now
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              Isolation and expression of the Drosophila drosulfakinin neural peptide gene product, DSK-I.

              R. Nichols (1992)
              The Drosophila drosulfakinin (dsk) gene encodes the cholecystokinin homologues drosulfakinin-I (DSK-I) and drosulfakinin-II (DSK-II). The naturally occurring DSKI peptide was isolated from an extract of adult flies and its sequence determined by automated Edman degradation and sequence-specific radioimmunoassay. The dsk cDNA is expressed during the larval, pupal, and adult stages of development and is an abundant adult head transcript. Sequence-specific DSK antibodies localized DSK expression in the Drosophila larval central nervous system to medial neurosecretory cells and projections that extend from the neurons anteriorly into the brain and posteriorly down the ventral ganglion. The availability of the dsk transcript, sequence-specific DSK antibodies and the application of molecular genetics provide the opportunity to elucidate the role(s) of Drosophila CCK homologues in brain structure and function.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Genome Biol
                Title: Genome Biology
                Publisher: BioMed Central (London )
                ISSN (Print): 1465-6906
                ISSN (Electronic): 1465-6914
                Publication date (Print): 2002
                Publication date (Electronic): 28 October 2002
                Volume: 3
                Issue: 11
                Pages: reviews1032.1-reviews1032.2
                Affiliations
                [1 ]Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109-0606, USA
                Article
                Publisher ID: gb-2002-3-11-reviews1032
                DOI: 10.1186/gb-2002-3-11-reviews1032
                PMC ID: 244922
                PubMed ID: 12429066
                SO-VID: eab0fef9-8918-4cab-a44a-70c6e7de4f41
                Copyright © Copyright © 2002 BioMed Central Ltd
                History
                Categories
                Subject: Minireview

                ScienceOpen disciplines: Genetics
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                ScienceOpen disciplines: Genetics

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