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Stimulus‐dependent regulation and cellular expression of genes encoding neuropeptides, prohormone convertases, α‐amidating enzyme and 7B2 in identified Lymnaea neurons
Author(s) -
Spijker Sabine,
SharpBaker Hilary E.,
Geraerts Wijnand P. M.,
Van Minnen Jan,
Smit August B.
Publication year - 2004
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2004.02484.x
Subject(s) - prohormone , neuropeptide , biology , prohormone convertase , enzyme , biochemistry , gene expression , microbiology and biotechnology , gene , hormone , receptor
Synthesis of bioactive peptides is regulated by several post‐translational processing events, including cleavage of peptides from a prohormone, and chemical modifications. Using quantitative in situ hybridization and neuron‐specific macro‐arrays, we first demonstrated cell‐type specific expression levels of transcripts encoding prohormone convertases, peptide α‐amidating enzyme as well as the chaperone 7B2 in Lymnaea neurons. Second, we demonstrated a strict correlation between α‐amidating enzyme and its neuropeptide substrates. However, this strict relationship of gene expression of the three prohormone convertases and types of cleavage site used is not present. Third, we showed by a physiological stimulus, i.e. clean water, which leads to a stereotyped egg‐laying behaviour resulting in successful egg‐mass deposition, the co‐regulated induction of transcript levels of processing enzymes, 7B2, and egg‐laying hormone. These data indicate that (i) these enzymes (and chaperone) are involved in egg‐laying hormone neuropeptide biosynthesis, and (ii) neuropeptide release and transcript levels of both prohormones and processing enzymes are regulated in accordance with physiological demands.