| | Altered neuropeptide profile of Caenorhabditis elegans lacking the chaperone protein 7B2 as analyzed by mass spectrometryEdited by Christian Griesinger Received 11 January 2007; received in revised form 18 July 2007; accepted 6 August 2007. published online 14 August 2007. Abstract Cellular synthesis of naturally occurring, bioactive peptides requires the proprotein convertase PC2/EGL-3 for cleavage from the larger peptide precursors. A neuroendocrine chaperone 7B2 is needed for the proteolytical activation of proPC2, as extensively studied in mouse models. To determine the role of its orthologue in Caenorhabditis elegans, we analyzed wild-type and 7B2-null strains by HPLC and matrix-assisted laser desorption ionization time-of-flight mass spectrometry, which allowed the identification of a novel neuropeptide gene, flp-33. The presence and/or absence of some neuropeptides in 7B2-null animals strongly differs form the peptide profile in wild-type, suggesting a specific and determined action of 7B2 in C. elegans. Abbreviations: Da, Dalton, flp, FMRF amide-like peptide, m/z, mass-to-charge ratio, MALDI-TOF MS, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, MS/MS, tandem mass spectrometry, nlp, neuropeptide-like protein, PC, proprotein convertase, sbt-1, seven-B-two-1 Functional Genomics and Proteomics, Department of Biology, Katholieke Universiteit Leuven, Naamsestraat 59, B-3000 Leuven, Belgium  Corresponding author. Fax: +32 16323902.
PII: S0014-5793(07)00868-X doi:10.1016/j.febslet.2007.08.003 © 2007 Federation of European Biochemical Societies | |
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ABSTRACT
