A proteomic approach to neuropeptide function elucidation

Temmerman, L., Bogaerts, A., Meelkop, E., Cardoen, D., Boerjan, B., Janssen, T. and Schoofs, L. (2012) A proteomic approach to neuropeptide function elucidation. Peptides, 34 1: 3-9. doi:10.1016/j.peptides.2011.08.025

Author Temmerman, L.
Bogaerts, A.
Meelkop, E.
Cardoen, D.
Boerjan, B.
Janssen, T.
Schoofs, L.
Title A proteomic approach to neuropeptide function elucidation
Journal name Peptides   Check publisher's open access policy
ISSN 0196-9781
Publication date 2012-03
Year available 2011
Sub-type Article (original research)
DOI 10.1016/j.peptides.2011.08.025
Volume 34
Issue 1
Start page 3
End page 9
Total pages 7
Place of publication Philadelphia, PA, United States
Publisher Elsevier
Collection year 2013
Language eng
Formatted abstract
Many of the diverse functions of neuropeptides are still elusive. As they are ideally suited to modulate traditional signaling, their added actions are not always detectable under standard laboratory conditions. The search for function assignment to peptide encoding genes can therefore greatly benefit from molecular information. Specific molecular changes resulting from neuropeptide signaling may direct researchers to yet unknown processes or conditions, for which studying these signaling systems may eventually lead to phenotypic confirmation. Here, we applied gel-based proteomics after pdf-1 neuropeptide gene knockout in the model organism Caenorhabditis elegans. It has previously been described that pdf-1 null mutants display a locomotion defect, being slower and making more turns and reversals than wild type worms. The vertebrate functional homolog of PDF-1, vasocative intestinal peptide (VIP), is known to influence a plethora of processes, which have so far not been investigated for pdf-1. Because proteins represent the actual effectors inside an organism, proteomic analysis can guide our view to novel pdf-1 actions in the nematode worm. Our data show that knocking out pdf-1 results in alteration of levels of proteins involved in fat metabolism, stress resistance and development. This indicates a possible conservation of VIP-like actions for pdf-1 in C. elegans.
Keyword Caenorhabditis elegans
Pigment dispersing factor
Functional neurobiology
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status Non-UQ
Additional Notes Published online 6 September 2011

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
Queensland Brain Institute Publications
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