4.5 Article

Altered neuropeptide profile of Caenorhabditis elegans lacking the chaperone protein 7B2 as analyzed by mass spectrometry

Journal

FEBS LETTERS
Volume 581, Issue 22, Pages 4288-4292

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.08.003

Keywords

neuropeptide; peptidomics; mass spectrometry; MALDI-TOF MS; FLP; NLP

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Cellular synthesis of naturally occurring, bioactive peptides requires the proprotein convertase PC2/EGL-3 for cleavage from the larger peptide precursors. A neuroendocrine chaperone 7132 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 7132-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 7132-null animals strongly differs form the peptide profile in wild-type, suggesting a specific and determined action of 7132 in C. elegans. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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