title: Altered neuropeptide profile of Caenorhabditis elegans lacking the chaperone protein 7B2 as analyzed by mass spectrometry.
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.
authors: Functional Genomics and Proteomics, Department of Biology, Katholieke Universiteit Leuven, Naamsestraat 59, B-3000 Leuven, Belgium. Steven.husson@bio.kuleuven.be
authors: Steven J
authors: SJ
authors: Husson
authors: Liliane
authors: L
authors: Schoofs
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000235:genetics / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D017238:Genes, Helminth; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D051859:Neuroendocrine Secretory Protein 7B2 / Q000737:chemistry / Q000172:deficiency* / Q000235:genetics; D009479:Neuropeptides / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D051859:Neuroendocrine Secretory Protein 7B2; D009479:Neuropeptides