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DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2018-03-12
  • AnnouncementXML: Submission_2018-03-12_03:41:36.xml
  • DigitalObjectIdentifier: http://dx.doi.org/10.6019/PXD008942
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Supported dataset by repository
  • PrimarySubmitter: Sven Van Bael
  • Title: Mass spectrometric evidence for neuropeptide-amidating enzymes in C. elegans
  • Description: Neuropeptides constitute a vast and functionally diverse family of neurochemical signaling molecules, and are widely involved in the regulation of various physiological processes. The nematode C. elegans is well-suited for the study of neuropeptide biochemistry and function, as neuropeptide biosynthesis enzymes are not essential for C. elegans viability. This permits the study of neuropeptide biosynthesis in mutants lacking certain neuropeptide-processing enzymes. Mass spectrometry has been used to study the effects of proprotein convertase and carboxypeptidase mutations on proteolytic processing of neuropeptide precursors and on the peptidome in C. elegans. However, the enzymes required for the last step in the production of many bioactive peptides – the carboxyterminal amidation reaction – have not been characterized in this manner. Here, we describe three genes that encode homologs of neuropeptide amidation enzymes in C. elegans and used tandem LC-MS to compare neuropeptides in wild-type animals with those in newly generated mutants for these putative amidation enzymes. We report that mutants lacking both a functional peptidylglycine α-hydroxylating monooxygenase (PHM) and a peptidylglycine α-amidating monooxygenase (PAM) had a severely altered neuropeptide profile and also a decreased number of offspring. Interestingly, single mutants of the amidation enzymes still expressed some fully processed amidated neuropeptides, indicating the existence of a redundant amidation mechanism in C. elegans. In summary, the key steps in neuropeptide-processing in C. elegans seem to be executed by redundant enzymes, and loss of these enzymes severely affects brood size, supporting the need of amidated peptides for C. elegans reproduction.
  • SpeciesList: scientific name: Caenorhabditis elegans; NCBI TaxID: 6239;
  • ModificationList: Phospho; Amidated; Glu->pyro-Glu; Oxidation; Gln->pyro-Glu
  • Instrument: Q Exactive

Dataset History

VersionDatetimeStatusChangeLog Entry
02018-02-13 01:57:54ID requested
12018-03-12 03:41:37announced

Publication List

  1. Van Bael S, Watteyne J, Boonen K, De Haes W, Menschaert G, Ringstad N, Horvitz HR, Schoofs L, Husson SJ, Temmerman L, . J Biol Chem, 293(16):6052-6063(2018) [pubmed]

Keyword List

  1. curator keyword: Biological
  2. submitter keyword: Peptidomics
  3. mass spectrometry
  4. neuropeptide
  5. amidation
  6. copper monooxygenase
  7. PHM
  8. PAL
  9. PAM
  10. Caenorhabditis elegans
  11. LC-orbitrap MS

Contact List

    Liesbet Temmerman
    • contact affiliation: Department of Biology KU Leuven (University of Leuven) Belgium
    • contact email: Liesbet.Temmerman@kuleuven.be
    • lab head:
    Sven Van Bael
    • contact affiliation: KU Leuven
    • contact email: sven.vanbael@kuleuven.be
    • dataset submitter:

Full Dataset Link List

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