Mass spectrometric evidence for neuropeptide-amidating enzymes in Caenorhabditis elegans

The Journal of Biological Chemistry
Sven Van BaelLiesbet Temmerman

Abstract

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 Caenorhabditis 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 carboxyl-terminal 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 WT animals with those in newly generated mutants for these putative amidation enzymes. We report that mutants lacking both a functional peptidylglycine α-hydroxylating monooxygenase and a peptidylglycine α-amidating monooxygenase had a sever...Continue Reading

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Dec 24, 2018·Expert Review of Proteomics·Samantha Louise EdwardsLiliane Schoofs
Feb 8, 2019·Frontiers in Neural Circuits·Erik SvenssonHelgi B Schiöth
Sep 25, 2021·Mass Spectrometry Reviews·Ashley PhetsanthadLingjun Li

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